Synaptic localization of SAPAP1, a synaptic membrane‐associated protein
Copyright policy )Synaptic localization of SAPAP1, a synaptic membrane‐associated protein
AbstractBackground: SAPAP1 was originally identified as a protein interacting with the guanylate kinase domain of PSD‐95. SAPAP1 also interacts with various proteins, including neurofilaments, synaptic scaffolding molecule (S‐SCAM), nArgBP2, dynein light chain and Shank through different regions.Results: We expressed various regions of SAPAP1 in hippocampal neurones. The synaptic targeting of SAPAP1 was mediated by the N‐terminal region and did not depend on the interaction with PSD‐95 or S‐SCAM. SAPAP1 was not involved in the synaptic localization of PSD‐95 or S‐SCAM, but affected that of Shank. The synaptic targeting of SAPAP1 was not suppressed by blocking NMDA or AMPA receptors. Fluorescent recovery after a photobleaching study revealed that SAPAP1 was immobile at synapses.Conclusion: SAPAP1 is a component of the static core of PSD, and its dynamics are different from those of the other PSD components, PSD‐95, S‐SCAM and BEGAIN.
Neurons, Binding Sites, Green Fluorescent Proteins, Membrane Proteins, Nerve Tissue Proteins, Hippocampus, Protein Structure, Tertiary, Rats, SAP90-PSD95 Associated Proteins, Proto-Oncogene Proteins c-myc, Luminescent Proteins, Neurofilament Proteins, COS Cells, Chlorocebus aethiops, Synapses, Animals, Carrier Proteins, Cells, Cultured
Neurons, Binding Sites, Green Fluorescent Proteins, Membrane Proteins, Nerve Tissue Proteins, Hippocampus, Protein Structure, Tertiary, Rats, SAP90-PSD95 Associated Proteins, Proto-Oncogene Proteins c-myc, Luminescent Proteins, Neurofilament Proteins, COS Cells, Chlorocebus aethiops, Synapses, Animals, Carrier Proteins, Cells, Cultured
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