The interaction of the cell-contact proteins VASP and vinculin is regulated by phosphatidylinositol-4,5-bisphosphate. (Q52530407)

2 May 2018

title

The interaction of the cell-contact proteins VASP and vinculin is regulated by phosphatidylinositol-4,5-bisphosphate. (English)

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2 May 2018

author name string

Hüttelmaier S

1

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2 May 2018

Mayboroda O

2

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2 May 2018

Harbeck B

3

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2 May 2018

Jarchau T

4

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2 May 2018

Jockusch BM

5

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2 May 2018

Rüdiger M

6

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2 May 2018

language of work or name

English

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publication date

1 April 1998

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2 May 2018

published in

Current Biology

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2 May 2018

volume

8

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2 May 2018

page(s)

479-488

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2 May 2018

issue

9

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2 May 2018

Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein)

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The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the proline-rich domain in vinculin

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VASP interaction with vinculin: a recurring theme of interactions with proline-rich motifs.

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Overexpression of vinculin suppresses cell motility in BALB/c 3T3 cells

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Suppression of tumorigenicity in transformed cells after transfection with vinculin cDNA

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Vinculin is essential for muscle function in the nematode

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A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family

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Mena, a relative of VASP and Drosophila Enabled, is implicated in the control of microfilament dynamics

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F-actin binding site masked by the intramolecular association of vinculin head and tail domains

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The carboxy-terminal tail domain of vinculin contains a cryptic binding site for acidic phospholipids.

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Molecular mechanisms for focal adhesion assembly through regulation of protein-protein interactions

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Intramolecular interactions in vinculin control alpha-actinin binding to the vinculin head

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Crosstalk between cell adhesion molecules: vinculin as a paradigm for regulation by conformation.

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Characterization of an F-actin-binding domain in the cytoskeletal protein vinculin

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Acidic phospholipids inhibit the intramolecular association between the N- and C-terminal regions of vinculin, exposing actin-binding and protein kinase C phosphorylation sites

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Intramolecular interactions regulate serine/threonine phosphorylation of vinculin

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Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-bisphosphate

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Cryptic sites in vinculin

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Adhesion to fibronectin stimulates inositol lipid synthesis and enhances PDGF-induced inositol lipid breakdown

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Characterization of two F-actin-binding and oligomerization sites in the cell-contact protein vinculin

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Interaction of the 47-kDa talin fragment and the 32-kDa vinculin fragment with acidic phospholipids: a computer analysis

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Regulation of Phospholipase C-γ1 by Profilin and Tyrosine Phosphorylation

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The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells

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Phosphorylation of focal adhesion vasodilator-stimulated phosphoprotein at Ser157 in intact human platelets correlates with fibrinogen receptor inhibition

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Beta-catenin: a common target for the regulation of cell adhesion by Wnt-1 and Src signaling pathways.

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Identifiers

DOI

1 reference

2 May 2018

PubMed ID

9560340

1 reference

2 May 2018