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The proline/arginine-rich domain is a major determinant of dynamin self-activation.

ABSTRACT: 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 1-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.

SUBMITTER: Barylko B

PROVIDER: S-EPMC3017478 | biostudies-literature | 2010 Dec

REPOSITORIES: biostudies-literature

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The proline/arginine-rich domain is a major determinant of dynamin self-activation.

Barylko Barbara B Wang Lei L Binns Derk D DD Ross Justin A JA Tassin Tara C TC Collins Katie A KA Jameson David M DM Albanesi Joseph P JP

Biochemistry 20101123 50

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 1-dynamin 2 and dynamin 1-dynamin 3 ...[more]

PMID: 21082776

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