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PDBsum entry 3bct
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Armadillo repeat
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PDB id
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3bct
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Contents |
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* Residue conservation analysis
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DOI no:
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Cell
90:871-882
(1997)
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PubMed id:
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Three-dimensional structure of the armadillo repeat region of beta-catenin.
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A.H.Huber,
W.J.Nelson,
W.I.Weis.
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ABSTRACT
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Beta-catenin is essential for cadherin-based cell adhesion and Wnt/Wingless
growth factor signaling. In these roles, it binds to cadherins, Tcf-family
transcription factors, and the tumor suppressor gene product Adenomatous
Polyposis Coli (APC). A core region of beta-catenin, composed of 12 copies of a
42 amino acid sequence motif known as an armadillo repeat, mediates these
interactions. The three-dimensional structure of a protease-resistant fragment
of beta-catenin containing the armadillo repeat region has been determined. The
12 repeats form a superhelix of helices that features a long, positively charged
groove. Although unrelated in sequence, the beta-catenin binding regions of
cadherins, Tcfs, and APC are acidic and are proposed to interact with this
groove.
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Selected figure(s)
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Figure 2.
Figure 2. Stereo Views of Electron Density MapsThe region
near Trp-338, which interacts with Arg residues in the groove of
β59, is shown. The upper panel shows a portion of the refined
Form A model in the experimental 2.4 Å MAD-phased map. The
lower panel shows the same region of the Form B model in the
final 2.9 ŠForm B 2F[o] − F[c] map. Both maps are
contoured at 1.0 σ.
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Figure 5.
Figure 5. Stereo View Showing Relative Motion of the Two
Halves of β59The Cαs from residues 193–390 from Form A
(gray) and Form B (black) have been superimposed. The
COOH-terminal portions of the two structures are related by an
11.5° rotation about the axis shown as a straight vertical
line. The asterisk marks the middle of the loop that replaces H1
in repeat 7. This figure was made with MOLSCRIPT ([21]).
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The above figures are
reprinted
by permission from Cell Press:
Cell
(1997,
90,
871-882)
copyright 1997.
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Figures were
selected
by an automated process.
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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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C.F.Lee,
A.V.Hauenstein,
J.K.Fleming,
W.C.Gasper,
V.Engelke,
B.Sankaran,
S.I.Bernstein,
and
T.Huxford
(2011).
X-ray crystal structure of the UCS domain-containing UNC-45 myosin chaperone from Drosophila melanogaster.
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Structure,
19,
397-408.
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PDB code:
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G.Drechsel,
J.Bergler,
K.Wippel,
N.Sauer,
K.Vogelmann,
and
S.Hoth
(2011).
C-terminal armadillo repeats are essential and sufficient for association of the plant U-box armadillo E3 ubiquitin ligase SAUL1 with the plasma membrane.
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J Exp Bot,
62,
775-785.
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L.Zhang,
X.Yang,
S.Yang,
and
J.Zhang
(2011).
The Wnt /β-catenin signaling pathway in the adult neurogenesis.
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Eur J Neurosci,
33,
1-8.
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S.Mokhtarzada,
C.Yu,
A.Brickenden,
and
W.Y.Choy
(2011).
Structural characterization of partially disordered human chibby: insights into its function in the wnt-signaling pathway.
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Biochemistry,
50,
715-726.
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C.A.Ewens,
P.Kloppsteck,
A.Förster,
X.Zhang,
and
P.S.Freemont
(2010).
Structural and functional implications of phosphorylation and acetylation in the regulation of the AAA+ protein p97.
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Biochem Cell Biol,
88,
41-48.
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G.S.Yochum,
C.M.Sherrick,
M.Macpartlin,
and
R.H.Goodman
(2010).
A beta-catenin/TCF-coordinated chromatin loop at MYC integrates 5' and 3' Wnt responsive enhancers.
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Proc Natl Acad Sci U S A,
107,
145-150.
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H.S.Kang,
G.ZeRuth,
K.Lichti-Kaiser,
S.Vasanth,
Z.Yin,
Y.S.Kim,
and
A.M.Jetten
(2010).
Gli-similar (Glis) Krüppel-like zinc finger proteins: insights into their physiological functions and critical roles in neonatal diabetes and cystic renal disease.
|
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Histol Histopathol,
25,
1481-1496.
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H.Striegl,
M.A.Andrade-Navarro,
and
U.Heinemann
(2010).
