Human homologues of yeast vacuolar protein sorting 29 and 35

被引:32
|
作者
Edgar, AJ
Polak, JM
机构
[1] Imperial Coll Sch Med, Dept Histochem, Div Investigat Sci, London W12 0NN, England
[2] Imperial Coll Sch Med, Tissue Engn Ctr, Div Investigat Sci, London W12 0NN, England
关键词
ABC transporters; carboxypeptidase Y; endocytic; lung; lysosome; mannose-6-phosphate receptor; PEP; secretory; sorting nexins; YfcE;
D O I
10.1006/bbrc.2000.3727
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In the yeast Saccharomyces cerevisiae, a membrane coat complex is required for endosome to Golgi retrograde transport. The vacuolar protein sorting proteins Vps29p, Vps35p, and Vps26p are required for prevacuolar/late endosome to Gels retrieval of the vacuolar hydrolase receptor Vps10p. They form a cargo recognition and concentration subcomplex, termed the inner shell of the retromer coat, prior to vesicle formation by the addition of the membrane-deforming outer shell. We have cloned the human and murine homologues of yeast Vps29p and the human homologue of Vps35p. They encode 182 and 796 residue proteins, with 43 and 29% identity to their respective yeast. The 10.5 kb, 5 exon, VPS29 gene is located on chromosome 12q24 and the 29.6 kb, 17 exon, VPS35 gene is on chromosome 16. In humans, Vps29p, Vps35p, and H beta 58, the homologue of Vps26p, may form an inner shell of the retromer coat similar to that found in yeast. (C) 2000 Academic Press.
引用
收藏
页码:622 / 630
页数:9
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