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PDBsum entry 1ntv
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Signaling protein
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PDB id
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1ntv
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Contents |
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* Residue conservation analysis
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Structure
11:569-579
(2003)
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PubMed id:
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Origins of peptide selectivity and phosphoinositide binding revealed by structures of disabled-1 PTB domain complexes.
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P.C.Stolt,
H.Jeon,
H.K.Song,
J.Herz,
M.J.Eck,
S.C.Blacklow.
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ABSTRACT
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Formation of the mammalian six-layered neocortex depends on a signaling pathway
that involves Reelin, the very low-density lipoprotein receptor, the
apolipoprotein E receptor-2 (ApoER2), and the adaptor protein Disabled-1 (Dab1).
The 1.5 A crystal structure of a complex between the Dab1 phosphotyrosine
binding (PTB) domain and a 14-residue peptide from the ApoER2 tail explains the
unusual preference of Dab1 for unphosphorylated tyrosine within the NPxY motif
of the peptide. Crystals of the complex soaked with the phosphoinositide
PI-4,5P(2) (PI) show that PI binds to conserved basic residues on the PTB domain
opposite the peptide binding groove. This finding explains how the Dab1 PTB
domain can simultaneously bind PI and the ApoER2 tail. Recruitment of the Dab1
PTB domain to PI-rich regions of the plasma membrane may facilitate association
with the Reelin receptor cytoplasmic tails to transduce a critical positional
cue to migrating neurons.
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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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M.Dieckmann,
M.F.Dietrich,
and
J.Herz
(2010).
Lipoprotein receptors--an evolutionarily ancient multifunctional receptor family.
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Biol Chem,
391,
1341-1363.
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O.Y.Kwon,
K.Hwang,
J.A.Kim,
K.Kim,
I.C.Kwon,
H.K.Song,
and
H.Jeon
(2010).
Dab1 binds to Fe65 and diminishes the effect of Fe65 or LRP1 on APP processing.
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J Cell Biochem,
111,
508-519.
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X.Tong,
D.Zitserman,
I.Serebriiskii,
M.Andrake,
R.Dunbrack,
and
F.Roegiers
(2010).
Numb independently antagonizes Sanpodo membrane targeting and Notch signaling in Drosophila sensory organ precursor cells.
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Mol Biol Cell,
21,
802-810.
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K.N.Pandey
(2009).
Functional roles of short sequence motifs in the endocytosis of membrane receptors.
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Front Biosci,
14,
5339-5360.
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J.Radzimanowski,
S.Ravaud,
S.Schlesinger,
J.Koch,
K.Beyreuther,
I.Sinning,
and
K.Wild
(2008).
Crystal structure of the human Fe65-PTB1 domain.
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J Biol Chem,
283,
23113-23120.
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PDB codes:
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M.Leone,
E.C.Yu,
R.C.Liddington,
E.B.Pasquale,
and
M.Pellecchia
(2008).
The PTB domain of tensin: NMR solution structure and phosphoinositides binding studies.
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Biopolymers,
89,
86-92.
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PDB code:
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P.A.Keyel,
J.R.Thieman,
R.Roth,
E.Erkan,
E.T.Everett,
S.C.Watkins,
J.E.Heuser,
and
L.M.Traub
(2008).
The AP-2 adaptor beta2 appendage scaffolds alternate cargo endocytosis.
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Mol Biol Cell,
19,
5309-5326.
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A.Rosenhouse-Dantsker,
and
D.E.Logothetis
(2007).
Molecular characteristics of phosphoinositide binding.
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Pflugers Arch,
455,
45-53.
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C.J.McCleverty,
D.C.Lin,
and
R.C.Liddington
(2007).
Structure of the PTB domain of tensin1 and a model for its recruitment to fibrillar adhesions.
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Protein Sci,
16,
1223-1229.
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PDB code:
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D.F.Ceccarelli,
I.M.Blasutig,
M.Goudreault,
Z.Li,
J.Ruston,
T.Pawson,
and
F.Sicheri
(2007).
Non-canonical interaction of phosphoinositides with pleckstrin homology domains of Tiam1 and ArhGAP9.
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J Biol Chem,
282,
13864-13874.
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PDB codes:
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E.Im,
and
A.Kazlauskas
(2007).
PtdIns-4,5-P2 as a potential therapeutic target for pathologic angiogenesis.
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Expert Opin Ther Targets,
11,
443-451.
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J.Li,
X.Mao,
L.Q.Dong,
F.Liu,
and
L.Tong
(2007).
Crystal structures of the BAR-PH and PTB domains of human APPL1.
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Structure,
15,
525-533.
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PDB codes:
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R.K.Mahadev,
S.M.Di Pietro,
J.M.Olson,
H.L.Piao,
G.S.Payne,
and
M.Overduin
(2007).
Structure of Sla1p homology domain 1 and interaction with the NPFxD endocytic internalization motif.
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EMBO J,
26,
1963-1971.
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PDB code:
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E.Förster,
Y.Jossin,
S.Zhao,
X.Chai,
M.Frotscher,
and
A.M.Goffinet
(2006).
Recent progress in understanding the role of Reelin in radial neuronal migration, with specific emphasis on the dentate gyrus.
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Eur J Neurosci,
23,
901-909.
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H.S.Hoe,
T.S.Tran,
Y.Matsuoka,
B.W.Howell,
and
G.W.Rebeck
(2006).
DAB1 and Reelin effects on amyloid precursor protein and ApoE receptor 2 trafficking and processing.
