Coronin 2A regulates a subset of focal-adhesion-turnover events through the cofilin pathway.

Abstract:

:Coronins are conserved F-actin-binding proteins that are important for motility and actin dynamics. Unlike type I coronins, coronin 2A localizes to stress fibers and some focal adhesions, and is excluded from the leading edge. Depletion of coronin 2A in MTLn3 cells decreases cell motility and turnover of focal adhesions. Surprisingly, none of the pathways known to regulate focal-adhesion turnover are affected by depletion of coronin 2A. Depletion of coronin 2A does, however, increase phospho-cofilin, suggesting that misregulation of cofilin might affect adhesion dynamics. Slingshot-1L, a cofilin-activating phosphatase, localizes to focal adhesions and interacts with coronin 2A. Depletion of coronin 2A reduces cofilin activity at focal adhesions, as measured by barbed-end density and actin FRAP. In both fixed cells and live cells, cofilin localizes to the proximal end of some focal adhesions. Although expression of wild-type cofilin in coronin-2A-depleted cells has no major effect on focal-adhesion dynamics, expression of an active mutant of cofilin bypasses the defects in cell motility and focal-adhesion disassembly. These results implicate both coronin 2A and cofilin as factors that can regulate a subset of focal-adhesion-turnover events.

journal_name

J Cell Sci

journal_title

Journal of cell science

authors

Marshall TW,Aloor HL,Bear JE

doi

10.1242/jcs.051482

subject

Has Abstract

pub_date

2009-09-01 00:00:00

pages

3061-9

issue

Pt 17

eissn

0021-9533

issn

1477-9137

pii

jcs.051482

journal_volume

122

pub_type

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