Differential expression of isoforms of PSD-95 binding protein (GKAP/SAPAP1) during rat brain development

被引:25
作者
Kawashima, N
Takamiya, K
Sun, J
Kitabatake, A
Sobue, K
机构
[1] OSAKA UNIV,SCH MED,CTR BIOMED RES,DEPT NEUROCHEM & NEUROPHARMACOL,SUITA,OSAKA 565,JAPAN
[2] HOKKAIDO UNIV,SCH MED,DEPT CARDIOVASC MED,KITA KU,SAPPORO,HOKKAIDO 060,JAPAN
关键词
postsynaptic density; PSD-95/SAP90;
D O I
10.1016/S0014-5793(97)01399-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
PSD-95/SAP90, which binds to the C-terminus of NMDA receptor and Shaker-type potassium channel, is one of the major postsynaptic density proteins, Recently, novel classes of proteins interacting with the guanylate kinase domain of PSD-95 have been identified, guanylate kinase-associated protein (GKAP) and SAP90/PSD-95-associated proteins (SAPAPs). Here we report the isolation of new isoforms of PSD-95 binding protein (GKAP/SAPAP1) using the yeast two-hybrid system. The isolated protein directly interacts with the guanylate kinase domain of PSD-95, Northern blot analyses revealed that the expression of these isoforms containing distinct N-terminal sequences is differentially regulated during brain development, The present findings suggest that each isoform of the PSD-95 binding protein is differentially expressed in a development-dependent manner and may be involved in the complex formation of PSD-95 and channel/receptors at the postsynaptic density. (C) 1997 Federation of European Biochemical Societies.
引用
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页码:301 / 304
页数:4
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