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Published 10 December 2001. doi:10.1083/jcb.200106039
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© The Rockefeller University Press, 0021-9525/2001/12/937 $5.00
The Journal of Cell Biology, Volume 155, Number 6, December 10, 2001 937-948

Article

Crystal structure of Sar1-GDP at 1.7 Å resolution and the role of the NH2 terminus in ER export



Mingdong Huang1,2, Jacques T. Weissman1, Sophie Béraud-Dufour1, Peng Luan1, Chenqian Wang1, Wei Chen1, Meir Aridor1, Ian A. Wilson2,4 and William E. Balch1,2,3

1 Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92130
2 Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92130
3 The Institute of Childhood and Neglected Diseases, The Scripps Research Institute, La Jolla, CA 92130
4 The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92130

Address correspondence to William Balch, Dept. of Cell Biology, IMM-11, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037-1092. Tel.: (858) 784-2310. Fax: (858) 784-9706. E-mail: webalch{at}scripps.edu

The Sar1 GTPase is an essential component of COPII vesicle coats involved in export of cargo from the ER. We report the 1.7-Å structure of Sar1 and find that consistent with the sequence divergence of Sar1 from Arf family GTPases, Sar1 is structurally distinct. In particular, we show that the Sar1 NH2 terminus contains two regions: an NH2-terminal extension containing an evolutionary conserved hydrophobic motif that facilitates membrane recruitment and activation by the mammalian Sec12 guanine nucleotide exchange factor, and an {alpha}1' amphipathic helix that contributes to interaction with the Sec23/24 complex that is responsible for cargo selection during ER export. We propose that the hydrophobic Sar1 NH2-terminal activation/recruitment motif, in conjunction with the {alpha}1' helix, mediates the initial steps in COPII coat assembly for export from the ER.

Key Words: Sar1; ER; COPII; vesicle transport; Golgi


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