Interaction with the IQ3 motif of myosin-10 is required for calmodulin-like protein-dependent filopodial extension

被引：9

作者：

Bennett, Richard D. ^{[1
,2
]}

Caride, Ariel J. ^{[1
]}

Mauer, Amy S. ^{[1
]}

Strehler, Emanuel E. ^{[1
]}

机构：

[1] Mayo Clin, Coll Med, Dept Biochem & Mol Biol, Rochester, MN 55905 USA

[2] Mayo Grad Sch, Cell Biol & Genet Program, Rochester, MN 55905 USA

来源：

FEBS LETTERS | 2008年 / 582卷 / 16期

关键词：

calmodulin-like protein; filopodia; IQ domain; motility; myosin-10;

D O I：

10.1016/j.febslet.2008.05.051

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Calmodulin-like protein (CLP) is a specific light chain of unconventional myosin-10 (Myo10) and enhances Myo10-dependent filopodial extension. Here we show that phenylalanine-795 in the third IQ domain (IQ3) of Myo10 is critical for CLP binding. Remarkably, mutation of F795 to alanine had little effect on calmodulin binding to IQ3. Fluorescence microscopy and time-lapse video microscopy showed that HeLa cells expressing CLP and transiently transfected with GFP-Myo10-F795A exhibited significantly shorter filopodia and decreased intrafilopodial motility compared to wildtype GFP-Myo10-transfected cells. Thus, F795 represents a unique anchor for CLP and is essential for CLP-mediated Myo10 function in filopodial extension and motility.

引用

页码：2377 / 2381

页数：5

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