The Proline/Arginine-Rich Domain Is a Major Determinant of Dynamin Self-Activation

被引：11

作者：

Barylko, Barbara ^{[1
]}

Wang, Lei ^{[1
]}

Binns, Derk D. ^{[1
]}

Ross, Justin A. ^{[2
]}

Tassin, Tara C. ^{[1
]}

Collins, Katie A. ^{[1
]}

Jameson, David M. ^{[2
]}

Albanesi, Joseph P. ^{[1
]}

机构：

[1] Univ Texas SW Med Ctr Dallas, Dept Pharmacol, Dallas, TX 75235 USA

[2] Univ Hawaii, John A Burns Sch Med, Dept Cell & Mol Biol, Honolulu, HI 96813 USA

来源：

BIOCHEMISTRY | 2010年 / 49卷 / 50期

基金：

美国国家卫生研究院;

关键词：

GTPASE; MECHANISM;

D O I：

10.1021/bi101343p

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：

Dynamins induce membrane vesiculation during endocytosis and Golgi budding in a process that requires assembly-dependent GTPase activation. Brain-specific dynamin 1 has a weaker propensity to self-assemble and self-activate than ubiquitously expressed dynamin 2. Here we show that dynamin 3, which has important functions in neuronal synapses, shares the self-assembly and GTPase activation characteristics of dynamin 2. Analysis of dynamin hybrids and of dynamin I dynamin 2 and dynamin 1 dynamin 3 heteropolymers reveals that concentration-dependent GTPase activation is suppressed by the C-terminal proline/arginine-rich domain of dynamin 1. Dynamin proline/arginine-rich domains also mediate interactions with SH3 domain-containing proteins and thus regulate both self-association and heteroassociation of dynamins.

引用

页码：10592 / 10594

页数：3

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