Armadillo motifs involved in vesicular transport.
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PLoS One,
5,
e8991.
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J.E.Braun,
F.Tritschler,
G.Haas,
C.Igreja,
V.Truffault,
O.Weichenrieder,
and
E.Izaurralde
(2010).
The C-terminal alpha-alpha superhelix of Pat is required for mRNA decapping in metazoa.
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EMBO J,
29,
2368-2380.
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PDB codes:
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L.K.Lee,
M.A.Ginsburg,
C.Crovace,
M.Donohoe,
and
D.Stock
(2010).
Structure of the torque ring of the flagellar motor and the molecular basis for rotational switching.
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Nature,
466,
996.
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PDB code:
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P.D.McCrea,
and
D.Gu
(2010).
The catenin family at a glance.
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J Cell Sci,
123,
637-642.
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T.C.Terwilliger
(2010).
Rapid model building of alpha-helices in electron-density maps.
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Acta Crystallogr D Biol Crystallogr,
66,
268-275.
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T.C.Terwilliger
(2010).
Rapid model building of beta-sheets in electron-density maps.
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Acta Crystallogr D Biol Crystallogr,
66,
276-284.
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T.C.Terwilliger
(2010).
Rapid chain tracing of polypeptide backbones in electron-density maps.
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Acta Crystallogr D Biol Crystallogr,
66,
285-294.
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U.Straschil,
A.M.Talman,
D.J.Ferguson,
K.A.Bunting,
Z.Xu,
E.Bailes,
R.E.Sinden,
A.A.Holder,
E.F.Smith,
J.C.Coates,
and
Rita Tewari
(2010).
The Armadillo repeat protein PF16 is essential for flagellar structure and function in Plasmodium male gametes.
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PLoS One,
5,
e12901.
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V.L.Katis,
J.J.Lipp,
R.Imre,
A.Bogdanova,
E.Okaz,
B.Habermann,
K.Mechtler,
K.Nasmyth,
and
W.Zachariae
(2010).
Rec8 phosphorylation by casein kinase 1 and Cdc7-Dbf4 kinase regulates cohesin cleavage by separase during meiosis.
|
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Dev Cell,
18,
397-409.
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Y.Gu,
N.Kaplinsky,
M.Bringmann,
A.Cobb,
A.Carroll,
A.Sampathkumar,
T.I.Baskin,
S.Persson,
and
C.R.Somerville
(2010).
Identification of a cellulose synthase-associated protein required for cellulose biosynthesis.
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Proc Natl Acad Sci U S A,
107,
12866-12871.
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A.Hölsken,
J.Kreutzer,
B.M.Hofmann,
V.Hans,
F.Oppel,
M.Buchfelder,
R.Fahlbusch,
I.Blümcke,
and
R.Buslei
(2009).
Target gene activation of the Wnt signaling pathway in nuclear beta-catenin accumulating cells of adamantinomatous craniopharyngiomas.
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Brain Pathol,
19,
357-364.
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C.Mosimann,
G.Hausmann,
and
K.Basler
(2009).
Beta-catenin hits chromatin: regulation of Wnt target gene activation.
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Nat Rev Mol Cell Biol,
10,
276-286.
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D.A.Mason,
D.E.Stage,
and
D.S.Goldfarb
(2009).
Evolution of the metazoan-specific importin alpha gene family.
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J Mol Evol,
68,
351-365.
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D.Yee,
and
D.R.Goring
(2009).
The diversity of plant U-box E3 ubiquitin ligases: from upstream activators to downstream target substrates.
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J Exp Bot,
60,
1109-1121.
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E.Delva,
D.K.Tucker,
and
A.P.Kowalczyk
(2009).
The desmosome.
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Cold Spring Harbor Perspect Biol,
1,
a002543.
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H.J.Choi,
J.C.Gross,
S.Pokutta,
and
W.I.Weis
(2009).
Interactions of plakoglobin and beta-catenin with desmosomal cadherins: basis of selective exclusion of alpha- and beta-catenin from desmosomes.
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J Biol Chem,
284,
31776-31788.
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PDB code:
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H.Striegl,
Y.Roske,
D.Kümmel,
and
U.Heinemann
(2009).
Unusual armadillo fold in the human general vesicular transport factor p115.
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PLoS ONE,
4,
e4656.
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PDB code:
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H.Wu,
K.Symes,
D.C.Seldin,
and
I.Dominguez
(2009).
