Key result
Vinculin and metavinculin oligomerization and interactions with F-actin play important roles in cellular adhesions and scaffolding functions.
This review highlights the structural and functional differences between vinculin and metavinculin oligomers in mediating cell adhesion and F-actin bundling.
Vinculin oligomerization may bolster adhesion scaffolding; leaves open its role in force sensing and cardiac applications.
Vinculin, and its splice variant metavinculin, are scaffolding proteins that localize to cellular adhesions. Vinculin is a key player in mediating cell adhesion, motility, and cellular response to force. In the past decade, a number of new studies have evaluated the importance of vinculin oligomers, especially in their role of bundling F-actin. Emerging evidence also suggests that vinculin oligomerization is important for vinculin's scaffolding function. Here we describe the latest findings on vinculin's interaction with F-actin and we clarify the different known vinculin oligomers. Differences in these functions between vinculin and metavinculin provide key insights to the structure and function of these oligomers, and should guide further studies.
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Thompson et al. (2013) reported a review. Vinculin and metavinculin was evaluated. Vinculin and metavinculin oligomerization and interactions with F-actin play important roles in cellular adhesions and scaffolding functions.
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