Publication Date:
2001-11-17
Description:
Proteins are transported from the endoplasmic reticulum (ER) in vesicles formed by coat protein complex II (COPII). Soluble secretory proteins are thought to leave the ER in these vesicles by "bulk flow" or through recognition by hypothetical shuttling receptors. We found that Erv29p, a conserved transmembrane protein, was directly required for packaging glycosylated pro-alpha-factor (gpalphaf) into COPII vesicles in Saccharomyces cerevisiae. Further, an Erv29p-gpalphaf complex was isolated from ER-derived transport vesicles. In vivo, export of gpalphaf from the ER was saturable and depended on the expression level of Erv29p. These results indicate that membrane receptors can link soluble cargo proteins to the COPII coat.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Belden, W J -- Barlowe, C -- New York, N.Y. -- Science. 2001 Nov 16;294(5546):1528-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11711675" target="_blank"〉PubMed〈/a〉
Keywords:
COP-Coated Vesicles/*metabolism
;
Carboxypeptidases/metabolism
;
Cathepsin A
;
Cross-Linking Reagents
;
Dimerization
;
Endoplasmic Reticulum/*metabolism
;
Glycosylation
;
Golgi Apparatus/metabolism
;
Kinetics
;
Membrane Proteins/chemistry/genetics/isolation & purification/*metabolism
;
Membrane Transport Proteins
;
Peptides/chemistry/genetics/isolation & purification/*metabolism
;
Precipitin Tests
;
Protein Folding
;
Protein Precursors/chemistry/isolation & purification/*metabolism
;
Protein Transport
;
Qb-SNARE Proteins
;
Saccharomyces cerevisiae/genetics/*metabolism/ultrastructure
;
*Saccharomyces cerevisiae Proteins
;
Solubility
;
Succinimides/pharmacology
;
*Vesicular Transport Proteins
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
Permalink
