Focal adhesions (FAs) are macromolecular complexes that connect the actin cytoskeleton to the extracellular matrix. Regulated assembly and disassembly of FAs is essential for cell migration and thus important for many physiological processes, such as wound healing, cancer metastasis and embryonic development. However, FA disassembly is only poorly understood, although a number of factors, such as FA kinase (FAK) and paxillin, are known to be involved. On page 3928, Pradeep Uchil, Walther Mothes and co-workers identify the tripartite motif (TRIM)/RBCC protein family member TRIM15 as a novel component of FAs to which it is recruited through interactions with paxillin. They show that TRIM15 localises to FAs at an early stage of their assembly and remains stably bound to them, thus forming part of the FA scaffold. Consequently, cells that lack TRIM15 have impairments in cell migration and exhibit defects in FA disassembly, suggesting that TRIM15 regulates FA dynamics at the disassembly step. Furthermore, the authors are able to pinpoint endocytosis of activated β1 integrin, a key event in FA disassembly, as the step that is delayed in TRIM15-depleted cells. Indeed, overexpression of factors that control integrin endocytosis partially rescue the migration defect inTRIM15-knockdown cells. Thus, taken together, the data presented here describe TRIM15 as a novel FA component that regulates FA turnover by facilitating local FA disassembly.
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IN THIS ISSUE| 15 September 2014
TRIM15 in focal adhesion disassembly
Online Issn: 1477-9137
Print Issn: 0021-9533
© 2014. Published by The Company of Biologists Ltd
J Cell Sci (2014) 127 (18): e1805.
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TRIM15 in focal adhesion disassembly. J Cell Sci 15 September 2014; 127 (18): e1805. doi:
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