Publication Date:
2004-04-10
Description:
Directionality in intracellular trafficking is essential to ensure the correct localization of proteins along the secretory pathway. Here, we found evidence for an active mechanism that prohibited back-fusion of de novo-generated vesicles with their donor compartment. Tip20p is a peripheral membrane protein implicated in consumption of COPI vesicles at the endoplasmic reticulum. However, a specific mutant of TIP20 did not interfere with COPII vesicle generation but allowed these vesicles to fuse back to the endoplasmic reticulum, a process that does not occur normally in the cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kamena, Faustin -- Spang, Anne -- New York, N.Y. -- Science. 2004 Apr 9;304(5668):286-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Friedrich Miescher Laboratorium der Max Planck Gesellschaft, Spemannstrasse 39, D-72076 Tubingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15073376" target="_blank"〉PubMed〈/a〉
Keywords:
COP-Coated Vesicles/*physiology/ultrastructure
;
Carrier Proteins/genetics/*physiology
;
Endoplasmic Reticulum/metabolism/*physiology/ultrastructure
;
Glycoproteins/genetics/*physiology
;
Golgi Apparatus/metabolism
;
Intracellular Membranes/physiology/ultrastructure
;
*Membrane Fusion
;
Mutation
;
Peptides/metabolism
;
Protein Transport
;
Recombinant Fusion Proteins/metabolism
;
Saccharomyces cerevisiae/genetics/*physiology/ultrastructure
;
Saccharomyces cerevisiae Proteins/genetics/metabolism
;
Vesicular Transport Proteins
;
alpha-Glucosidases/genetics/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
