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* Residue conservation analysis
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PDB id:
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Ligase, cell cycle
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Title:
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Crystal structure of scskp1-sccdc4-cpd peptide complex
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Structure:
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Centromere DNA-binding protein complex cbf3 subunit d. Chain: a, c. Fragment: residues 36-63 deleted. Synonym: scskp1, suppressor of kinetochore protein 1. Engineered: yes. Cdc4 protein. Chain: b, d. Fragment: residues 601-604 and 609-624 deleted.
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: cbf3d or skp1 or ydr328c or d9798.14. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Biol. unit:
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Trimer (from
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Resolution:
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2.70Å
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R-factor:
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0.239
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R-free:
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0.273
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Authors:
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S.Orlicky,X.Tang,A.Willems,M.Tyers,F.Sicheri
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Key ref:
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S.Orlicky
et al.
(2003).
Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase.
Cell,
112,
243-256.
PubMed id:
DOI:
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Date:
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12-Dec-02
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Release date:
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18-Feb-03
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PROCHECK
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Headers
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References
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Gene Ontology (GO) functional annotation
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Biological process
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ubiquitin-dependent protein catabolic process
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1 term
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Biochemical function
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protein binding
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1 term
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DOI no:
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Cell
112:243-256
(2003)
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PubMed id:
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Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase.
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S.Orlicky,
X.Tang,
A.Willems,
M.Tyers,
F.Sicheri.
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ABSTRACT
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Cell cycle progression depends on precise elimination of cyclins and
cyclin-dependent kinase (CDK) inhibitors by the ubiquitin system. Elimination of
the CDK inhibitor Sic1 by the SCFCdc4 ubiquitin ligase at the onset of S phase
requires phosphorylation of Sic1 on at least six of its nine Cdc4-phosphodegron
(CPD) sites. A 2.7 A X-ray crystal structure of a Skp1-Cdc4 complex bound to a
high-affinity CPD phosphopeptide from human cyclin E reveals a core CPD motif,
Leu-Leu-pThr-Pro, bound to an eight-bladed WD40 propeller domain in Cdc4. The
low affinity of each CPD motif in Sic1 reflects structural discordance with one
or more elements of the Cdc4 binding site. Reengineering of Cdc4 to reduce
selection against Sic1 sequences allows ubiquitination of lower phosphorylated
forms of Sic1. These features account for the observed phosphorylation threshold
in Sic1 recognition and suggest an equilibrium binding mode between a single
receptor site in Cdc4 and multiple low-affinity CPD sites in Sic1.
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Selected figure(s)
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Figure 3.
Figure 3. Substrate Orientation within the Skp1-Cdc4-CPD
Complex(A) Comparison of the ScSkp1-ScCdc4-CPD complex and the
hSkp1-hSkp2 complex. Complexes were superimposed through a least
squares optimization of Skp1 β strands 1 to 3 and α helices 1
to 6 (RMSD Cα = 0.74Å). Skp1 and F box secondary
structure elements that deviate significantly in size and
position between the two structures are labeled.(B) Model of the
ubiquitin-E2-SCF^Cdc4-CPD complex. The arrow indicates the 59
Å distance separating the phosphate group of the CPD and
the active site cysteine of the E2.
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Figure 4.
Figure 4. The CPD Binding Pocket of the WD40 Domain(A)
Surface representation of the CPD binding pocket, indicating
invariant and highly conserved residues. Basic (blue),
hydrophobic (green), and small polar residues (orange) are
shown. The bound CPD is in ball and stick representation with
carbon (white), nitrogen (blue), oxygen (red), and phosphorous
(yellow) atoms shown.(B) Surface representation of CPD binding
region indicating electrostatic potential. Blue and red indicate
regions of positive and negative potential, respectively, over
the range 10 to −10 k[B]T.(C) Stereo ribbons representation of
side chains and molecular interactions in the CPD binding
pocket. Highly conserved and invariant side chains of Cdc4 and
the CPD are displayed in ball and stick representation. Sites of
mutation that give rise to severe and intermediate loss of
function (see Figure 5) are colored red and blue, respectively;
nonessential residues are colored green.(D) Schematic of CPD
binding pocket interactions with the CPD peptide.
