Abstract:
:Syntaxins are thought to participate in the specific interactions between vesicles and acceptor membranes in intracellular protein trafficking. VAM3 of Saccharomyces cerevisiae encodes a 33 kDa protein (Vam3p) with a hydrophobic transmembrane segment at its C terminus. Vam3p has structural similarities to syntaxins of yeast, animal and plant cells. delta vam3 cells accumulated spherical structures of 200-600 nm in diameter, but lacked normal large vacuolar compartments. Loss of function of Vam3p resulted in inefficient processing of vacuolar proteins proteinase A, proteinase B and carboxypeptidase Y, and defective maturation of alkaline phosphatase. Subcellular fractionation and immunofluorescence microscopy showed that Vam3p was localized to the vacuolar membranes. Vam3p was accumulated in certain regions of the vacuolar membranes. We conclude from these observations that Vam3p is a novel member of syntaxin in the vacuoles and it provides the t-SNARE function in a late step of the vacuolar assembly.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Wada Y,Nakamura N,Ohsumi Y,Hirata Asubject
Has Abstractpub_date
1997-06-01 00:00:00pages
1299-306eissn
0021-9533issn
1477-9137journal_volume
110 ( Pt 11)pub_type
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journal_title:Journal of cell science
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journal_title:Journal of cell science
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journal_title:Journal of cell science
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journal_title:Journal of cell science
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journal_title:Journal of cell science
pub_type: 杂志文章
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journal_title:Journal of cell science
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journal_title:Journal of cell science
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journal_title:Journal of cell science
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