Insights into COPII coat nucleation from the structure of Sec23•Sar1 complexed with the active fragment of sec31

被引:182
作者
Bi, Xiping
Mancias, Joseph D.
Goldberg, Jonathan
机构
[1] Mem Sloan Kettering Canc Ctr, Howard Hughes Med Inst, New York, NY 10021 USA
[2] Mem Sloan Kettering Canc Ctr, Struct Biol Program, New York, NY 10021 USA
关键词
D O I
10.1016/j.devcel.2007.10.006
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The COPII vesicular coat forms on the endoplasmic reticulum from Sar1-GTP, Sec23/24 and Sec13/31 protein subunits. Here, we define the interaction between Sec23/24 center dot Sar1 and Sec13/31, involving a 40 residue Sec31 fragment. In the crystal structure of the ternary complex, Sec31 binds as an extended polypeptide across a composite surface of the Sec23 and Sar1-GTP molecules, explaining the step-wise character of Sec23/24 center dot Sar1 and Sec13/31 recruitment to the membrane. The Sec31 fragment stimulates GAP activity of Sec23/24, and a convergence of Sec3l and Sec23 residues at the Sar1 GTPase active site explains how GTP hydrolysis is triggered leading to COPII coat disassembly. The Sec31 active fragment is accommodated in a binding groove supported in part by Sec23 residue Phe380. Substitution of the corresponding residue F382L in human Sec23A causes cranio-lenticulo-sutural dysplasia, and we suggest that this mutation disrupts the nucleation of COPII coat proteins at endoplasmic reticulum exit sites.
引用
收藏
页码:635 / 645
页数:11
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