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PMID:10644767
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| Citation |
Hirao, K, Hata, Y, Yao, I, Deguchi, M, Kawabe, H, Mizoguchi, A and Takai, Y (2000) Three isoforms of synaptic scaffolding molecule and their characterization. Multimerization between the isoforms and their interaction with N-methyl-D-aspartate receptors and SAP90/PSD-95-associated protein. J. Biol. Chem. 275:2966-72 |
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| Abstract |
The synaptic scaffolding molecule (S-SCAM) has been identified as a protein interacting with SAP90/PSD-95-associated protein (SAPAP) (also called guanylate kinase-associated protein/hDLG-associated protein). S-SCAM has six PDZ (we have numbered them PDZ-0 to -5), two WW, and one guanylate kinase (GK) domains and interacts with N-methyl-D-aspartate (NMDA) receptor via PDZ-5 and SAPAP via the GK domain. We have identified here shorter isoforms of S-SCAM that start at the 164th or 224th methionine, and we renamed the original one, S-SCAMalpha, the middle one, S-SCAMbeta, and the shortest one, S-SCAM-gamma. S-SCAMbeta and -gamma have five PDZ (PDZ-1 to -5), two WW, and one GK domains. S-SCAMalpha interacted with S-SCAMbeta and -gamma through the region containing PDZ-4 and -5. The region containing both of PDZ-4 and -5 is sufficient for the clustering of NMDA receptors and forms a dimer in gel filtration, suggesting that S-SCAM forms multimers via the interaction between the C-terminal PDZ domains and assembles NMDA receptors into clusters. S-SCAMbeta and -gamma also interacted with SAPAP, suggesting that the N-terminal region of the GK domain is not necessary for the interaction. Finally, we have identified the interaction of the PDZ domains of S-SCAM with the GK domain of PSD-95/SAP90. S-SCAM, PSD-95/SAP90, and SAPAP are colocalized at least in some part in brain. Therefore, S-SCAM, PSD-95/SAP90, and SAPAP may form a complex in vivo. |
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| Keywords |
Adaptor Proteins, Signal Transducing; Amino Acid Sequence; Animals; Base Sequence; Biopolymers; CHO Cells; COS Cells; Carrier Proteins/chemistry; Carrier Proteins/metabolism; Cerebellum/metabolism; Chromatography, Gel; Cricetinae; DNA Primers; Guanylate Kinase; Microscopy, Fluorescence; Molecular Sequence Data; Nerve Tissue Proteins/chemistry; Nerve Tissue Proteins/metabolism; Protein Binding; Protein Isoforms/chemistry; Protein Isoforms/metabolism; Rats; Receptors, N-Methyl-D-Aspartate/metabolism; Retina/metabolism; Sequence Homology, Amino Acid |
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