Sec24 Proteins and Sorting at the Endoplasmic Reticulum

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 result...

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Bibliographic Details
Published in:The Journal of biological chemistry 1999-03, Vol.274 (12), p.7833-7840
Main Authors: Pagano, Alessandra, Letourneur, François, Garcia-Estefania, David, Carpentier, Jean-Louis, Orci, Lelio, Paccaud, Jean-Pierre
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Arabidopsis
Biochemistry, Molecular Biology
Caenorhabditis elegans
Caenorhabditis elegans Proteins
Cells, Cultured
Cloning, Molecular
DNA - metabolism
Drosophila melanogaster
Endoplasmic Reticulum - physiology
Humans
Life Sciences
Mannose-Binding Lectins
Membrane Proteins - genetics
Membrane Proteins - metabolism
Membrane Proteins - physiology
Microscopy, Fluorescence
Molecular Sequence Data
Proteins - genetics
Proteins - physiology
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Sequence Alignment
Vesicular Transport Proteins
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.274.12.7833