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* Residue conservation analysis
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DOI no:
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Nature
427:171-175
(2004)
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PubMed id:
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Vinculin activation by talin through helical bundle conversion.
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T.Izard,
G.Evans,
R.A.Borgon,
C.L.Rush,
G.Bricogne,
P.R.Bois.
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ABSTRACT
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Vinculin is a conserved component and an essential regulator of both cell-cell
(cadherin-mediated) and cell-matrix (integrin-talin-mediated focal adhesions)
junctions, and it anchors these adhesion complexes to the actin cytoskeleton by
binding to talin in integrin complexes or to alpha-actinin in cadherin
junctions. In its resting state, vinculin is held in a closed conformation
through interactions between its head (Vh) and tail (Vt) domains. The binding of
vinculin to focal adhesions requires its association with talin. Here we report
the crystal structures of human vinculin in its inactive and talin-activated
states. Talin binding induces marked conformational changes in Vh, creating a
novel helical bundle structure, and this alteration actively displaces Vt from
Vh. These results, as well as the ability of alpha-actinin to also bind to Vh
and displace Vt from pre-existing Vh-Vt complexes, support a model whereby Vh
functions as a domain that undergoes marked structural changes that allow
vinculin to direct cytoskeletal assembly in focal adhesions and adherens
junctions. Notably, talin's effects on Vh structure establish helical bundle
conversion as a signalling mechanism by which proteins direct cellular responses.
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Selected figure(s)
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Figure 3.
Figure 3: Structure of inactive human vinculin. a, Cartoon
representation of the closed conformation of vinculin (Vh,
residues 1 -258, pink; Vt, 879 -1066, light blue). b, c,
Electrostatic surface potential (red, negative; blue, positive)
of the Vh -Vt complex. b, Head-on view of each interface (left,
Vh; right, Vt) when Vh and Vt are taken apart (that is, Vh is
rotated 90° to the left and Vt is rotated 90° to the right with
respect to the orientation shown in a). Residues involved in
interdomain contacts are labelled. c, Same orientation as in a,
revealing the acidic pocket created when Vh binds to Vt. Acidic
residues lining the pocket are indicated in yellow.
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Figure 4.
Figure 4: Structure of Vh when activated by talin. a,
Electrostatic surface potential (red, negative; blue, positive)
of Vh when bound to talin. Talin VBS3 is shown in ball-and-stick
representation (oxygen atoms, red; carbon, yellow; nitrogen,
blue; bonds, black). b, The C-terminal bundle (helices  4
-7) of active (red) and inactive (pink) Vh are superimposed
(back view of Fig. 3a). Talin VBS3, dark blue; Vt, light blue.
c, Movements and helical distortions (green arrows) of the
helices ( 1
-4) of the N-terminal bundle of inactive Vh (pink) occurring on
activation of Vh (red) by talin VBS3 (dark blue). Helices H1 -5
of inactive Vt (grey) are shown when bound to Vh (pink).
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2004,
427,
171-175)
copyright 2004.
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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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T.Izard,
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Shigella applies molecular mimicry to subvert vinculin and invade host cells.
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J Cell Biol,
175,
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W.H.Ziegler,
R.C.Liddington,
and
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A vinculin binding domain from the talin rod unfolds to form a complex with the vinculin head.
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Structure,
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PDB codes:
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K.Briknarová,
F.Nasertorabi,
M.L.Havert,
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P.R.Bois,
R.A.Borgon,
C.Vonrhein,
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Structural dynamics of alpha-actinin-vinculin interactions.
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Mol Cell Biol,
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PDB code:
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T.H.Millard,
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PDB code:
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C.L.Rush,
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Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle.
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PDB codes:
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K.A.Demali
(2004).
Vinculin--a dynamic regulator of cell adhesion.
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Trends Biochem Sci,
29,
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K.Takeda,
and
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(2004).
A fluorescence cell biology approach to map the second integrin-binding site of talin to a 130-amino acid sequence within the rod domain.
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J Biol Chem,
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M.C.Subauste,
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C.E.Turner,
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and
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Vinculin modulation of paxillin-FAK interactions regulates ERK to control survival and motility.
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J Cell Biol,
165,
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S.Witt,
A.Zieseniss,
U.Fock,
B.M.Jockusch,
and
S.Illenberger
(2004).
Comparative biochemical analysis suggests that vinculin and metavinculin cooperate in muscular adhesion sites.
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| |
J Biol Chem,
279,
31533-31543.
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T.Izard,
and
C.Vonrhein
(2004).
Structural basis for amplifying vinculin activation by talin.
|
| |
J Biol Chem,
279,
27667-27678.
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PDB code:
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Z.Zhang,
G.Izaguirre,
S.Y.Lin,
H.Y.Lee,
E.Schaefer,
and
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(2004).
The phosphorylation of vinculin on tyrosine residues 100 and 1065, mediated by SRC kinases, affects cell spreading.
|
| |
Mol Biol Cell,
15,
4234-4247.
|
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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.
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