Threonine 393 of beta-catenin regulates interaction with Axin.
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J Cell Biochem,
108,
52-63.
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L.Shapiro,
and
W.I.Weis
(2009).
Structure and biochemistry of cadherins and catenins.
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Cold Spring Harbor Perspect Biol,
1,
a003053.
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M.Figueroa,
M.V.Hinrichs,
M.Bunster,
P.Babbitt,
J.Martinez-Oyanedel,
and
J.Olate
(2009).
Biophysical studies support a predicted superhelical structure with armadillo repeats for Ric-8.
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Protein Sci,
18,
1139-1145.
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M.J.Nadolski,
and
M.E.Linder
(2009).
Molecular recognition of the palmitoylation substrate Vac8 by its palmitoyltransferase Pfa3.
|
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J Biol Chem,
284,
17720-17730.
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R.Mo,
T.L.Chew,
M.T.Maher,
G.Bellipanni,
E.S.Weinberg,
and
C.J.Gottardi
(2009).
The terminal region of beta-catenin promotes stability by shielding the Armadillo repeats from the axin-scaffold destruction complex.
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J Biol Chem,
284,
28222-28231.
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T.C.Terwilliger,
P.D.Adams,
R.J.Read,
A.J.McCoy,
N.W.Moriarty,
R.W.Grosse-Kunstleve,
P.V.Afonine,
P.H.Zwart,
and
L.W.Hung
(2009).
Decision-making in structure solution using Bayesian estimates of map quality: the PHENIX AutoSol wizard.
|
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Acta Crystallogr D Biol Crystallogr,
65,
582-601.
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W.W.Franke
(2009).
Discovering the molecular components of intercellular junctions-a historical view.
|
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Cold Spring Harbor Perspect Biol,
1,
a003061.
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Y.An,
C.Y.Chen,
B.Moyer,
P.Rotkiewicz,
M.A.Elsliger,
A.Godzik,
I.A.Wilson,
and
W.E.Balch
(2009).
Structural and functional analysis of the globular head domain of p115 provides insight into membrane tethering.
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J Mol Biol,
391,
26-41.
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PDB codes:
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A.Hartsock,
and
W.J.Nelson
(2008).
Adherens and tight junctions: structure, function and connections to the actin cytoskeleton.
|
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Biochim Biophys Acta,
1778,
660-669.
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A.Klaus,
and
W.Birchmeier
(2008).
Wnt signalling and its impact on development and cancer.
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Nat Rev Cancer,
8,
387-398.
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B.A.Thompson,
V.Tremblay,
G.Lin,
and
D.A.Bochar
(2008).
CHD8 is an ATP-dependent chromatin remodeling factor that regulates beta-catenin target genes.
|
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Mol Cell Biol,
28,
3894-3904.
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C.J.Gottardi,
and
M.Peifer
(2008).
Terminal regions of beta-catenin come into view.
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Structure,
16,
336-338.
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K.M.Schmidt-Ott,
and
J.Barasch
(2008).
WNT/beta-catenin signaling in nephron progenitors and their epithelial progeny.
|
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Kidney Int,
74,
1004-1008.
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M.Lal,
X.Song,
J.L.Pluznick,
V.Di Giovanni,
D.M.Merrick,
N.D.Rosenblum,
V.Chauvet,
C.J.Gottardi,
Y.Pei,
and
M.J.Caplan
(2008).
Polycystin-1 C-terminal tail associates with beta-catenin and inhibits canonical Wnt signaling.
|
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Hum Mol Genet,
17,
3105-3117.
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M.de la Roche,
J.Worm,
and
M.Bienz
(2008).
The function of BCL9 in Wnt/beta-catenin signaling and colorectal cancer cells.
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BMC Cancer,
8,
199.
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P.C.da Fonseca,
and
E.P.Morris
(2008).
Structure of the Human 26S Proteasome: SUBUNIT RADIAL DISPLACEMENTS OPEN THE GATE INTO THE PROTEOLYTIC CORE.
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J Biol Chem,
283,
23305-23314.
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R.Götz
(2008).
Inter-cellular adhesion disruption and the RAS/RAF and beta-catenin signalling in lung cancer progression.
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Cancer Cell Int,
8,
7.
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S.Bahmanyar,
D.D.Kaplan,
J.G.Deluca,
T.H.Giddings,
E.T.O'Toole,
M.Winey,
E.D.Salmon,
P.J.Casey,
W.J.Nelson,
and
A.I.Barth
(2008).
beta-Catenin is a Nek2 substrate involved in centrosome separation.
|
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Genes Dev,
22,
91.
