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KMID : 0578320080250030385
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Molecules and Cells
2008 Volume.25 No. 3 p.385 ~ p.389
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GTP Binding Is Required for SEPT12 to Form Filaments and to Interact with SEPT11
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Ding Xiangming
Wan Bo
Yu Long
Yu Wenbo
Liu Ming
Chen Fang
Shen ShuQing
Cao Lihuan
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Abstract
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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 GTP-binding 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.
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KEYWORD
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Co-localization, GTP-binding Domain, Protein Interaction, Septin, Subcellular Localization
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