Synaptic localization of SAPAP1, a synaptic membrane-associated protein
Ikuko Yao1, Junko Iida, Wataru Nishimura
1Department of Medical Biochemistry, Graduate School of Medicine, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8519, Japan.
Background:
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.
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