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Differential expression of isoforms of PSD‐95 binding protein (GKAP/SAPAP1) during rat brain development 1
Author(s) -
Kawashima Nozomu,
Takamiya Kogo,
Sun Jie,
Kitabatake Akira,
Sobue Kenji
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01399-9
Subject(s) - postsynaptic density , guanylate kinase , gene isoform , biology , postsynaptic potential , microbiology and biotechnology , protein kinase a , biochemistry , receptor , kinase , membrane protein , gene , membrane
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.