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J Biol Chem,
281,
35176-35185.
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J.Herz,
and
Y.Chen
(2006).
Reelin, lipoprotein receptors and synaptic plasticity.
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Nat Rev Neurosci,
7,
850-859.
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X.Shi,
T.Hong,
K.L.Walter,
M.Ewalt,
E.Michishita,
T.Hung,
D.Carney,
P.Peña,
F.Lan,
M.R.Kaadige,
N.Lacoste,
C.Cayrou,
F.Davrazou,
A.Saha,
B.R.Cairns,
D.E.Ayer,
T.G.Kutateladze,
Y.Shi,
J.Côté,
K.F.Chua,
and
O.Gozani
(2006).
ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression.
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Nature,
442,
96-99.
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H.Jeon,
and
S.C.Blacklow
(2005).
Structure and physiologic function of the low-density lipoprotein receptor.
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Annu Rev Biochem,
74,
535-562.
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M.Xu,
L.Arnaud,
and
J.A.Cooper
(2005).
Both the phosphoinositide and receptor binding activities of Dab1 are required for Reelin-stimulated Dab1 tyrosine phosphorylation.
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Brain Res Mol Brain Res,
139,
300-305.
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P.C.Stolt,
Y.Chen,
P.Liu,
H.H.Bock,
S.C.Blacklow,
and
J.Herz
(2005).
Phosphoinositide binding by the disabled-1 PTB domain is necessary for membrane localization and Reelin signal transduction.
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J Biol Chem,
280,
9671-9677.
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R.Garuti,
C.Jones,
W.P.Li,
P.Michaely,
J.Herz,
R.D.Gerard,
J.C.Cohen,
and
H.H.Hobbs
(2005).
The modular adaptor protein autosomal recessive hypercholesterolemia (ARH) promotes low density lipoprotein receptor clustering into clathrin-coated pits.
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J Biol Chem,
280,
40996-41004.
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S.K.Mishra,
P.A.Keyel,
M.A.Edeling,
A.L.Dupin,
D.J.Owen,
and
L.M.Traub
(2005).
Functional dissection of an AP-2 beta2 appendage-binding sequence within the autosomal recessive hypercholesterolemia protein.
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J Biol Chem,
280,
19270-19280.
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U.Beffert,
E.J.Weeber,
A.Durudas,
S.Qiu,
I.Masiulis,
J.D.Sweatt,
W.P.Li,
G.Adelmann,
M.Frotscher,
R.E.Hammer,
and
J.Herz
(2005).
Modulation of synaptic plasticity and memory by Reelin involves differential splicing of the lipoprotein receptor Apoer2.
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Neuron,
47,
567-579.
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D.J.Owen,
B.M.Collins,
and
P.R.Evans
(2004).
Adaptors for clathrin coats: structure and function.
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Annu Rev Cell Dev Biol,
20,
153-191.
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H.H.Bock,
Y.Jossin,
P.May,
O.Bergner,
and
J.Herz
(2004).
Apolipoprotein E receptors are required for reelin-induced proteasomal degradation of the neuronal adaptor protein Disabled-1.
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J Biol Chem,
279,
33471-33479.
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J.W.Yu,
J.M.Mendrola,
A.Audhya,
S.Singh,
D.Keleti,
D.B.DeWald,
D.Murray,
S.D.Emr,
and
M.A.Lemmon
(2004).
Genome-wide analysis of membrane targeting by S. cerevisiae pleckstrin homology domains.
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Mol Cell,
13,
677-688.
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M.S.Robinson
(2004).
Adaptable adaptors for coated vesicles.
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Trends Cell Biol,
14,
167-174.
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N.R.Blatner,
R.V.Stahelin,
K.Diraviyam,
P.T.Hawkins,
W.Hong,
D.Murray,
and
W.Cho
(2004).
The molecular basis of the differential subcellular localization of FYVE domains.
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J Biol Chem,
279,
53818-53827.
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T.G.Kutateladze,
D.G.Capelluto,
C.G.Ferguson,
M.L.Cheever,
A.G.Kutateladze,
G.D.Prestwich,
and
M.Overduin
(2004).
Multivalent mechanism of membrane insertion by the FYVE domain.
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J Biol Chem,
279,
3050-3057.
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A.Farooq,
L.Zeng,
K.S.Yan,
K.S.Ravichandran,
and
M.M.Zhou
(2003).
Coupling of folding and binding in the PTB domain of the signaling protein Shc.
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Structure,
11,
905-913.
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PDB codes:
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H.H.Bock,
Y.Jossin,
P.Liu,
E.Förster,
P.May,
A.M.Goffinet,
and
J.Herz
(2003).
Phosphatidylinositol 3-kinase interacts with the adaptor protein Dab1 in response to Reelin signaling and is required for normal cortical lamination.
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J Biol Chem,
278,
38772-38779.
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K.S.Yan,
and
M.M.Zhou
(2003).
Examining both sides of a Janus PTB domain.
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Structure,
11,
482-484.
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L.M.Traub
(2003).
Sorting it out: AP-2 and alternate clathrin adaptors in endocytic cargo selection.
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J Cell Biol,
163,
203-208.
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M.Yun,
L.Keshvara,
C.G.Park,
Y.M.Zhang,
J.B.Dickerson,
J.Zheng,
C.O.Rock,
T.Curran,
and
H.W.Park
(2003).
Crystal structures of the Dab homology domains of mouse disabled 1 and 2.
|
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J Biol Chem,
278,
36572-36581.
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PDB codes:
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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.
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