ESCRT公司
胞质分裂
中段
TSG101型
螺旋线圈
细胞生物学
内体
化学
异四聚体
生物
蛋白质亚单位
细胞分裂
生物化学
细胞内
细胞
小RNA
微泡
基因
作者
Hyung Ho Lee,Natalie Elia,Rodolfo Ghirlando,Jennifer Lippincott‐Schwartz,James H. Hurley
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:2008-10-24
卷期号:322 (5901): 576-580
被引量:233
标识
DOI:10.1126/science.1162042
摘要
The ESCRT (endosomal sorting complex required for transport) machinery is required for the scission of membrane necks in processes including the budding of HIV-1 and cytokinesis. An essential step in cytokinesis is recruitment of the ESCRT-I complex and the ESCRT-associated protein ALIX to the midbody (the structure that tethers two daughter cells) by the protein CEP55. Biochemical experiments show that peptides from ALIX and the ESCRT-I subunit TSG101 compete for binding to the ESCRT and ALIX-binding region (EABR) of CEP55. We solved the crystal structure of EABR bound to an ALIX peptide at a resolution of 2.0 angstroms. The structure shows that EABR forms an aberrant dimeric parallel coiled coil. Bulky and charged residues at the interface of the two central heptad repeats create asymmetry and a single binding site for an ALIX or TSG101 peptide. Both ALIX and ESCRT-I are required for cytokinesis, which suggests that multiple CEP55 dimers are required for function.
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