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X.Chen,
J.Yang,
P.M.Evans,
and
C.Liu
(2008).
Wnt signaling: the good and the bad.
|
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Acta Biochim Biophys Sin (Shanghai),
40,
577-594.
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B.Baminger,
M.L.Ludwiczek,
G.Kontaxis,
S.Knapp,
and
R.Konrat
(2007).
Protein-protein interaction site mapping using NMR-detected mutational scanning.
|
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J Biomol NMR,
38,
133-137.
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B.Dalhus,
I.H.Helle,
P.H.Backe,
I.Alseth,
T.Rognes,
M.Bjørås,
and
J.K.Laerdahl
(2007).
Structural insight into repair of alkylated DNA by a new superfamily of DNA glycosylases comprising HEAT-like repeats.
|
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Nucleic Acids Res,
35,
2451-2459.
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C.Jeronimo,
D.Forget,
A.Bouchard,
Q.Li,
G.Chua,
C.Poitras,
C.Thérien,
D.Bergeron,
S.Bourassa,
J.Greenblatt,
B.Chabot,
G.G.Poirier,
T.R.Hughes,
M.Blanchette,
D.H.Price,
and
B.Coulombe
(2007).
Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme.
|
| |
Mol Cell,
27,
262-274.
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D.L.Stokes
(2007).
Desmosomes from a structural perspective.
|
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Curr Opin Cell Biol,
19,
565-571.
|
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J.P.Muñoz,
C.H.Huichalaf,
D.Orellana,
and
R.B.Maccioni
(2007).
cdk5 modulates beta- and delta-catenin/Pin1 interactions in neuronal cells.
|
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J Cell Biochem,
100,
738-749.
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M.Ritco-Vonsovici,
A.Ababou,
and
M.Horton
(2007).
Molecular plasticity of beta-catenin: new insights from single-molecule measurements and MD simulation.
|
| |
Protein Sci,
16,
1984-1998.
|
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R.G.Garces,
W.Gillon,
and
E.F.Pai
(2007).
Atomic model of human Rcd-1 reveals an armadillo-like-repeat protein with in vitro nucleic acid binding properties.
|
| |
Protein Sci,
16,
176-188.
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PDB code:
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R.K.Nookala,
S.Hussain,
and
L.Pellegrini
(2007).
Insights into Fanconi Anaemia from the structure of human FANCE.
|
| |
Nucleic Acids Res,
35,
1638-1648.
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PDB code:
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R.L.Daugherty,
and
C.J.Gottardi
(2007).
Phospho-regulation of Beta-catenin adhesion and signaling functions.
|
| |
Physiology (Bethesda),
22,
303-309.
|
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W.W.Yue,
M.Hassler,
S.M.Roe,
V.Thompson-Vale,
and
L.H.Pearl
(2007).
Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase.
|
| |
EMBO J,
26,
4402-4412.
|
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PDB codes:
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X.C.He,
T.Yin,
J.C.Grindley,
Q.Tian,
T.Sato,
W.A.Tao,
R.Dirisina,
K.S.Porter-Westpfahl,
M.Hembree,
T.Johnson,
L.M.Wiedemann,
T.A.Barrett,
L.Hood,
H.Wu,
and
L.Li
(2007).
PTEN-deficient intestinal stem cells initiate intestinal polyposis.
|
| |
Nat Genet,
39,
189-198.
|
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Y.S.Kim,
H.S.Kang,
and
A.M.Jetten
(2007).
The Krüppel-like zinc finger protein Glis2 functions as a negative modulator of the Wnt/beta-catenin signaling pathway.
|
| |
FEBS Lett,
581,
858-864.
|
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A.E.Hodel,
M.T.Harreman,
K.F.Pulliam,
M.E.Harben,
J.S.Holmes,
M.R.Hodel,
K.M.Berland,
and
A.H.Corbett
(2006).
Nuclear localization signal receptor affinity correlates with in vivo localization in Saccharomyces cerevisiae.
|
| |
J Biol Chem,
281,
23545-23556.
|
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D.Kimelman,
and
W.Xu
(2006).
beta-catenin destruction complex: insights and questions from a structural perspective.
|
| |
Oncogene,
25,
7482-7491.
|
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F.Rook,
F.Corke,
M.Baier,
R.Holman,
A.G.May,
and
M.W.Bevan
(2006).
