Sec35p, a Novel Peripheral Membrane Protein, Is Required for ER to Golgi Vesicle Docking
Autor: | Charles Barlowe, Susan M. VanRheenen, Xiaochun Cao, Vladimir Lupashin, M. Gerard Waters |
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Rok vydání: | 1998 |
Předmět: |
Saccharomyces cerevisiae Proteins
Vesicle docking Molecular Sequence Data Coated Vesicles Vesicular Transport Proteins Golgi Apparatus Coated vesicle Saccharomyces cerevisiae Biology Endoplasmic Reticulum Vesicle tethering GTP Phosphohydrolases Fungal Proteins 03 medical and health sciences symbols.namesake Munc18 Proteins 0302 clinical medicine GTP-Binding Proteins Amino Acid Sequence Cloning Molecular DNA Fungal Secretory pathway 030304 developmental biology Golgi vesicle docking 0303 health sciences Base Sequence Conserved oligomeric Golgi complex Membrane Proteins Biological Transport Articles Cell Biology Golgi apparatus Cell biology Secretory protein rab GTP-Binding Proteins symbols Carrier Proteins Gene Deletion 030217 neurology & neurosurgery |
Zdroj: | The Journal of Cell Biology |
ISSN: | 1540-8140 0021-9525 |
DOI: | 10.1083/jcb.141.5.1107 |
Popis: | SEC35 was identified in a novel screen for temperature-sensitive mutants in the secretory pathway of the yeast Saccharomyces cerevisiae (Wuestehube et al., 1996. Genetics . 142:393–406). At the restrictive temperature, the sec35-1 strain exhibits a transport block between the ER and the Golgi apparatus and accumulates numerous vesicles. SEC35 encodes a novel cytosolic protein of 32 kD, peripherally associated with membranes. The temperature-sensitive phenotype of sec35-1 is efficiently suppressed by YPT1 , which encodes the rab-like GTPase required early in the secretory pathway, or by SLY1-20 , which encodes a dominant form of the ER to Golgi target -SNARE–associated protein Sly1p. Weaker suppression is evident upon overexpression of genes encoding the vesicle-SNAREs SEC22 , BET1 , or YKT6 . The cold-sensitive lethality that results from deleting SEC35 is suppressed by YPT1 or SLY1-20 . These genetic relationships suggest that Sec35p acts upstream of, or in conjunction with, Ypt1p and Sly1p as was previously found for Uso1p. Using a cell-free assay that measures distinct steps in vesicle transport from the ER to the Golgi, we find Sec35p is required for a vesicle docking stage catalyzed by Uso1p. These genetic and biochemical results suggest Sec35p acts with Uso1p to dock ER-derived vesicles to the Golgi complex. |
Databáze: | OpenAIRE |
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