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

Barbara Barylko, Lei Wang, Derk D. Binns, Justin A. Ross, Tara C. Tassin, Katie A. Collins, David M. Jameson, Joseph P. Albanesi

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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.

Original languageEnglish (US)
Pages (from-to)10592-10594
Number of pages3
JournalBiochemistry
Volume49
Issue number50
DOIs
StatePublished - Dec 21 2010

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ASJC Scopus subject areas

  • Biochemistry

Cite this

Barylko, B., Wang, L., Binns, D. D., Ross, J. A., Tassin, T. C., Collins, K. A., Jameson, D. M., & Albanesi, J. P. (2010). The proline/arginine-rich domain is a major determinant of dynamin self-activation. Biochemistry, 49(50), 10592-10594. https://doi.org/10.1021/bi101343p