Uncovering Principles That Control Septin-Septin Interactions
Uncovering Principles That Control Septin-Septin Interactions
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DOI：
10.1074/jbc.m112.387464
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发表时间：
2012-08-31
影响因子：
4.8
通讯作者：
Trimble, William S.
中科院分区：
文献类型：
--
作者：
Kim, Moshe S.;Froese, Carol D.;Trimble, William S.
Septins comprise a conserved family of GTPases important in cytokinesis. These proteins polymerize into filaments from rod-shaped heteromeric septin complexes. Septins interact with one another at two interfaces (NC and G) that alternate within the complex. Here, we show that small mutations at the N terminus greatly enhance the formation of SEPT2 homopolymers. Taking advantage of this mutation to examine polymer formation using SEPT2 alone, we show that both NC and G interfaces are required for filament formation. However, co-expression of wild type SEPT2 with SEPT2 containing mutations at either NC or G interfaces revealed that only the NC mutant suppressed filament formation. NC mutants are able to interact with one another at putative Ginterfaces, whereas G mutants fail to interact at NC interfaces. In addition, all promiscuous septin pair-wise interactions occur at the G interface. These findings suggest that G interface interactions must occur before NC interactions during polymer formation.