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2003,
112,
243-256)
copyright 2003.
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Figures were
selected
by the author.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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A.Saha,
S.Lewis,
G.Kleiger,
B.Kuhlman,
and
R.J.Deshaies
(2011).
Essential role for ubiquitin-ubiquitin-conjugating enzyme interaction in ubiquitin discharge from Cdc34 to substrate.
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Mol Cell, 42,
75-83.
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C.Xu,
and
J.Min
(2011).
Structure and function of WD40 domain proteins.
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Protein Cell, 2,
202-214.
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PDB codes:
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D.M.Duda,
D.C.Scott,
M.F.Calabrese,
E.S.Zimmerman,
N.Zheng,
and
B.A.Schulman
(2011).
Structural regulation of cullin-RING ubiquitin ligase complexes.
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Curr Opin Struct Biol, 21,
257-264.
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|
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S.Marjan Varedi K,
P.J.Woolf,
and
X.N.Lin
(2011).
Minimum protein oscillator based on multisite phosphorylation∕dephosphorylation.
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IET Syst Biol, 5,
27.
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Z.Hua,
and
R.D.Vierstra
(2011).
The cullin-RING ubiquitin-protein ligases.
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Annu Rev Plant Biol, 62,
299-334.
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A.Y.Hung,
C.C.Sung,
I.L.Brito,
and
M.Sheng
(2010).
Degradation of postsynaptic scaffold GKAP and regulation of dendritic spine morphology by the TRIM3 ubiquitin ligase in rat hippocampal neurons.
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PLoS One, 5,
e9842.
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C.Stark,
T.C.Su,
A.Breitkreutz,
P.Lourenco,
M.Dahabieh,
B.J.Breitkreutz,
M.Tyers,
and
I.Sadowski
(2010).
PhosphoGRID: a database of experimentally verified in vivo protein phosphorylation sites from the budding yeast Saccharomyces cerevisiae.
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Database (Oxford), 2010,
bap026.
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C.U.Stirnimann,
E.Petsalaki,
R.B.Russell,
and
C.W.Müller
(2010).
WD40 proteins propel cellular networks.
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Trends Biochem Sci, 35,
565-574.
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C.Xu,
C.Bian,
W.Yang,
M.Galka,
H.Ouyang,
C.Chen,
W.Qiu,
H.Liu,
A.E.Jones,
F.MacKenzie,
P.Pan,
S.S.Li,
H.Wang,
and
J.Min
(2010).
Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2).
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Proc Natl Acad Sci U S A, 107,
19266-19271.
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PDB codes:
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D.C.Scott,
J.K.Monda,
C.R.Grace,
D.M.Duda,
R.W.Kriwacki,
T.Kurz,
and
B.A.Schulman
(2010).
A dual E3 mechanism for Rub1 ligation to Cdc53.
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Mol Cell, 39,
784-796.
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D.Wu,
J.E.Sylvester,
L.L.Parker,
G.Zhou,
and
S.J.Kron
(2010).
Peptide reporters of kinase activity in whole cell lysates.
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Biopolymers, 94,
475-486.
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J.A.Diehl,
and
B.Ponugoti
(2010).
Ubiquitin-dependent proteolysis in G1/S phase control and its relationship with tumor susceptibility.
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Genes Cancer, 1,
717-724.
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J.Durgan,
and
P.J.Parker
(2010).
Regulation of the tumour suppressor Fbw7α by PKC-dependent phosphorylation and cancer-associated mutations.
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Biochem J, 432,
77-87.
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J.Liu,
and
R.Nussinov
(2010).
Molecular dynamics reveal the essential role of linker motions in the function of cullin-RING E3 ligases.
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J Mol Biol, 396,
1508-1523.
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J.R.England,
J.Huang,
M.J.Jennings,
R.D.Makde,
and
S.Tan
(2010).
