beta′-COP, a novel subunit of coatomer.
نویسندگان
چکیده
منابع مشابه
zeta-COP, a subunit of coatomer, is required for COP-coated vesicle assembly
cDNA encoding the 20-kD subunit of coatomer, zeta-COP, predicts a protein of 177-amino acid residues, similar in sequence to AP17 and AP19, subunits of the clathrin adaptor complexes. Polyclonal antibody directed to zeta-COP blocks the binding of coatomer to Golgi membranes and prevents the assembly of COP-coated vesicles on Golgi cisternae. Unlike other coatomer subunits (beta-, beta'-, gamma-...
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We isolated a novel yeast α-COP mutant, ret1-3, in which α-COP is degraded after cells are shifted to a restrictive temperature. ret1-3 cells cease growth at 28°C and accumulate the ER precursor of carboxypeptidase Y (p1CPY). In a screen for high copy suppressors of these defects, we isolated the previously unidentified yeast ε-COP gene. ε-COP (Sec28p) overproduction suppresses the defects of r...
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15 صفحه اولArchitecture of coatomer: molecular characterization of delta-COP and protein interactions within the complex
Coatomer is a cytosolic protein complex that forms the coat of COP I-coated transport vesicles. In our attempt to analyze the physical and functional interactions between its seven subunits (coat proteins, [COPs] alpha-zeta), we engaged in a program to clone and characterize the individual coatomer subunits. We have now cloned, sequenced, and overexpressed bovine alpha-COP, the 135-kD subunit o...
متن کاملScyl1 scaffolds class II Arfs to specific subcomplexes of coatomer through the c-COP appendage domain
Coatomer (COPI)-coated vesiclesmediatemembrane trafficking in the early secretory pathway. There are at least three subclasses of COPI coats and two classes of Arf GTPases that couple COPI coat proteins to membranes. Whether mechanisms exist to link specific Arfs to specific COPI subcomplexes is unknown. We now demonstrate that Scy1-like protein 1 (Scyl1), a member of the Scy1-like family of ca...
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ژورنال
عنوان ژورنال: The EMBO Journal
سال: 1993
ISSN: 0261-4189
DOI: 10.1002/j.1460-2075.1993.tb05945.x