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- 저자 : Graig, Ann Marie (검색결과 1 건)
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Kim, Eunjoon,Naisbitt, Scott,Hsueh, Yi-Ping,Rao, Anuradha,Rothschild, Adam,Graig, Ann Marie,Sheng, Morgan 부산대학교 유전공학연구소 1997 분자생물학 연구보 Vol.13 No.-
The molecular mechanisms underlying the organization of ion channels and signsling molecules at the synaptic junction are largely unknown. Recently, members of the PSD-95/SAP90 family of synaptic MAGUK(menbrane-acssociated guanylate kinase) proteins have been shown to interact. via their NH_2-terminal PDZ domains, with certain ion channels(NMDA receptors and K^+channels). thereby promoting the clustering of these proteins. Although the function of the NH_2-terminal PDZ domains in relatively well characterized, the function of the Src homology 3(SH3) domain and the guanylate kinase-like(GK)domain in the COOH-terminal half of PSD-95 has remained obscure. WE now repoet the isolation of a novel synaptic protein. termed GKAP for guanylate kinase-associated protein. that binds directly to the GK domain of the known members of the mammalian PSD-95 family. GKAP shows a unique domain structure and appear to be a major constituent of the postsynaptic density. GKAP colocalizes and coimmunoprecipitates with PSD-95 in vivo,and colusters with PSD-95 and K^+ channels/parent lack of guanylate kinase enzymatic activity, the fact that the GK domain can as a site for protein-protein interaction has implications for the function of diverse GK-containing proteins(such as p55,ZO-1,and LIN-2/CASK).
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