RCC1 uses a conformationally diverse loop region to interact with the nucleosome: a model for the RCC1-nucleosome complex.
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J Mol Biol, 398,
518-529.
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|
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|
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J.Walczak-Sztulpa,
J.Eggenschwiler,
D.Osborn,
D.A.Brown,
F.Emma,
C.Klingenberg,
R.C.Hennekam,
G.Torre,
M.Garshasbi,
A.Tzschach,
M.Szczepanska,
M.Krawczynski,
J.Zachwieja,
D.Zwolinska,
P.L.Beales,
H.H.Ropers,
A.Latos-Bielenska,
and
A.W.Kuss
(2010).
Cranioectodermal Dysplasia, Sensenbrenner syndrome, is a ciliopathy caused by mutations in the IFT122 gene.
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Am J Hum Genet, 86,
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M.Sadowski,
R.Suryadinata,
X.Lai,
J.Heierhorst,
and
B.Sarcevic
(2010).
Molecular basis for lysine specificity in the yeast ubiquitin-conjugating enzyme Cdc34.
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Mol Cell Biol, 30,
2316-2329.
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M.Z.Bao,
T.R.Shock,
and
H.D.Madhani
(2010).
Multisite phosphorylation of the Saccharomyces cerevisiae filamentous growth regulator Tec1 is required for its recognition by the E3 ubiquitin ligase adaptor Cdc4 and its subsequent destruction in vivo.
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Eukaryot Cell, 9,
31-36.
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N.Pashkova,
L.Gakhar,
S.C.Winistorfer,
L.Yu,
S.Ramaswamy,
and
R.C.Piper
(2010).
WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins.
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Mol Cell, 40,
433-443.
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PDB code:
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|
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P.Radivojac,
V.Vacic,
C.Haynes,
R.R.Cocklin,
A.Mohan,
J.W.Heyen,
M.G.Goebl,
and
L.M.Iakoucheva
(2010).
Identification, analysis, and prediction of protein ubiquitination sites.
|
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Proteins, 78,
365-380.
|
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|
|
|
|
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R.D.Makde,
J.R.England,
H.P.Yennawar,
and
S.Tan
(2010).
Structure of RCC1 chromatin factor bound to the nucleosome core particle.
|
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Nature, 467,
562-566.
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PDB code:
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R.Schweiger,
and
M.Linial
(2010).
Cooperativity within proximal phosphorylation sites is revealed from large-scale proteomics data.
|
| |
Biol Direct, 5,
6.
|
|
|
|
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S.Akhoondi,
L.Lindström,
M.Widschwendter,
M.Corcoran,
J.Bergh,
C.Spruck,
D.Grandér,
and
O.Sangfelt
(2010).
Inactivation of FBXW7/hCDC4-β expression by promoter hypermethylation is associated with favorable prognosis in primary breast cancer.
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Breast Cancer Res, 12,
R105.
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S.Orlicky,
X.Tang,
V.Neduva,
N.Elowe,
E.D.Brown,
F.Sicheri,
and
M.Tyers
(2010).
An allosteric inhibitor of substrate recognition by the SCF(Cdc4) ubiquitin ligase.
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Nat Biotechnol, 28,
733-737.
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PDB code:
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T.Mittag,
J.Marsh,
A.Grishaev,
S.Orlicky,
H.Lin,
F.Sicheri,
M.Tyers,
and
J.D.Forman-Kay
(2010).
Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase.
|
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Structure, 18,
494-506.
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X.H.Wu,
H.Zhang,
and
Y.D.Wu
(2010).
Is Asp-His-Ser/Thr-Trp tetrad hydrogen-bond network important to WD40-repeat proteins: a statistical and theoretical study.
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| |
Proteins, 78,
1186-1194.
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C.Salazar,
and
T.Höfer
(2009).
Multisite protein phosphorylation--from molecular mechanisms to kinetic models.
|
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FEBS J, 276,
3177-3198.
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G.Kleiger,
A.Saha,
S.Lewis,
B.Kuhlman,
and
R.J.Deshaies
(2009).