Impaired sucrose induction1 encodes a conserved plant-specific protein that couples carbohydrate availability to gene expression and plant growth.
|
| |
Plant J,
46,
1045-1058.
|
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F.Tang,
Y.Peng,
J.J.Nau,
E.J.Kauffman,
and
L.S.Weisman
(2006).
Vac8p, an armadillo repeat protein, coordinates vacuole inheritance with multiple vacuolar processes.
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EMBO J,
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L.A.Ligon,
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Dynein binds to beta-catenin and may tether microtubules at adherens junctions.
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Nat Cell Biol,
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ND9P, a novel protein with armadillo-like repeats involved in exocytosis: physiological studies using allelic mutants in paramecium.
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Genetics,
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Structure of Pumilio reveals similarity between RNA and peptide binding motifs.
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Cell,
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PDB code:
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T.A.Graham,
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Tcf4 can specifically recognize beta-catenin using alternative conformations.
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Nat Struct Biol,
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PDB code:
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T.C.Terwilliger
(2001).
Maximum-likelihood density modification using pattern recognition of structural motifs.
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Acta Crystallogr D Biol Crystallogr,
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Gibberellins signal nuclear import of PHOR1, a photoperiod-responsive protein with homology to Drosophila armadillo.
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Cell,
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Crystal structure of a Pumilio homology domain.
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Mol Cell,
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PDB codes:
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B.Kobe,
and
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When protein folding is simplified to protein coiling: the continuum of solenoid protein structures.
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Trends Biochem Sci,
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Characterization of the N-terminal domain of the yeast transcriptional repressor Tup1. Proposal for an association model of the repressor complex Tup1 x Ssn6.
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J Biol Chem,
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Defining functional domains within PF16: a central apparatus component required for flagellar motility.
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Cell Motil Cytoskeleton,
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J Cell Biol,
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PDB code:
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and
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Biochemistry,
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Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain.
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PDB codes:
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Plakoglobin regulates the expression of the anti-apoptotic protein BCL-2.
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Structure of the dimerization and beta-catenin-binding region of alpha-catenin.
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Mol Cell,
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PDB codes:
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T.A.Graham,
C.Weaver,
F.Mao,
D.Kimelman,
and
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Crystal structure of a beta-catenin/Tcf complex.
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Cell,
103,
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PDB code:
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T.Akiyama
(2000).
Wnt/beta-catenin signaling.
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Cytokine Growth Factor Rev,
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Nucleus-vacuole junctions in Saccharomyces cerevisiae are formed through the direct interaction of Vac8p with Nvj1p.
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Mol Biol Cell,
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B.Kobe,
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Turn up the HEAT.
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Structure,
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Controversies at the cytoplasmic face of the cadherin-based adhesion complex.
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Curr Opin Cell Biol,
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beta-catenin can be transported into the nucleus in a Ran-unassisted manner.
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Mol Biol Cell,
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Cold Spring Harb Symp Quant Biol,
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L.M.Rice,
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Crystal structure of the vesicular transport protein Sec17: implications for SNAP function in SNARE complex disassembly.
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Mol Cell,
4,
85-95.
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PDB code:
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M.Bienz
(1999).
APC: the plot thickens.
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Curr Opin Genet Dev,
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M.G.Prieve,
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Nuclear localization and formation of beta-catenin-lymphoid enhancer factor 1 complexes are not sufficient for activation of gene expression.
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Mol Cell Biol,
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M.R.Groves,
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Topological characteristics of helical repeat proteins.
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Curr Opin Struct Biol,
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M.R.Groves,
N.Hanlon,
P.Turowski,
B.A.Hemmings,
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(1999).
The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs.
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Cell,
96,
99.
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PDB code:
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M.W.Klymkowsky,
B.O.Williams,
G.D.Barish,
H.E.Varmus,
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(1999).
Membrane-anchored plakoglobins have multiple mechanisms of action in Wnt signaling.
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Mol Biol Cell,
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M.W.Klymkowsky
(1999).
Plakophilin, armadillo repeats, and nuclear localization.
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Microsc Res Tech,
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P.J.Morin
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beta-catenin signaling and cancer.
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Bioessays,
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R.T.Cox,
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J.Stein,
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Roles of the C terminus of Armadillo in Wingless signaling in Drosophila.
