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  Biochemical and genetic evidence for the involvement of yeast Ypt6-GTPase in protein retrieval to different Golgi compartments

Luo, Z. L., & Gallwitz, D. (2003). Biochemical and genetic evidence for the involvement of yeast Ypt6-GTPase in protein retrieval to different Golgi compartments. Journal of Biological Chemistry, 278(2), 791-799. Retrieved from http://www.jbc.org/content/278/2/791.full.pdf+html.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F19C-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-E295-8
Genre: Journal Article

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599297.pdf (Publisher version), 965KB
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Luo, Z. L., Author
Gallwitz, D.1, Author              
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1Department of Molecular Genetics, MPI for biophysical chemistry, Max Planck Society, ou_578622              

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 Abstract: Yeast Ypt6p, the homologue of the mammalian Rab6 GTPase, is not essential for cell viability. Based on previous studies with ypt6 deletion mutants, a regulatory role of the GTPase either in protein retrieval to the trans-Golgi network or in forward transport between the endoplasmic reticulum (ER) and early Golgi compartments was proposed. To assess better the primary role(s) of Ypt6p, temperature-sensitive ypt6 mutants were generated and analyzed biochemically and genetically. Defects in N-glycosylation of proteins passing the Golgi and of Golgi- resident glycosyltransferases as well as protein sorting defects in the trans-Golgi were recorded shortly after functional loss of Ypt6p. ER-to-Golgi transport and protein secretion were delayed but not interrupted. Mis-sorting of the vesicular SNARE Sec22p to the late Golgi was also observed. Combination of the ypt6-2 mutant allele with a number of mutants in forward and retrograde transport between ER, Golgi, and endosomes led to synthetic negative growth defects. The results obtained indicate that Ypt6p acts in endosome-to-Golgi, in intra-Golgi retrograde transport, and possibly also in Golgi-to-ER trafficking.

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Language(s): eng - English
 Dates: 2003-01-10
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 278 (2) Sequence Number: - Start / End Page: 791 - 799 Identifier: -