Rapid E2-E3 assembly and disassembly enable processive ubiquitylation of cullin-RING ubiquitin ligase substrates.
|
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Cell, 139,
957-968.
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|
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J.Liu,
and
R.Nussinov
(2009).
The mechanism of ubiquitination in the cullin-RING E3 ligase machinery: conformational control of substrate orientation.
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PLoS Comput Biol, 5,
e1000527.
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J.S.Friedman,
J.W.Ray,
N.Waseem,
K.Johnson,
M.J.Brooks,
T.Hugosson,
D.Breuer,
K.E.Branham,
D.S.Krauth,
S.J.Bowne,
L.S.Sullivan,
V.Ponjavic,
L.Gränse,
R.Khanna,
E.H.Trager,
L.M.Gieser,
D.Hughbanks-Wheaton,
R.I.Cojocaru,
N.M.Ghiasvand,
C.F.Chakarova,
M.Abrahamson,
H.H.Göring,
A.R.Webster,
D.G.Birch,
G.R.Abecasis,
Y.Fann,
S.S.Bhattacharya,
S.P.Daiger,
J.R.Heckenlively,
S.Andréasson,
and
A.Swaroop
(2009).
Mutations in a BTB-Kelch protein, KLHL7, cause autosomal-dominant retinitis pigmentosa.
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Am J Hum Genet, 84,
792-800.
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K.Corcoran,
X.Wang,
and
L.Lybarger
(2009).
Adapter-mediated substrate selection for endoplasmic reticulum-associated degradation.
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J Biol Chem, 284,
17475-17487.
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L.S.Garrenton,
A.Braunwarth,
S.Irniger,
E.Hurt,
M.Künzler,
and
J.Thorner
(2009).
Nucleus-specific and cell cycle-regulated degradation of mitogen-activated protein kinase scaffold protein Ste5 contributes to the control of signaling competence.
|
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Mol Cell Biol, 29,
582-601.
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M.Zhuang,
M.F.Calabrese,
J.Liu,
M.B.Waddell,
A.Nourse,
M.Hammel,
D.J.Miller,
H.Walden,
D.M.Duda,
S.N.Seyedin,
T.Hoggard,
J.W.Harper,
K.P.White,
and
B.A.Schulman
(2009).
Structures of SPOP-substrate complexes: insights into molecular architectures of BTB-Cul3 ubiquitin ligases.
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Mol Cell, 36,
39-50.
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PDB codes:
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N.Ito,
M.Watanabe-Matsui,
K.Igarashi,
and
K.Murayama
(2009).
Crystal structure of the Bach1 BTB domain and its regulation of homodimerization.
|
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Genes Cells, 14,
167-178.
|
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N.W.Pierce,
G.Kleiger,
S.O.Shan,
and
R.J.Deshaies
(2009).
Detection of sequential polyubiquitylation on a millisecond timescale.
|
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Nature, 462,
615-619.
|
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R.J.Deshaies,
and
C.A.Joazeiro
(2009).
RING domain E3 ubiquitin ligases.
|
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Annu Rev Biochem, 78,
399-434.
|
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S.J.Werden,
J.Lanchbury,
D.Shattuck,
C.Neff,
M.Dufford,
and
G.McFadden
(2009).
The myxoma virus m-t5 ankyrin repeat host range protein is a novel adaptor that coordinately links the cellular signaling pathways mediated by Akt and Skp1 in virus-infected cells.
|
| |
J Virol, 83,
12068-12083.
|
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S.Sonnberg,
S.B.Fleming,
and
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(2009).
A truncated two-{alpha}-helix F-box present in poxvirus ankyrin-repeat proteins is sufficient for binding the SCF1 ubiquitin ligase complex.
|
| |
J Gen Virol, 90,
1224-1228.
|
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|
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S.Wu,
and
D.A.Wolf
(2009).
Destruction of RhoA CULtivates actin.
|
| |
Mol Cell, 35,
735-736.
|
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Y.Iwatani,
D.S.Chan,
L.Liu,
H.Yoshii,
J.Shibata,
N.Yamamoto,
J.G.Levin,
A.M.Gronenborn,
and
W.Sugiura
(2009).
