January 1, 1985Journal of Cellular Biochemistry
Molecular shape and self‐association of vinculin and metavinculin
Key result
Vinculin and metavinculin have globular heads and rod-shaped tails forming multimers, while talin is an elongated, flexible molecule in high ionic strength buffers.
Population
Vinculin (130,000-dalton), metavinculin (150,000-dalton), and talin proteins
Design
Preclinical
Authors
Discussion
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Implication
Vinculin-metavinculin multimers extend adhesion protein models; leaves open cardiac mechanotransduction roles pending functional validation.
Structured PICO
P
Population
Vinculin (130,000-dalton), metavinculin (150,000-dalton), and talin proteins
E
Exposure
Rotary shadowing and electron microscopy
O
Outcome
Molecular shape and self-association
Provides structural characterization of the adhesion plaque proteins vinculin, metavinculin, and talin, demonstrating their multimerization capabilities.
Cite This Study
Molony et al. (1985) studied this question. Vinculin, metavinculin, and talin was evaluated on Molecular shape and self-association. Vinculin and metavinculin have globular heads and rod-shaped tails forming multimers, while talin is an elongated, flexible molecule in high ionic strength buffers.