Home LiteratureArticle Details
PMID: 7997272 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

XL alpha s is a new type of G protein.

Nature ·Vol. 372 ·No. 6508 ·1994-00-00 ·Pages 804-9

Kehlenbach RH, Matthey J, Huttner WB

Abstract

The GTP-binding proteins are well-known regulators of cellular functions, including vesicular transport. Cholera toxin, which is known to catalyse ADP-ribosylation of the alpha s subunit of heterotrimeric G proteins, stimulates secretory vesicle formation from the trans-Golgi network. Here we describe a new cholera toxin target, an 'extra large' G protein (XL alpha s; M(r) 92K) which consists of a new 51K XL-portion linked to a G alpha s truncated at the amino terminus. XL alpha s is specifically associated with the trans-Golgi network and occurs selectively in cells containing both the regulated and the constitutive pathway of protein secretion. Hence, XL alpha s may mediate the effects of cholera toxin on secretory vesicle formation.

MeSH Terms
Adenosine Diphosphate Ribose/metabolism Amino Acid Sequence Animals Base Sequence Cholera Toxin/pharmacology Chromogranins DNA, Complementary GTP-Binding Protein alpha Subunits, Gs GTP-Binding Proteins/drug effects,genetics,metabolism Golgi Apparatus/metabolism Heterotrimeric GTP-Binding Proteins Membrane Proteins/metabolism Molecular Sequence Data Nerve Tissue Proteins PC12 Cells Rats Subcellular Fractions Tissue Distribution
Chemicals
Chromogranins DNA, Complementary Membrane Proteins Nerve Tissue Proteins Adenosine Diphosphate Ribose Cholera Toxin GTP-Binding Proteins Gnas protein, rat GTP-Binding Protein alpha Subunits, Gs Heterotrimeric GTP-Binding Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Kehlenbach R H
Institute for Neurobiology, University of Heidelberg, Germany.
Matthey J
Huttner W B
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1994-00-00
Pages
804-9
Language
English
Region
England
NLM ID
0410462
Subset
IM
Databases
GENBANK
X84047
Corrections
ErratumIn
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