Specific interaction of vinculin with α-actinin

Wachsstock, Daniel H.; Wilkins, James A.; Lin, Shin

doi:10.1016/0006-291x(87)90564-x

Cited by 183 publications

(113 citation statements)

References 15 publications

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“…For example, it has been reported that a-actinin binds to vinculin, another protein concentrated in focal adhesions (Wachsstock et al ., 1987) . Using a blot assay we have failed to detect an interaction between the 53-kD fragment and vinculin but have shown that this apparent interaction occurs in the 27-kD domain of a-actinin .…”

Section: Discussionmentioning

confidence: 99%

Disruption of the actin cytoskeleton after microinjection of proteolytic fragments of alpha-actinin.

Pavalko

Burridge

1991

The Journal of Cell Biology

151

102

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Section: Discussionmentioning

confidence: 99%

Disruption of the actin cytoskeleton after microinjection of proteolytic fragments of alpha-actinin.

Pavalko

Burridge

1991

The Journal of Cell Biology

151

102

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“…The intramolecular interaction between Vh and Vt masks the F-actin-binding domain located in Vt (15). The binding of talin and ␣-actinin (16,17) to the D1 subdomain of vinculin induces a helical bundle conversion of this subdomain, leading to the disruption of the intramolecular interaction and the exposure of the cryptic F-actin-binding domain of Vt (18 -20). Interestingly, the bacterial protein IpaA from Shigella mimics the activation of vinculin by talin (21).…”

mentioning

confidence: 99%

Vinculin Is a Dually Regulated Actin Filament Barbed End-capping and Side-binding Protein

Clainche

Dwivedi

Didry

et al. 2010

Journal of Biological Chemistry

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The focal adhesion protein vinculin is an actin-binding protein involved in the mechanical coupling between the actin cytoskeleton and the extracellular matrix. An autoinhibitory interaction between the N-terminal head (Vh) and the C-terminal tail (Vt) of vinculin masks an actin filament side-binding domain in Vt. The binding of several proteins to Vh disrupts this intramolecular interaction and exposes the actin filament sidebinding domain. Here, by combining kinetic assays and microscopy observations, we show that Vt inhibits actin polymerization by blocking the barbed ends of actin filaments. In low salt conditions, Vt nucleates actin filaments capped at their barbed ends. We determined that the interaction between vinculin and the barbed end is characterized by slow association and dissociation rate constants. This barbed end capping activity requires C-terminal amino acids of Vt that are dispensable for actin filament side binding. Like the side-binding domain, the capping domain of vinculin is masked by an autoinhibitory interaction between Vh and Vt. In contrast to the side-binding domain, the capping domain is not unmasked by the binding of a talin domain to Vh and requires the dissociation of an additional autoinhibitory interaction. Finally, we show that vinculin and the formin mDia1, which is involved in the processive elongation of actin filaments in focal adhesions, compete for actin filament barbed ends.

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“…␣-Actinin interacts with several cytoskeletal proteins in addition to actin. A partial list of proteins includes vinculin (17), zyxin (18), and the newly described proteins palladin (19) and CLP-36 (20,21). A third group of proteins that interact with ␣-actinin includes signaling molecules such as extracellular signal-regulated kinase 1 (22), mitogen-activated protein kinase/extracellular signal-regulated kinase kinase kinase 1 (23), PKN, a fatty acid and Rho-activated serine/threonine protein kinase (24), and the p85 subunit of phosphatidylinositol 3-kinase (25).…”

mentioning

confidence: 99%

The Cytoskeletal/Non-muscle Isoform of α-Actinin Is Phosphorylated on Its Actin-binding Domain by the Focal Adhesion Kinase

Izaguirre¹,

Aguirre²,

Hu³

et al. 2001

Journal of Biological Chemistry

136

155

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␣-Actinin is tyrosine-phosphorylated in activated human platelets (Izaguirre, G., Aguirre, L., Ji, P., Aneskievich, B., and Haimovich, B. (1999) J. Biol. Chem. 274, 37012-37020). Analysis of platelet RNA by reverse transcription-polymerase chain reaction revealed that ␣-actinin expressed in platelets is identical to the cytoskeletal/non-muscle isoform. A construct of this isoform containing a His 6 tag at the amino terminus was generated. Robust tyrosine phosphorylation of the recombinant protein was detected in cells treated with the tyrosine phosphatase inhibitor vanadate. The tyrosine phosphorylation site was localized to the amino-terminal domain by proteolytic digestion. A recombinant ␣-actinin protein containing a Tyr 3 Phe mutation at position 12 (Y12F) was no longer phosphorylated when expressed in vanadate-treated cells, indicating that tyrosine 12 is the site of phosphorylation. The wild type recombinant protein was not phosphorylated in cells lacking the focal adhesion kinase (FAK). Re-expression of FAK in these cells restored ␣-actinin phosphorylation. Purified wild type ␣-actinin, but not the Y12F mutant, was phosphorylated in vitro by wild type as well as a Phe-397 mutant of FAK. In contrast, no phosphorylation was detected in the presence of a kinase-dead FAK. Tyrosine phosphorylation reduced the amount of ␣-actinin that cosedimented with actin filaments. These results establish that ␣-actinin is a direct substrate for FAK and suggest that ␣-actinin mediates FAK-dependent signals that could impact the physical properties of the cytoskeleton.

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Specific interaction of vinculin with α-actinin

Cited by 183 publications

References 15 publications

Disruption of the actin cytoskeleton after microinjection of proteolytic fragments of alpha-actinin.

Disruption of the actin cytoskeleton after microinjection of proteolytic fragments of alpha-actinin.

Vinculin Is a Dually Regulated Actin Filament Barbed End-capping and Side-binding Protein

The Cytoskeletal/Non-muscle Isoform of α-Actinin Is Phosphorylated on Its Actin-binding Domain by the Focal Adhesion Kinase

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