Publication Date:
1991-11-22
Description:
The binding of cytosolic coat proteins to organelles may regulate membrane structure and traffic. Evidence is presented that a small guanosine triphosphate (GTP)-binding protein, the adenosine diphosphate ribosylation factor (ARF), reversibly associates with the Golgi apparatus in an energy, GTP, and fungal metabolite brefeldin A (BFA)-sensitive manner similar to, but distinguishable from, the 110-kilodalton cytosolic coat protein beta-COP. Addition of beta gamma subunits of G proteins inhibited the association of both ARF and beta-COP with Golgi membranes that occurred upon incubation with guanosine 5'-O-(3-thiotriphosphate) (GTP-gamma-S). Thus, heterotrimeric G proteins may function to regulate the assembly of coat proteins onto the Golgi membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Donaldson, J G -- Kahn, R A -- Lippincott-Schwartz, J -- Klausner, R D -- New York, N.Y. -- Science. 1991 Nov 22;254(5035):1197-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1957170" target="_blank"〉PubMed〈/a〉
Keywords:
ADP-Ribosylation Factors
;
Aluminum/pharmacology
;
*Aluminum Compounds
;
Animals
;
Biological Transport
;
Brefeldin A
;
CHO Cells
;
Coatomer Protein
;
Cricetinae
;
Cyclopentanes/pharmacology
;
Endoplasmic Reticulum/metabolism
;
Fluorides/pharmacology
;
GTP-Binding Proteins/*metabolism
;
Golgi Apparatus/*metabolism
;
Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology
;
In Vitro Techniques
;
Intracellular Membranes/metabolism
;
Microtubule-Associated 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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