Publication Date:
1998-02-21
Description:
Syntaxins are thought to function during vesicular transport as receptors on the target membrane and to contribute to the specificity of membrane docking and fusion by interacting with vesicle-associated receptors. Here, syntaxin 5 (Syn5) was shown to be an integral component of endoplasmic reticulum-derived transport vesicles. This pool, but not the target, Golgi-associated Syn5 pool, was essential for the assembly of vesicular-tubular pre-Golgi intermediates and the delivery of cargo to the Golgi. The requirement for vesicle-associated Syn5 in transport suggests a reevaluation of the basis for operation of the early secretory pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rowe, T -- Dascher, C -- Bannykh, S -- Plutner, H -- Balch, W E -- CA58689/CA/NCI NIH HHS/ -- GM 42336/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 30;279(5351):696-700.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9445473" target="_blank"〉PubMed〈/a〉
Keywords:
Adenosine Triphosphate/metabolism
;
Animals
;
Antibodies
;
Biological Transport
;
Carrier Proteins/metabolism
;
Cell Line
;
Endoplasmic Reticulum/*metabolism
;
Golgi Apparatus/*metabolism/ultrastructure
;
Mannose-Binding Lectins
;
Membrane Fusion
;
*Membrane Glycoproteins
;
Membrane Proteins/immunology/*metabolism
;
N-Ethylmaleimide-Sensitive Proteins
;
Organelles/metabolism
;
Qa-SNARE Proteins
;
Qb-SNARE Proteins
;
Qc-SNARE Proteins
;
R-SNARE Proteins
;
Rats
;
SNARE Proteins
;
*Vesicular Transport Proteins
;
Vesicular stomatitis Indiana virus/physiology
;
Viral Envelope Proteins/metabolism
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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