HIV-1 Vif-mediated ubiquitination/degradation of APOBEC3G involves four critical lysine residues in its C-terminal domain.
|
| |
Proc Natl Acad Sci U S A, 106,
19539-19544.
|
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A.C.Minella,
K.R.Loeb,
A.Knecht,
M.Welcker,
B.J.Varnum-Finney,
I.D.Bernstein,
J.M.Roberts,
and
B.E.Clurman
(2008).
Cyclin E phosphorylation regulates cell proliferation in hematopoietic and epithelial lineages in vivo.
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| |
Genes Dev, 22,
1677-1689.
|
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A.Saha,
and
R.J.Deshaies
(2008).
Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation.
|
| |
Mol Cell, 32,
21-31.
|
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|
|
|
|
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B.J.Thompson,
V.Jankovic,
J.Gao,
S.Buonamici,
A.Vest,
J.M.Lee,
J.Zavadil,
S.D.Nimer,
and
I.Aifantis
(2008).
Control of hematopoietic stem cell quiescence by the E3 ubiquitin ligase Fbw7.
|
| |
J Exp Med, 205,
1395-1408.
|
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|
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B.L.Olson,
M.B.Hock,
S.Ekholm-Reed,
J.A.Wohlschlegel,
K.K.Dev,
A.Kralli,
and
S.I.Reed
(2008).
SCFCdc4 acts antagonistically to the PGC-1{alpha} transcriptional coactivator by targeting it for ubiquitin-mediated proteolysis.
|
| |
Genes Dev, 22,
252-264.
|
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C.Kanei-Ishii,
T.Nomura,
T.Takagi,
N.Watanabe,
K.I.Nakayama,
and
S.Ishii
(2008).
Fbxw7 Acts as an E3 Ubiquitin Ligase That Targets c-Myb for Nemo-like Kinase (NLK)-induced Degradation.
|
| |
J Biol Chem, 283,
30540-30548.
|
|
|
|
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D.J.Killian,
E.Harvey,
P.Johnson,
M.Otori,
S.Mitani,
and
D.Xue
(2008).
SKR-1, a homolog of Skp1 and a member of the SCF(SEL-10) complex, regulates sex-determination and LIN-12/Notch signaling in C. elegans.
|
| |
Dev Biol, 322,
322-331.
|
|
|
|
|
|
|
D.Ju,
X.Wang,
H.Xu,
and
Y.Xie
(2008).
Genome-wide analysis identifies MYND-domain protein Mub1 as an essential factor for Rpn4 ubiquitylation.
|
| |
Mol Cell Biol, 28,
1404-1412.
|
|
|
|
|
|
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D.M.Duda,
L.A.Borg,
D.C.Scott,
H.W.Hunt,
M.Hammel,
and
B.A.Schulman
(2008).
Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation.
|
| |
Cell, 134,
995.
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PDB codes:
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D.W.Choi,
Y.M.Seo,
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B.J.Thompson,
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K.P.Lu,
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X.Tang,
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Cell, 129,
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Y.Yoshida,
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A.A.Yunus,
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B.Padmanabhan,
K.I.Tong,
T.Ohta,
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Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancer.
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Mol Cell, 21,
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B.T.Seet,
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Nat Struct Mol Biol, 13,
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K.Horie-Inoue,
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PDB code:
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PDB code:
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A.Atir-Lande,
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PDB code:
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D.Ungermannova,
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PDB codes:
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F.P.Silva,
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Mol Genet Genomics, 273,
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Function and regulation of cullin-RING ubiquitin ligases.
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The Hedgehog-inducible ubiquitin ligase subunit WSB-1 modulates thyroid hormone activation and PTHrP secretion in the developing growth plate.
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Nat Cell Biol, 7,
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Different HECT domain ubiquitin ligases employ distinct mechanisms of polyubiquitin chain synthesis.
