Molecules and Cells

Korean Society for Molecular and Cellular Biology (한국분자세포생물학회)
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GTP Binding Is Required for SEPT12 to Form Filaments and to Interact with SEPT11

  • Ding, Xiangming (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University) ;
  • Yu, Wenbo (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University) ;
  • Liu, Ming (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University) ;
  • Shen, ShuQing (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University) ;
  • Chen, Fang (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University) ;
  • Cao, Lihuan (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University) ;
  • Wan, Bo (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University) ;
  • Yu, Long (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University)
  • Received : 2007.08.16
  • Accepted : 2007.11.26
  • Published : 2008.05.31
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Abstract

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 $SEPT12^{G56A}$ generated large aggregates. In addition, wild-type SEPT12 failed to form filaments when coexpressed with $SEPT12^{G56A}$. We also observed that GTP-binding by SEPT12 is required for interaction with SEPT11 but not with itself.

Keywords

Acknowledgement

Supported by : National Natural Science Foundation of China

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