期刊
MOLECULAR CELL
卷 27, 期 2, 页码 197-213出版社
CELL PRESS
DOI: 10.1016/j.molcel.2007.05.033
关键词
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资金
- NCI NIH HHS [R01 CA109699-03, CA109699, R01 CA109699-04, R01 CA109699-01, R01 CA109699-02, R01 CA109699-05, R01 CA109699] Funding Source: Medline
- NIGMS NIH HHS [R01 GM058486-06, R01 GM058486-05, R01 GM058486-07, R01 GM058486, GM58486, R01 GM058486-08] Funding Source: Medline
- NINDS NIH HHS [R01 NS054022-02, R01 NS054022] Funding Source: Medline
Histone deacetylase 6 (HDAC6) is a tubulin-specific deacetylase that regulates microtubuledependent cell movement. In this study, we identify the F-actin-binding protein cortactin as a HDAC6 substrate. We demonstrate that HDAC6 binds cortactin and that overexpression of HDAC6 leads to hypoacetylation of cortactin, whereas inhibition of HDAC6 activity leads to cortactin hyperacetylation. HDAC6 alters the ability of cortactin to bind F-actin by modulating a charge patch in its repeat region. Introduction of charge-preserving or charge-neutralizing mutations in this cortactin repeat region correlates with the gain or loss of F-actin binding ability, respectively. Cells expressing a charge-neutralizing cortactin mutant were less motile than control cells or cells expressing a charge-preserving mutant. These findings suggest that, in addition to its role in microtubuledependent cell motility, HDAC6 influences actin-dependent cell motility by altering the acetylation status of cortactin, which, in turn, changes the F-actin binding activity of cortactin.
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