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The SV40 large T antigen contains a decoy phosphodegron that mediates its interactions with Fbw7/hCdc4.
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J Biol Chem, 280,
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P.J.Stogios,
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Sequence and structural analysis of BTB domain proteins.
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Genome Biol, 6,
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R.Barbey,
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Inducible dissociation of SCF(Met30) ubiquitin ligase mediates a rapid transcriptional response to cadmium.
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EMBO J, 24,
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The structure of cyclin E1/CDK2: implications for CDK2 activation and CDK2-independent roles.
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EMBO J, 24,
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PDB code:
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S.Rottmann,
Y.Wang,
M.Nasoff,
Q.L.Deveraux,
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A TRAIL receptor-dependent synthetic lethal relationship between MYC activation and GSK3beta/FBW7 loss of function.
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Proc Natl Acad Sci U S A, 102,
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Coevolution of cyclin Pcl5 and its substrate Gcn4.
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Eukaryot Cell, 4,
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T.Shirogane,
J.Jin,
X.L.Ang,
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SCFbeta-TRCP controls clock-dependent transcription via casein kinase 1-dependent degradation of the mammalian period-1 (Per1) protein.
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J Biol Chem, 280,
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X.L.Ang,
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SCF-mediated protein degradation and cell cycle control.
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Oncogene, 24,
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A.E.Miele,
P.J.Watson,
P.R.Evans,
L.M.Traub,
and
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Two distinct interaction motifs in amphiphysin bind two independent sites on the clathrin terminal domain beta-propeller.
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Nat Struct Mol Biol, 11,
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PDB code:
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|
A.Y.Madrona,
and
D.K.Wilson
(2004).
The structure of Ski8p, a protein regulating mRNA degradation: Implications for WD protein structure.
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Protein Sci, 13,
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PDB code:
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C.Kanei-Ishii,
T.Nomura,
J.Tanikawa,
E.Ichikawa-Iwata,
and
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Differential sensitivity of v-Myb and c-Myb to Wnt-1-induced protein degradation.
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J Biol Chem, 279,
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D.V.Hansen,
A.V.Loktev,
K.H.Ban,
and
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Plk1 regulates activation of the anaphase promoting complex by phosphorylating and triggering SCFbetaTrCP-dependent destruction of the APC Inhibitor Emi1.
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Mol Biol Cell, 15,
5623-5634.
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H.Rajagopalan,
P.V.Jallepalli,
C.Rago,
V.E.Velculescu,
K.W.Kinzler,
B.Vogelstein,
and
C.Lengauer
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Inactivation of hCDC4 can cause chromosomal instability.
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Nature, 428,
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H.Yamano,
K.Kominami,
C.Harrison,
K.Kitamura,
S.Katayama,
S.Dhut,
T.Hunt,
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Requirement of the SCFPop1/Pop2 Ubiquitin Ligase for Degradation of the Fission Yeast S Phase Cyclin Cig2.
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J Biol Chem, 279,
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J.M.Hsu,
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C.T.Yu,
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Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated hepatoma up-regulated protein (HURP) proteolysis by a proline-rich region.
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J Biol Chem, 279,
32592-32602.
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J.Nie,
S.S.Li,
and
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A novel PTB-PDZ domain interaction mediates isoform-specific ubiquitylation of mammalian Numb.
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J Biol Chem, 279,
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J.Smalle,
and
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The ubiquitin 26S proteasome proteolytic pathway.
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Annu Rev Plant Biol, 55,
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K.G.Kumar,
J.J.Krolewski,
and
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Phosphorylation and specific ubiquitin acceptor sites are required for ubiquitination and degradation of the IFNAR1 subunit of type I interferon receptor.
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J Biol Chem, 279,
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K.H.Moberg,
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The Drosophila F box protein archipelago regulates dMyc protein levels in vivo.
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Curr Biol, 14,
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K.Kumar,
M.Brady,
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Selective abolition of pancreatic RNase binding to its inhibitor protein.
