An interaction between vinculin and talin

Burridge, Keith; Mangeat, Paul

doi:10.1038/308744a0

Cited by 426 publications

(270 citation statements)

References 18 publications

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“…Our results clearly show that vinculin and talin occur in type I particle aggregates, where they could mediate the association of actin with the cytoplasmic tail of integrin (14,35,42,46,60). The proximity of actin filaments to /~-integrin is suggested by our observation that antibodies to the cytoplasmic tail of/~-integrin did not label that protein when overlying actin filaments are present.…”

Section: Aggregates Of Membrane Particlessupporting

confidence: 53%

Structures linking microfilament bundles to the membrane at focal contacts

Samuelsson

Luther

Pumplin

et al. 1993

The Journal of Cell Biology

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Abstract. We used quick-freeze, deep-etch, rotary replication and immunogold cytochemistry to identify a new structure at focal contacts. In Xenopus fibroblasts, elongated aggregates of particles project from the membrane to contact bundles of actin microfilaments. Before terminating, a single bundle of microfilaments interacts with several aggregates that appear intermittently over a distance of several microns. Aggregates are enriched in proteins believed to mediate actin-membrane interactions at focal contacts, including B~-integrin, vinculin, and talin, but they appear to contain less t~-actinin and filamin. We also identified a second, smaller class of aggregates of membrane particles that contained/~-integrin but not vinculin or talin and that were not associated with actin microfilaments. Our results indicate that vinculin, talin, and ~-integrin are assembled into distinctive structures that mediate multiple lateral interactions between microfilaments and the membrane at focal contacts.F OCAL contacts are specialized structures where actin filaments converge and terminate at the plasma membrane (16,32,44,63,65). Interactions between the membrane and microfilaments involve several proteins that are concentrated at focal contacts, including integrin (e.g., references 17, 21, 22; reviewed in 1, 61) and cytoskeletal proteins such as vinculin (26), talin (13), fimbrin (9), tensin (71), paxillin (68), zyxin (5), and ot-actinin (40). Biochemical studies have suggested several ways in which these proteins could anchor microfilaments to the cytoplasmic surface of the plasma membrane at focal contacts. Early studies suggested that particular isoforms of integrin ("CSAT'; 47) bound talin, and that this complex then bound vinculin (35; reviewed in 15). Later studies showed that integrins could also bind tx-actinin (53). Thus, integrin could anchor actin filaments indirectly through the actin-binding protein, tx-actinin, as well as through talin and vinculin. If both of these mechanisms are important for actin-membrane interactions, one would expect all these proteins to be concentrated at focal contacts.Structural studies also suggest two models for microfilament-membrane interactions at focal contacts. Focal contacts are several microns long, and individual actin filaments course over this entire distance before terminating (8). These filaments could bind to the membrane laterally as they approach their termini. In this case, vinculin, talin, integrin, and other proteins of focal contacts would be expected to concentrate at many points along the filament length. Alter- natively, filaments could attach only at their termini. In this case, the proteins of focal contacts would be expected to occur only at the ends of microfilaments.Predictions of the relationship between actin microfilaments and the membrane, and of the distribution of proteins at focal contacts, can be tested by ultrastructural methods coupled with immunocytochemistry. We exposed the cytoplasmic surfaces of ventral membrane by mechanical shearing, the...

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Section: Aggregates Of Membrane Particlessupporting

confidence: 53%

Structures linking microfilament bundles to the membrane at focal contacts

Samuelsson

Luther

Pumplin

et al. 1993

The Journal of Cell Biology

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“…15A, Moscow 121552, USSR brane. However, despite the intracellular localization of vinculin and talin at the microfilamentmembrane attachment sites and their interactions with integral membrane proteins and each other, talin and vinculin have not been shown to be actinbinding proteins [4,12,16]. Therefore, the role of these proteins in F-actin-membrane linkages is poorly understood.…”

Section: Introductionmentioning

confidence: 99%

“…The proteins talin and vinculin have been localized in specialized regions of plasma membrane-microfilament association and have been established as cytoskeletal markers of microfilament-membrane attachment sites of cultivated cells and cell-cell contact regions of smooth and striated muscle [l-11]. Vinculin and talin are able to form a tight complex [12]. Talin has been found to interact with an integral plasma membrane protein -fibronectin receptor [13,14].…”

Section: Introductionmentioning

confidence: 99%

Interaction of iodinated vinculin, metavinculin and α‐actinin with cytoskeletal proteins

1987

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Iodinated vinculin, metavinculin and ct-actinin were used to probe the interaction of these proteins with electrophoretically separated cytoskeletai proteins. Using the gel overlay technique, we detected strong binding of 12SI-vinculin and 12SI-metavinculin to ct-actinin, 175 kDa polypeptide, talin, vinculin and metavinculin themselves, and moderate binding to actin. 12sI-ct-actinin was capable of interacting with vinculin and metavinculin. The specific binding of 125-I-ct-actinin to vinculin and metavinculin immobilized on a polysterene surface was also demonstrated. We suggest that the ability of vinculin and ~-actinin to form a complex may be realized in microfilament-membrane linkages.Vinculin; Metavinculin; ct-Actinin; Microfilament-membrane interaction

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“…Talin in vitro binds vinculin [2], a-actinin [3], interacts with actin [4], promotes actin nucleation [5] and induces an increase in internal F-actin chain stiffness [6]. Further, talin is capable of interacting with phospholipid membranes.…”

Section: Introductionmentioning

confidence: 99%

Determination of the affinity of talin and vinculin to charged lipid vesicles: a light scatter study

1995

FEBS Letters

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Recent experimental findings have demonstrated that both talin and vinculin bind to phospholipids and insert into the hydrophobic region of lipid membranes. Here, we show that the light scatter method can be used for measuring the affinity of proteins to phospholipid membranes. Large unilamellar DNIPC/ DMPG vesicles were produced by the extrusion technique (LUVETs). We have used repeated heating/cooling scans between 15°C and 35°C to ensure protein-lipid interaction/insertion. A molar affinity of talin, K = 2.9 x 104 M -1 and of vinculin, K = 3.3 × 105 M -1 to lipid vesicles, respectively, was determined from the plot; light scatter signal at 380 nm against protein concentrations by fitting the term, In (Ioll -1) = A -K x c to the data.

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An interaction between vinculin and talin

Cited by 426 publications

References 18 publications

Structures linking microfilament bundles to the membrane at focal contacts

Structures linking microfilament bundles to the membrane at focal contacts

Interaction of iodinated vinculin, metavinculin and α‐actinin with cytoskeletal proteins

Determination of the affinity of talin and vinculin to charged lipid vesicles: a light scatter study

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