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The Sec15 protein responds to the function of the GTP binding protein, Sec4, to control vesicular traffic in yeast

SEC15 function is required at a late stage of the yeast secretory pathway. Duplication of the gene encoding the ras-like, GTP-binding protein, Sec4, can suppress the partial loss of function resulting from the sec15-l mutation, but cannot suppress disruption of sec15. Analysis of the SEC15 gene pred...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1989
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115742/
https://www.ncbi.nlm.nih.gov/pubmed/2504727
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collection PubMed
description SEC15 function is required at a late stage of the yeast secretory pathway. Duplication of the gene encoding the ras-like, GTP-binding protein, Sec4, can suppress the partial loss of function resulting from the sec15-l mutation, but cannot suppress disruption of sec15. Analysis of the SEC15 gene predicts a hydrophilic protein product of 105 kD. Anti-Sec15 antibody recognizes a protein of 116-kD apparent molecular mass which is associated with a microsomal fraction of yeast in a strongly pH dependent fashion. Overproduction of Sec15 protein interferes with the secretory pathway, resulting in the formation of a cluster of secretory vesicles, and a patch of Sec15 protein revealed by immunofluorescence. The sec4-8 and sec2-4l mutations, but not mutations in other SEC genes, prevent formation of the Sec15 protein patch. We propose that Sec15 protein responds to the function of the Sec4 protein to control vesicular traffic.
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spelling pubmed-21157422008-05-01 The Sec15 protein responds to the function of the GTP binding protein, Sec4, to control vesicular traffic in yeast J Cell Biol Articles SEC15 function is required at a late stage of the yeast secretory pathway. Duplication of the gene encoding the ras-like, GTP-binding protein, Sec4, can suppress the partial loss of function resulting from the sec15-l mutation, but cannot suppress disruption of sec15. Analysis of the SEC15 gene predicts a hydrophilic protein product of 105 kD. Anti-Sec15 antibody recognizes a protein of 116-kD apparent molecular mass which is associated with a microsomal fraction of yeast in a strongly pH dependent fashion. Overproduction of Sec15 protein interferes with the secretory pathway, resulting in the formation of a cluster of secretory vesicles, and a patch of Sec15 protein revealed by immunofluorescence. The sec4-8 and sec2-4l mutations, but not mutations in other SEC genes, prevent formation of the Sec15 protein patch. We propose that Sec15 protein responds to the function of the Sec4 protein to control vesicular traffic. The Rockefeller University Press 1989-09-01 /pmc/articles/PMC2115742/ /pubmed/2504727 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
The Sec15 protein responds to the function of the GTP binding protein, Sec4, to control vesicular traffic in yeast
title The Sec15 protein responds to the function of the GTP binding protein, Sec4, to control vesicular traffic in yeast
title_full The Sec15 protein responds to the function of the GTP binding protein, Sec4, to control vesicular traffic in yeast
title_fullStr The Sec15 protein responds to the function of the GTP binding protein, Sec4, to control vesicular traffic in yeast
title_full_unstemmed The Sec15 protein responds to the function of the GTP binding protein, Sec4, to control vesicular traffic in yeast
title_short The Sec15 protein responds to the function of the GTP binding protein, Sec4, to control vesicular traffic in yeast
title_sort sec15 protein responds to the function of the gtp binding protein, sec4, to control vesicular traffic in yeast
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115742/
https://www.ncbi.nlm.nih.gov/pubmed/2504727