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Proc Natl Acad Sci U S A, 101,
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L.E.Brunson,
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L.Kozubowski,
and
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The amino-terminal portion of the F-box protein Met30p mediates its nuclear import and assimilation into an SCF complex.
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J Biol Chem, 279,
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L.Pintard,
A.Willems,
and
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Cullin-based ubiquitin ligases: Cul3-BTB complexes join the family.
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EMBO J, 23,
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L.Wang,
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D.Ju,
and
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Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase.
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J Biol Chem, 279,
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M.B.Yaffe,
and
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The use of in vitro peptide-library screens in the analysis of phosphoserine/threonine-binding domain structure and function.
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Annu Rev Biophys Biomol Struct, 33,
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M.Welcker,
A.Orian,
J.E.Grim,
J.A.Grim,
R.N.Eisenman,
and
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A nucleolar isoform of the Fbw7 ubiquitin ligase regulates c-Myc and cell size.
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Curr Biol, 14,
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M.Welcker,
A.Orian,
J.Jin,
J.E.Grim,
J.A.Grim,
J.W.Harper,
R.N.Eisenman,
and
B.E.Clurman
(2004).
The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation.
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Proc Natl Acad Sci U S A, 101,
9085-9090.
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N.Spielewoy,
K.Flick,
T.I.Kalashnikova,
J.R.Walker,
and
C.Wittenberg
(2004).
Regulation and recognition of SCFGrr1 targets in the glucose and amino acid signaling pathways.
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Mol Cell Biol, 24,
8994-9005.
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Q.Yan,
T.Kamura,
Y.Cai,
J.Jin,
M.Ivan,
A.Mushegian,
R.C.Conaway,
and
J.W.Conaway
(2004).
Identification of Elongin C and Skp1 sequences that determine Cullin selection.
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J Biol Chem, 279,
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S.Jäger,
H.T.Schwartz,
H.R.Horvitz,
and
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The Caenorhabditis elegans F-box protein SEL-10 promotes female development and may target FEM-1 and FEM-3 for degradation by the proteasome.
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Proc Natl Acad Sci U S A, 101,
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S.J.Goldenberg,
T.C.Cascio,
S.D.Shumway,
K.C.Garbutt,
J.Liu,
Y.Xiong,
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Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases.
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| |
Cell, 119,
517-528.
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PDB code:
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|
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|
|
|
S.K.Dove,
R.C.Piper,
R.K.McEwen,
J.W.Yu,
M.C.King,
D.C.Hughes,
J.Thuring,
A.B.Holmes,
F.T.Cooke,
R.H.Michell,
P.J.Parker,
and
M.A.Lemmon
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Svp1p defines a family of phosphatidylinositol 3,5-bisphosphate effectors.
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EMBO J, 23,
1922-1933.
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T.Cardozo,
and
M.Pagano
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The SCF ubiquitin ligase: insights into a molecular machine.
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Nat Rev Mol Cell Biol, 5,
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T.Mizushima,
T.Hirao,
Y.Yoshida,
S.J.Lee,
T.Chiba,
K.Iwai,
Y.Yamaguchi,
K.Kato,
T.Tsukihara,
and
K.Tanaka
(2004).
Structural basis of sugar-recognizing ubiquitin ligase.
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| |
Nat Struct Mol Biol, 11,
365-370.
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|
PDB codes:
|
|
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|
|
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|
|
X.Ye,
G.Nalepa,
M.Welcker,
B.M.Kessler,
E.Spooner,
J.Qin,
S.J.Elledge,
B.E.Clurman,
and
J.W.Harper
(2004).
Recognition of phosphodegron motifs in human cyclin E by the SCF(Fbw7) ubiquitin ligase.
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J Biol Chem, 279,
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Y.Li,
S.Gazdoiu,
Z.Q.Pan,
and
S.Y.Fuchs
(2004).
Stability of homologue of Slimb F-box protein is regulated by availability of its substrate.
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J Biol Chem, 279,
11074-11080.
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A.E.Elia,
P.Rellos,
L.F.Haire,
J.W.Chao,
F.J.Ivins,
K.Hoepker,
D.Mohammad,
L.C.Cantley,
S.J.Smerdon,
and
M.B.Yaffe
(2003).
