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J Biol Chem, Vol. 274, Issue 39, 27463-27466, September 24, 1999
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From the Guanylate kinase-associated protein
(GKAP)/SAP90/PSD-95-associated protein (SAPAP)/DLG-associated protein
(DAP) is a protein of the postsynaptic density (PSD), and binds to the
guanylate kinase domain of PSD-95/synapse-associated protein (SAP) 90 and synaptic scaffolding molecule. GKAP/SAPAP/DAP recruits PSD-95/SAP90 and its interacting protein, brain-enriched guanylate
kinase-interacting protein, into the Triton X-100-insoluble fraction in
transfected cells, suggesting that GKAP/SAPAP/DAP may link several PSD
components to the Triton X-100-insoluble structures in the PSD. We have
identified here a novel neuronal GKAP/SAPAP/DAP-binding protein and
named it synamon. Synamon has seven ankyrin repeats at the
NH2 terminus followed by one src homology 3 domain
and one PSD-95/Dlg-A/ZO-1 domain, and several proline-rich
regions at the carboxyl terminus. Synamon interacts with the
COOH-terminal region of GKAP/SAPAP/DAP via the middle
region containing a PSD-95/Dlg-A/ZO-1 domain. Synamon was
coimmunoprecipitated with SAPAP from rat crude synaptosomes and
colocalized with SAPAP in primary cultured rat hippocampal neurons.
Because synamon is composed of various protein-interacting modules, it
may also interact with proteins other than GKAP/SAPAP/DAP to organize
the architecture of the PSD.
Takai Biotimer Project, Exploratory Research
for Advanced Technology, Japan Science and Technology Corporation, c/o
JCR Pharmaceuticals Co. Ltd., 2-2-10 Murotani, Nishi-ku, Kobe 651-2241, Japan and § Department of Molecular Biology and
Biochemistry, Osaka University Graduate School of Medicine, Faculty of
Medicine, Suita 565-0871, Japan
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