Palmitoylation participates in G protein coupled signal transduction by affecting its oligomerization.

Palmitoylation participates in G protein coupled signal transduction by affecting its oligomerization. Research Abstract Details 

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Palmitoylation participates in G protein coupled signal transduction by affecting its oligomerization. Abstract Text:

Hui Yang,Liang Qu,Jianqiang Ni,Mengxi Wang,Youguo Huang,

Much in vivo and in vitro evidence has shown that the alpha subunits of heterotrimeric GTP-binding proteins (G proteins) exist as oligomers in their base state and disaggregate when being activated. In this article, the influence of palmitoylation modification of Galpha(o) on its oligomerization was explored extensively. Galpha(o) protein was expressed and purified from Escherichia coli strain JM109 cotransformed with pQE60(Galpha(o)) and pBB131(N-myristoyltransferase). Non-denaturing gel electrophoresis analysis revealed that Galpha(o) existed to a small extent as monomers but mostly as oligomers including dimers, trimers, tetramers and pentamers which could disaggregate completely into monomers by GTPgammaS stimulation. Palmitoylated Galpha(o), on the other hand, only present as oligomers that were difficult to disaggregate into monomers. The effect of palmitoylation on oligomerization of Galpha(o) was further investigated by several other biochemical and biophysical methods including gel filtration chromatography, analytical ultracentrifugation and atomic force microscopy analysis. The results consistently demonstrated that palmitoylation facilitated oligomerization of the Galpha(o) protein. Autoradiography indicated that [(14)C]-palmitoylated Galpha(o) would in no case disaggregate into monomers after treatment with GTPgammaS. [(35)S]-GTPgammaS binding activity assay showed that palmitoylated Galpha(o) was saturated at only 7.8 nmol/mg compared to 21.8 nmol/mg for non-palmitoylated Galpha(o). Fluorescent quenching studies using BODIPY FL-GTPgammaS as a probe showed that the conformation of GTP-binding domain of Galpha(o) tended to become more compact after palmitoylation. These results implied that palmitoylation may regulate the GDP/GTP exchange of Galpha(o) by influencing the oligomerization state of Galpha(o) and thereby modulate the on-off switch of the G protein in G protein-coupled signal transduction.

Palmitoylation participates in G protein coupled signal transduction by affecting its oligomerization. Publishing Authors By Initials

H Yang,L Qu,J Ni,M Wang,Y Huang,

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MEDLINE DATE: 2008 Jan-Feb

Palmitoylation participates in G protein coupled signal transduction by affecting its oligomerization. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Molecular membrane biology

VOLUME: 25

Page Numbers: 58-71

Journal Abbreviation: Mol. Membr. Biol.

ISSN: 0968-7688

DAY: 21

MONTH: 12

YEAR: 2007

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LANGUAGE: eng

NlmUniqueID: 9430797

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Grant and Affiliation Information for Palmitoylation participates in G protein coupled signal transduction by affecting its oligomerization.

AFFILIATION: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, PR China.

Country: England

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MEDLINETA: Mol Membr Biol

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