The chloride intracellular channel protein CLIC4 inhibits filopodium formation induced by constitutively active mutants of formin mDia2

FEBS Letters

article

Elisabetta Argenzio¹  Metello Innocenti² 

[1] Division of Cell Biology, The Netherlands Cancer Institute;Heidelberg University Biochemistry Center (BZH), Heidelberg University

关键词: actin;    CLIC4;    cytoskeleton;    filopodia;    formins;    mDia2;   

DOI  :  10.1002/1873-3468.13766

来源: John Wiley & Sons Ltd.

【 摘 要 】

Chloride intracellular channel 4 (CLIC4) functions in diverse actin-dependent processes. Upon Rho activation, CLIC4 reversibly translocates from the cytosol to the plasma membrane to regulate cell adhesion and migration. At the plasma membrane, CLIC4 counters the formation of filopodia, which requires actin assembly by the formin mammalian Diaphanous (mDia)2. To this end, mDia2 must be activated through conversion from the closed to the open conformation. Thus, CLIC4 could harness the activation or the open conformation of mDia2 to inhibit filopodium formation. Here, we find that CLIC4 silencing enhances the filopodia induced by two constitutively active mDia2 mutants. Furthermore, we report that CLIC4 binds the actin-regulatory region of mDia2 in vitro. These results suggest that CLIC4 modulates the activity of the open conformation of mDia2, shedding new light into how cells may control filopodia.

【 授权许可】

Unknown