BEGAIN (brain-enriched guanylate kinase-associated protein), a novel neuronal PSD-95/SAP90-binding protein

被引:71
|
作者
Deguchi, M
Hata, Y
Takeuchi, M
Ide, N
Hirao, K
Yao, IK
Irie, M
Toyoda, A
Takai, Y
机构
[1] ERATO, Japan Sci & Technol Corp, JCR Pharmaceut Co Ltd, Takai Biotimer Project,Nishi Ku, Kobe, Hyogo 6512241, Japan
[2] Osaka Univ, Sch Med, Dept Biochem & Mol Biol, Suita, Osaka 565, Japan
关键词
D O I
10.1074/jbc.273.41.26269
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 is a synaptic membrane-associated guanylate kinase with three PDZ, one SH3, and one guanylate kinase (GK) domain. PSD-95/SAP90 binds various proteins through the PDZ domains and organizes synaptic junctions. PSD-95/SAP90 also interacts with the postsynaptic density (PSD) fraction-enriched protein, named SAPAP (also called GKAP and DAP), through the GK domain. SAPAP is Triton X-100-insoluble and recruits PSD-95/SAP90 into the Triton X-100-insoluble fraction in the transfected cells, suggesting that SAPAP may fix PSD-95/SAP90 to the PSD. Here we report a novel protein interacting with the GK domain of PSD95/SAP90, BEGAIN. BEGAIN is specifically expressed in brain and enriched in the PSD fraction. BEGAIN is Triton X-100-soluble in the transfected cells but is recruited to the Triton X-100-insoluble fraction by SAPAP when coexpressed with PSD-95/SAP90. BEGAIN may be a novel PSD component associated with the core complex of PSD-95/SAP90 and SAPAP.
引用
收藏
页码:26269 / 26272
页数:4
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