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GTP Binding Is Required for SEPT12 to Form Filaments and to Interact with SEPT11
Xiangming Ding,Wenbo Yu,Ming Liu,ShuQing Shen,Fang Chen,Lihuan Cao,Bo Wan,Long Yu 한국분자세포생물학회 2008 Molecules and cells Vol.25 No.3
Septins are a family of filament-forming GTP-binding proteins involved in a variety of cellular process such as cytokinesis, exocytosis, and membrane dynamics. Here we report the biochemical and immunocytochemical characterization of a recently identified mammalian septin, SEPT12. SEPT12 binds GTP in vitro, and a mutation (Gly56 to Asn) in the GTPbinding motif abolished binding. Immunocytochemical analysis revealed that wild-type SEPT12 formed filamentous structures when transiently expressed in Hela cells whereas SEPT12G56A generated large aggregates. In addition, wild-type SEPT12 failed to form filaments when coexpressed with SEPT12G56A. We also observed that GTP-binding by SEPT12 is required for interaction with SEPT11 but not with itself.