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J Biol Chem, Vol. 274, Issue 12, 7833-7840, March 19, 1999
,
From the Department of Morphology, COPII proteins are necessary to generate
secretory vesicles at the endoplasmic reticulum. In yeast, the Sec24p
protein is the only COPII component in which two close orthologues have
been identified. By using gene knock-out in yeast, we found that the absence of one of these Sec24 orthologues resulted in a selective secretion defect for a subset of proteins released into the medium. Data base searches revealed the existence of an entire family of
Sec24-related proteins in humans, worms, flies, and plants. We
identified and cloned two new human cDNAs encoding proteins homologous to yeast Sec24p, in addition to two human cDNAs already present within the data bases. The entire Sec24 family identified to
date is characterized by clusters of highly conserved residues within
the 2/3 carboxyl-terminal domain of all the proteins and a divergent
amino terminus domain. Human (h) Sec24 orthologues co-immunoprecipitate
with hSec23Ap and migrate as a complex by size exclusion
chromatography. Immunofluorescence microscopy confirmed that these
proteins co-localize with hSec23p and hSec13p. Together, our data
suggest that in addition to its role in the shaping up of the vesicle,
the Sec23-24p complex may be implicated in cargo selection and concentration.
Institute of
Biology and Chemistry of Proteins, CNRS, Lyon, 69367 France
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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