GRP94, an ER chaperone with protein and peptide binding properties

被引:160
作者
Argon, Y
Simen, BB
机构
[1] Univ Chicago, Dept Pathol, Chicago, IL 60637 USA
[2] Univ Chicago, Dept Pharmacol & Physiol Sci, Chicago, IL 60637 USA
基金
美国国家卫生研究院;
关键词
antigen presentation; HSP90; peptide binding; protein folding; secretory pathway;
D O I
10.1006/scdb.1999.0320
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
GRP94 is the ER representative of the HSP90 family of stress-induced proteins. It binds to a limited number of proteins in the secretory pathway, apparently by recognizing advanced folding intermediates or incompletely assembled proteins. GRP94 also binds peptides and can act as a tumor vaccine, delivering the peptides for presentation to T lymphocytes. Here, we review the current data about GRP94 and propose a structural model that integrates the biochemical data and known functions of the protein.
引用
收藏
页码:495 / 505
页数:11
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