Self- and actin-templated assembly of mammalian septins
Self- and actin-templated assembly of mammalian septins
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DOI：
10.1016/s1534-5807(02)00366-0
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发表时间：
2002-12-01
影响因子：
11.8
通讯作者：
Mitchison, TJ
中科院分区：
文献类型：
--
作者：
Kinoshita, M;Field, CM;Mitchison, TJ
septin是细胞分裂和皮质组织所需的聚合gtp酶。它们靶向和聚集在特定细胞区域的原理尚不清楚。我们发现哺乳动物细胞中的septin在沿着肌动蛋白束和细胞质环的线性组织之间切换，直径约为0.6微米。重组隔素复合体自我组装成类似于细胞中的环。在肌动蛋白束的线性组织中加入了一种接头蛋白，苯胺。细胞中septin组织的扰动是通过表达与septin相互作用的氨酰胺片段或通过siRNA耗尽septin导致肌动蛋白束的丢失。我们的结论是，septin单独自组装成环，接头蛋白将septin招募到肌动蛋白束中，并且septin帮助组织这些束。
Septins are polymerizing GTPases required for cytokinesis and cortical organization. The principles by which they are targeted to, and assemble at, specific cell regions are unknown. We show that septins in mammalian cells switch between a linear organization along actin bundles and cytoplasmic rings, approximately 0.6 mum in diameter. A recombinant septin complex self-assembles into rings resembling those in cells. Linear organization along actin bundles was reconstituted by adding an adaptor protein, anillin. Perturbation of septin organization in cells by expression of a septin-interacting fragment of anillin or by septin depletion via siRNA causes loss of actin bundles. We conclude that septins alone self-assemble into rings, that adaptor proteins recruit septins to actin bundles, and that septins help organize these bundles.