Palmitoylation modification of G alpha(o) depresses its susceptibility   to GAP-43 activation

doi:10.1016/j.biocel.2008.12.011

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	Palmitoylation modification of G alpha(o) depresses its susceptibility to GAP-43 activation
	Yang, Hui ; Wan, Lixin ; Song, Fuchun ; Wang, Mengxi ; Huang, Youguo
刊名	international journal of biochemistry cell biology
	2009
关键词	GAP-43 G alpha(0) Palmitoylation GTP gamma S binding activity Oligomerization GROWTH CONE PROTEIN CONFORMATIONAL-CHANGE MEMBRANE ATTACHMENT SIGNAL-TRANSDUCTION ALPHA-SUBUNITS RECEPTOR G0 DISAGGREGATION STIMULATION G(O)ALPHA
DOI	10.1016/j.biocel.2008.12.011
英文摘要	Interaction between GAP-43 (growth associated protein-43) and G alpha(o) (alpha subunit of Go protein) influences the signal transduction pathways leading to differentiation of neural cells. GAP-43 is known to increase guanine nucleotide exchange by Gao, which is a major component of neuronal growth cone membranes. However, it is not clear whether GAP-43 stimulation is related to the Got, palmitoylation or the conversion of Goto from oligmers to monomers, which was shown to be a necessary regulatory factor in GDP/GTP exchange of G alpha(o). Here we expressed and purified GAP-43, GST-GAP-43 and Gao proteins, detected their stimulatory effect on [S-35]-GTP gamma S binding of G alpha(o). It was found that the EC50 of both GAP-43 and GST-GAP-43 activation were tenfold lower in case of depalmitoylated Ga. than palmitoylated Gao. Non-denaturing gel electrophoresis and p-PDM cross-linking analysis revealed that addition of GST-GAP-43 induced disassociation of depalmitoylated G alpha(o), from oligomers to monomers, but did not influence the oligomeric state of palmitoylated Gao, which suggests that palmitoylation is a key regulatory factor in GAP-43 stimulation on Ga,. These results indicated the interaction of GAP-43 and Goto could accelerate conversion of depalmitoylated Goto but not palmitoylated Get. from oligomers to monomers, so as to increase the GTP gamma S binding activity of G alpha(o). Results here provide new evidence about how signaling protein palmitoylation is involved in the G-protein-coupled signal transduction cascade, and give a useful clue on the participation of GAP-43 in G-protein cycle by its preferential activation of depalmitoylated G alpha(o). (c) 2008 Elsevier Ltd. All rights reserved.; http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000265768000007&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=8e1609b174ce4e31116a60747a720701 ; Biochemistry & Molecular Biology; Cell Biology; SCI(E); 5; ARTICLE; 7; 1495-1501; 41
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/247038]
专题	生命科学学院
推荐引用方式 GB/T 7714	Yang, Hui,Wan, Lixin,Song, Fuchun,et al. Palmitoylation modification of G alpha(o) depresses its susceptibility to GAP-43 activation[J]. international journal of biochemistry cell biology,2009.
APA	Yang, Hui,Wan, Lixin,Song, Fuchun,Wang, Mengxi,&Huang, Youguo.(2009).Palmitoylation modification of G alpha(o) depresses its susceptibility to GAP-43 activation.international journal of biochemistry cell biology.
MLA	Yang, Hui,et al."Palmitoylation modification of G alpha(o) depresses its susceptibility to GAP-43 activation".international journal of biochemistry cell biology (2009).