Direct dynamin-actin interactions regulate the actin cytoskeleton

被引：181

作者：

Gu, Changkyu ^{[1
,2
]}

Yaddanapudi, Suma ^{[1
,2
]}

Weins, Astrid ^{[3
]}

Osborn, Teresia ^{[4
]}

Reiser, Jochen ^{[5
]}

Pollak, Martin ^{[3
]}

Hartwig, John ^{[4
]}

Sever, Sanja ^{[1
,2
]}

机构：

[1] Harvard Univ, Sch Med, Div Nephrol, Dept Med, Charlestown, MA 02129 USA

[2] Massachusetts Gen Hosp, Charlestown, MA 02129 USA

[3] Beth Israel Deaconess Med Ctr, Div Nephrol, Boston, MA 02215 USA

[4] Brigham & Womens Hosp, Translat Med Div, Boston, MA 02115 USA

[5] Univ Miami, Div Nephrol & Hypertens, Coral Gables, FL 33124 USA

来源：

EMBO JOURNAL | 2010年 / 29卷 / 21期

关键词：

actin; cytoskeleton; dynamin; BARBED ENDS; LEADING-EDGE; GELSOLIN; GTPASE; PURIFICATION; NUCLEATION; MECHANISM; MOTILITY; DOMAIN; FILAMENTS;

D O I：

10.1038/emboj.2010.249

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：

The large GTPase dynamin assembles into higher order structures that are thought to promote endocytosis. Dynamin also regulates the actin cytoskeleton through an unknown, GTPase-dependent mechanism. Here, we identify a highly conserved site in dynamin that binds directly to actin filaments and aligns them into bundles. Point mutations in the actin-binding domain cause aberrant membrane ruffling and defective actin stress fibre formation in cells. Short actin filaments promote dynamin assembly into higher order structures, which in turn efficiently release the actin-capping protein (CP) gelsolin from barbed actin ends in vitro, allowing for elongation of actin filaments. Together, our results support a model in which assembled dynamin, generated through interactions with short actin filaments, promotes actin polymerization via displacement of actin-CPs. The EMBO Journal (2010) 29, 3593-3606. doi:10.1038/emboj.2010.249; Published online 8 October 2010

引用

页码：3593 / 3606

页数：14

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