Phosphatidyl inositol polyphosphate binding to the mammalian septin H5 is modulated by GTP

被引:235
作者
Zhang, JS
Kong, C
Xie, H
McPherson, PS
Grinstein, S
Trimble, WS [1 ]
机构
[1] Univ Toronto, Hosp Sick Children, Dept Biochem, Cell Biol Program, Toronto, ON M5G 1X8, Canada
[2] McGill Univ, Montreal Neurol Inst, Dept Neurol & Neurosurg, Montreal, PQ H3A 2B4, Canada
基金
美国国家卫生研究院; 英国医学研究理事会;
关键词
D O I
10.1016/S0960-9822(00)80115-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Background: Septins are members of a conserved family of GTPases found in organisms as diverse as budding yeast and mammals. In budding yeast, septins form hetero-oligomeric filaments that lie adjacent to the membrane at the mother-bud neck, whereas in mammals, they concentrate at the cleavage furrow of mitotic cells; in both cases, septins provide a required function for cytokinesis. What directs the location and determines the stability of septin filaments, however, remains unknown. Results: Here we show that the mammalian septin H5 is associated with the plasma membrane and specifically binds the phospholipids phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P-2) and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P-3). Deletion analysis revealed that this binding occurs at a site rich in basic residues that is conserved in most septins and is located adjacent to the GTP-binding motif. Phosphoinositide binding was inhibited by mutations within this motif and was also blocked by agents known to associate with PtdInsP(2) or by a peptide corresponding to the predicted PtdInsP(2)-binding sequence of H5. GTP binding and hydrolysis by H5 significantly reduced its PtdInsP(2)-binding capability. Treatment of cells with agents that occluded, dephosphorylated or degraded PtdInsP(2) altered the appearance and localization of H5. Conclusions: These results indicate that the interaction of septins with PtdInsP(2) might be an important cellular mechanism for the spatial and temporal control of septin accumulation. (C) 1999 Elsevier Science Ltd. All rights reserved.
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收藏
页码:1458 / 1467
页数:10
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