Publication Date:
1998-07-31
Description:
Membrane trafficking has heretofore been studied with intact organelles. Here, fusion-competent proteoliposomes were reconstituted from a yeast vacuole detergent extract. Homotypic vacuole fusion requires many membrane proteins, including the Ypt7p guanosine triphosphatase and a "SNARE complex" with Vam3p and Nyv1p. Proteoliposomes from extracts immunodepleted of either Vam3p or Ypt7p could not fuse, but vesicles reconstituted from a mixture of these depleted extracts had restored fusion activity. Purified preassembled vacuolar SNARE complex, when reconstituted with a SNARE-depleted extract, was fully functional for fusion. Thus, solubilized integral membrane components can be reconstituted for priming, docking, and fusion steps of organelle trafficking.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sato, K -- Wickner, W -- New York, N.Y. -- Science. 1998 Jul 31;281(5377):700-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dartmouth Medical School, Department of Biochemistry, Hanover, NH 03755-3844, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9685264" target="_blank"〉PubMed〈/a〉
Keywords:
Adenosine Triphosphate/metabolism
;
Fungal Proteins/metabolism
;
GTP Phosphohydrolases/*metabolism
;
GTP-Binding Proteins/*metabolism
;
*Membrane Fusion
;
Membrane Proteins/*metabolism
;
Proteolipids/metabolism
;
Qa-SNARE Proteins
;
SNARE Proteins
;
Saccharomyces cerevisiae/metabolism
;
*Saccharomyces cerevisiae Proteins
;
Solubility
;
Vacuoles/*metabolism
;
*Vesicular Transport Proteins
;
*rab GTP-Binding Proteins
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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