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

doi:10.1080/09687680701528697

CORC > 北京大学 > 生命科学学院

	Palmitoylation participates in G protein coupled signal transduction by affecting its oligomerization
	Yang, Hui ; Qu, Liang ; Ni, Jianqiang ; Wang, Mengxi ; Huang, Youguo
刊名	分子膜生物学
	2008
关键词	G alpha(o) palmitoylation oligomerization disaggregation GTP-binding activity conformation G-BETA-GAMMA ALPHA-SUBUNITS MEMBRANE ASSOCIATION DISULFIDE-ISOMERASE NUCLEOTIDE-BINDING ADENYLATE-CYCLASE PLASMA-MEMBRANE DISAGGREGATION RECEPTOR ACTIVATION
DOI	10.1080/09687680701528697
英文摘要	Much in vivo and in vitro evidence has shown that the a 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 G alpha(o) on its oligomerization was explored extensively. G alpha(o) protein was expressed and purified from Escherichia coli strain JM109 cotransformed with pQE60(G alpha(o)) and pBB131(N-myristoyltransferase). Non-denaturing gel electrophoresis analysis revealed that G alpha(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 GTP gamma S stimulation. Palmitoylated G alpha(o), on the other hand, only present as oligomers that were difficult to disaggregate into monomers. The effect of palmitoylation on oligomerization of G alpha(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 G alpha(o) protein. Autoradiography indicated that [C-14]-palmitoylated G alpha(o) would in no case disaggregate into monomers after treatment with GTP gamma S. [S-35]GTP gamma S binding activity assay showed that palmitoylated G alpha(o) was saturated at only 7.8 nmol/mg compared to 21.8 nmol/mg for non-palmitoylated G alpha(o). Fluorescent quenching studies using BODIPY FL-GTP gamma S as a probe showed that the conformation of GTP-binding domain of G alpha(o) tended to become more compact after palmitoylation. These results implied that palmitoylation may regulate the GDP/GTP exchange of G alpha(o) by influencing the oligomerization state of G alpha(o) and thereby modulate the on-off switch of the G protein in G protein-coupled signal transduction.; http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000252352700006&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=8e1609b174ce4e31116a60747a720701 ; Biochemistry & Molecular Biology; Cell Biology; SCI(E); 4; ARTICLE; 1; 58-71; 25
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/249479]
专题	生命科学学院
推荐引用方式 GB/T 7714	Yang, Hui,Qu, Liang,Ni, Jianqiang,et al. Palmitoylation participates in G protein coupled signal transduction by affecting its oligomerization[J]. 分子膜生物学,2008.
APA	Yang, Hui,Qu, Liang,Ni, Jianqiang,Wang, Mengxi,&Huang, Youguo.(2008).Palmitoylation participates in G protein coupled signal transduction by affecting its oligomerization.分子膜生物学.
MLA	Yang, Hui,et al."Palmitoylation participates in G protein coupled signal transduction by affecting its oligomerization".分子膜生物学 (2008).