The Arf GTPase-activating Protein, ASAP1, Binds Nonmuscle Myosin 2A to Control Remodeling of the Actomyosin Network

被引：27

作者：

Chen, Pei-Wen ^{[1
,5
]}

Jian, Xiaoying ^{[1
]}

Heissler, Sarah M. ^{[3
]}

Le, Kang ^{[4
]}

Luo, Ruibai ^{[1
]}

Jenkins, Lisa M. ^{[2
]}

Nagy, Attila ^{[3
]}

Moss, Joel ^{[4
]}

Sellers, James R. ^{[3
]}

Randazzo, Paul A. ^{[1
]}

机构：

[1] NCI, Lab Cellular & Mol Biol, Bethesda, MD 20892 USA

[2] NCI, Cell Biol Lab, Bethesda, MD 20892 USA

[3] NHLBI, Lab Mol Physiol, NIH, Bldg 10, Bethesda, MD 20892 USA

[4] NHLBI, Cardiovasc & Pulm Branch, NIH, Bldg 10, Bethesda, MD 20892 USA

[5] Grinnell Coll, Dept Biol, Grinnell, IA 50112 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2016年 / 291卷 / 14期

基金：

美国国家卫生研究院;

关键词：

CIRCULAR DORSAL RUFFLES; ACTIN CYTOSKELETON; CELL-MIGRATION; ANIONIC PHOSPHOLIPIDS; FOCAL ADHESIONS; PHOSPHORYLATION; DOMAIN; ASSOCIATION; EXPRESSION; PODOSOMES;

D O I：

10.1074/jbc.M115.701292

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：

ASAP1 regulates F-actin-based structures and functions, including focal adhesions (FAs) and circular dorsal ruffles (CDRs), cell spreading and migration. ASAP1 function requires its N-terminal BAR domain. We discovered that nonmuscle myosin 2A (NM2A) directly bound the BAR-PH tandem of ASAP1 in vitro. ASAP1 and NM2A co-immunoprecipitated and colocalized in cells. Knockdown of ASAP1 reduced colocalization of NM2A and F-actin in cells. Knockdown of ASAP1 or NM2A recapitulated each other's effects on FAs, cell migration, cell spreading, and CDRs. The NM2A-interacting BAR domain contributed to ASAP1 control of cell spreading and CDRs. Exogenous expression of NM2A rescued the effect of ASAP1 knockdown on CDRs but ASAP1 did not rescue NM2A knockdown defect in CDRs. Our results support the hypothesis that ASAP1 is a positive regulator of NM2A. Given other binding partners of ASAP1, ASAP1 may directly link signaling and the mechanical machinery of cell migration.

引用

页码：7517 / 7526

页数：10

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