Interaction of SAP97 with Minus-end-directed Actin Motor Myosin VI IMPLICATIONS FOR AMPA RECEPTOR TRAFFICKING

作者: Hongju Wu , Joanne E. Nash , Pedro Zamorano , Craig C. Garner

DOI: 10.1074/JBC.M203735200

关键词: Myosin light-chain kinaseAMPA receptorMotor proteinPDZ domainSH3 domainActinNeurotransmitter receptorCell biologyMyosinBiology

摘要: SAP97 is a modular protein composed of three PDZ domains, an SH3 domain, and guanylate kinase-like domain. It has been implicated functionally in the assembly structural stability synaptic junctions as well trafficking, recruitment, localization specific ion channels neurotransmitter receptors. The N terminus (S97N) shown to play key role selection binding partners at adhesion sites, clustering heterologous cells. Using S97N domain bait yeast two-hybrid screen, we identified minus-end-directed actin-based motor, myosin VI, partner. Moreover, light membrane fractions prepared from rat brain, found that VI form trimeric complex with α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptor subunit, GluR1. These data suggest may serve molecular link between GluR1 actin-dependent motor during dynamic translocation AMPA receptors postsynaptic plasma membrane.

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