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Genetics,
153,
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R.W.Grosse-Kunstleve,
and
A.T.Brunger
(1999).
A highly automated heavy-atom search procedure for macromolecular structures.
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Acta Crystallogr D Biol Crystallogr,
55,
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S.Miravet,
J.Piedra,
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Regulation of E-cadherin/Catenin association by tyrosine phosphorylation.
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J Biol Chem,
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T.C.Terwilliger,
and
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Automated MAD and MIR structure solution.
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Acta Crystallogr D Biol Crystallogr,
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T.Teh,
T.Tiganis,
and
B.Kobe
(1999).
Crystallization of importin alpha, the nuclear-import receptor.
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Acta Crystallogr D Biol Crystallogr,
55,
561-563.
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Y.T.Chen,
D.B.Stewart,
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Coupling assembly of the E-cadherin/beta-catenin complex to efficient endoplasmic reticulum exit and basal-lateral membrane targeting of E-cadherin in polarized MDCK cells.
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J Cell Biol,
144,
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Differential molecular interactions of beta-catenin and plakoglobin in adhesion, signaling and cancer.
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Curr Opin Cell Biol,
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A.K.Das,
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The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions.
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EMBO J,
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PDB code:
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C.Dingwall,
and
R.A.Laskey
(1998).
Nuclear import: a tale of two sites.
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Curr Biol,
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C.L.Adams,
and
W.J.Nelson
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Cytomechanics of cadherin-mediated cell-cell adhesion.
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Curr Opin Cell Biol,
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E.Conti,
M.Uy,
L.Leighton,
G.Blobel,
and
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Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha.
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Cell,
94,
193-204.
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PDB codes:
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E.F.Pai
(1998).
The alpha and beta of turning on a molecular switch.
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Nat Struct Biol,
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E.Mossessova,
J.M.Gulbis,
and
J.Goldberg
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Structure of the guanine nucleotide exchange factor Sec7 domain of human arno and analysis of the interaction with ARF GTPase.
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Cell,
92,
415-423.
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E.ter Haar,
A.Musacchio,
S.C.Harrison,
and
T.Kirchhausen
(1998).
Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker.
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Cell,
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563-573.
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PDB code:
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J.D.Brown,
and
R.T.Moon
(1998).
Wnt signaling: why is everything so negative?
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J.K.Hood,
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Cse1p is required for export of Srp1p/importin-alpha from the nucleus in Saccharomyces cerevisiae.
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J Biol Chem,
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K.K.Vithalani,
C.A.Parent,
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M.Penn,
D.A.Larochelle,
P.N.Devreotes,
and
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Identification of darlin, a Dictyostelium protein with Armadillo-like repeats that binds to small GTPases and is important for the proper aggregation of developing cells.
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Mol Biol Cell,
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K.Willert,
and
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Beta-catenin: a key mediator of Wnt signaling.
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Curr Opin Genet Dev,
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Structural biology of cadherins in the nervous system.
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Curr Opin Neurobiol,
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K.L.Guttridge,
J.Munguia,
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Differential importin-alpha recognition and nuclear transport by nuclear localization signals within the high-mobility-group DNA binding domains of lymphoid enhancer factor 1 and T-cell factor 1.
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Mol Cell Biol,
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M.H.Wong,
B.Rubinfeld,
and
J.I.Gordon
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Effects of forced expression of an NH2-terminal truncated beta-Catenin on mouse intestinal epithelial homeostasis.
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J Cell Biol,
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J.Groffen,
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Involvement of the tyrosine kinase fer in cell adhesion.
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Mol Cell Biol,
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Identification of structural elements involved in the interaction of simian virus 40 small tumor antigen with protein phosphatase 2A.
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J Biol Chem,
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H.Yamamoto,
H.Murai,
S.Koyama,
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Axin, a negative regulator of the Wnt signaling pathway, forms a complex with GSK-3beta and beta-catenin and promotes GSK-3beta-dependent phosphorylation of beta-catenin.
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EMBO J,
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Y.Ahmed,
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Regulation of armadillo by a Drosophila APC inhibits neuronal apoptosis during retinal development.
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Cell,
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T.H.Eickbush,
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Evolutionary specialization of the nuclear targeting apparatus.
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Proc Natl Acad Sci U S A,
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L.Shapiro
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The multi-talented beta-catenin makes its first appearance.
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Structure,
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1265-1268.
|
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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
code is
shown on the right.
|
|
Links
