期刊
NATURE CELL BIOLOGY
卷 16, 期 6, 页码 558-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb2975
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资金
- National Institutes of Health [R01 GM079139]
- American Heart Association post doctoral fellowship [10 POST3870021]
- Research Facilities Improvement Program [C06 RR16490]
- National Center for Research Resources of the National Institutes of Health [S10 RR26758]
Turnover of integrin-based focal adhesions (FAs) with the extracellular matrix (ECM) is essential for coordinated cell movement. In collectively migrating human keratinocytes, FAs assemble near the leading edge, grow and mature as a result of contractile forces and disassemble underneath the advancing cell body. We report that clustering of microtubule-associated CLASP1 and CLASP2 proteins around FAs temporally correlates with FA turnover. CLASPs and LL5 beta (also known as PHLDB2), which recruits CLASPs to FAs, facilitate FA disassembly. CLASPs are further required for FA-associated ECM degradation, and matrix metalloprotease inhibition slows FA disassembly similarly to CLASP or PHLDB2 (LL5 beta) depletion. Finally, CLASP-mediated microtubule tethering at FAs establishes an FA-directed transport pathway for delivery, docking and localized fusion of exocytic vesicles near FAs. We propose that CLASPs couple microtubule organization, vesicle transport and cell interactions with the ECM, establishing a local secretion pathway that facilitates FA turnover by severing cell-matrix connections.
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