Association of synapse-associated protein 90/ postsynaptic density-95-associated protein (SAPAP) with neurofilaments.
作者： Kazuyo Hirao , Yutaka Hata , Maki Deguchi , Ikuko Yao , Misa Ogura
DOI: 10.1046/J.1365-2443.2000.00318.X
关键词: Biology 、 Synapse 、 Receptor 、 Amino acid 、 Transfection 、 Cell biology 、 Guanylate kinase 、 Postsynaptic density 、 Neurofilament 、 Molecular biology 、 Rat brain
摘要: Background Synapse-associated protein (SAP) 90/Postsynaptic density (PSD)-95-associated (SAPAP) (also called Guanylate kinase-associated protein/hDLG-associated protein) interacts with the guanylate kinase domains of PSD-95 and synaptic scaffolding molecule (S-SCAM) via middle region containing 5 repeats 14 amino acids. SAPAP also binds recently identified proteins, nArgBP2 synamon Shank 1a), proline-rich C-terminus, respectively. is highly enriched in Triton X-100-insoluble PSD fraction, recruits into fraction transfected cells. We have further characterized here X-100-insolubility tried to identify structures which with. Results N-Methyl- d-aspartate receptors were recruited by SAPAP. The N-terminal was X-100-insoluble, whereas C-terminal regions X-100-soluble. proteins interacting 35S-methionine-labelled overlay assay, determined their acid sequences, found them be neurofilaments. interacted neurofilaments region, co-immunoprecipitated from rat brain, co-localized cells. Conclusion SAPAP associates may link various components
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