The molecular basis for phosphodependent substrate targeting and regulation of Plks by the Polo-box domain.
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| |
Cell, 115,
83-95.
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|
PDB code:
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|
|
|
|
|
C.Y.Eom,
and
I.R.Lehman
(2003).
Replication-initiator protein (UL9) of the herpes simplex virus 1 binds NFB42 and is degraded via the ubiquitin-proteasome pathway.
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Proc Natl Acad Sci U S A, 100,
9803-9807.
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G.Coadou,
J.Gharbi-Benarous,
S.Megy,
G.Bertho,
N.Evrard-Todeschi,
E.Segeral,
R.Benarous,
and
J.P.Girault
(2003).
NMR studies of the phosphorylation motif of the HIV-1 protein Vpu bound to the F-box protein beta-TrCP.
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Biochemistry, 42,
14741-14751.
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G.Wu,
G.Xu,
B.A.Schulman,
P.D.Jeffrey,
J.W.Harper,
and
N.P.Pavletich
(2003).
Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase.
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| |
Mol Cell, 11,
1445-1456.
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PDB code:
|
|
|
|
|
|
|
|
J.Jin,
T.Shirogane,
L.Xu,
G.Nalepa,
J.Qin,
S.J.Elledge,
and
J.W.Harper
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SCFbeta-TRCP links Chk1 signaling to degradation of the Cdc25A protein phosphatase.
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Genes Dev, 17,
3062-3074.
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K.Y.Cheng,
E.D.Lowe,
J.Sinclair,
E.A.Nigg,
and
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The crystal structure of the human polo-like kinase-1 polo box domain and its phospho-peptide complex.
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EMBO J, 22,
5757-5768.
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PDB codes:
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|
M.D.Petroski,
and
R.J.Deshaies
(2003).
Context of multiubiquitin chain attachment influences the rate of Sic1 degradation.
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Mol Cell, 11,
1435-1444.
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P.K.Jackson
(2003).
Ubiquitinating a phosphorylated Cdk inhibitor on the blades of the Cdc4 beta-propeller.
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Cell, 112,
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P.Klein,
T.Pawson,
and
M.Tyers
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Mathematical modeling suggests cooperative interactions between a disordered polyvalent ligand and a single receptor site.
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Curr Biol, 13,
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Q.He,
P.Cheng,
Y.Yang,
Q.He,
H.Yu,
and
Y.Liu
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FWD1-mediated degradation of FREQUENCY in Neurospora establishes a conserved mechanism for circadian clock regulation.
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EMBO J, 22,
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S.I.Reed
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Ratchets and clocks: the cell cycle, ubiquitylation and protein turnover.
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Nat Rev Mol Cell Biol, 4,
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S.Ono
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Regulation of actin filament dynamics by actin depolymerizing factor/cofilin and actin-interacting protein 1: new blades for twisted filaments.
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Biochemistry, 42,
13363-13370.
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T.A.Edwards,
B.D.Wilkinson,
R.P.Wharton,
and
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(2003).
Model of the brain tumor-Pumilio translation repressor complex.
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| |
Genes Dev, 17,
2508-2513.
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|
PDB code:
|
|
|
|
|
|
|
|
T.Pawson,
and
P.Nash
(2003).
Assembly of cell regulatory systems through protein interaction domains.
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Science, 300,
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W.Tang,
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V.S.Spiegelman,
A.A.Parkhitko,
and
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Interaction of Epstein-Barr virus latent membrane protein 1 with SCFHOS/beta-TrCP E3 ubiquitin ligase regulates extent of NF-kappaB activation.
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J Biol Chem, 278,
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Y.Su,
S.Ishikawa,
M.Kojima,
and
B.Liu
(2003).
Eradication of pathogenic beta-catenin by Skp1/Cullin/F box ubiquitination machinery.
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Proc Natl Acad Sci U S A, 100,
12729-12734.
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|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
|
|
Links
