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The Journal of Neuroscience, June 15, 2000, 20(12):4524-4534
Interaction of the Postsynaptic Density-95/Guanylate Kinase Domain-Associated Protein Complex with a Light Chain of Myosin-V and Dynein
Scott Naisbitt1, Juli Valtschanoff2, Daniel W. Allison3, Carlo Sala1, Eunjoon Kim4, Ann Marie Craig3, Richard J. Weinberg2, and Morgan Sheng1 1 Howard Hughes Medical Institute and Department of Neurobiology, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts 02114, 2 Department of Cell Biology and Anatomy, University of North Carolina, Chapel Hill, North Carolina 27599, 3 Department of Cell and Structural Biology, University of Illinois, Urbana-Champaign, Illinois 61801, and 4 Department of Pharmacology, Pusan National University, Kumjeong-ku, Pusan 609-735, South Korea
NMDA receptors interact directly with postsynaptic density-95 (PSD-95), a scaffold protein that organizes a cytoskeletal- signaling complex at the postsynaptic membrane. The molecular mechanism by which the PSD-95-based protein complex is trafficked to the postsynaptic site is unknown but presumably involves specific motor proteins. Here we demonstrate a direct interaction between the PSD-95-associated protein guanylate kinase domain-associated protein (GKAP) and dynein light chain (DLC), a light chain subunit shared by myosin-V (an actin-based motor) and cytoplasmic dynein (a microtubule-based motor). A yeast two-hybrid screen with GKAP isolated DLC2, a novel protein 93% identical to the previously cloned 8 kDa dynein light chain (DLC1). A complex containing PSD-95, GKAP, DLC, and myosin-V can be immunoprecipitated from rat brain extracts. DLC colocalizes with PSD-95 and F-actin in dendritic spines of cultured neurons and is enriched in biochemical purifications of PSD. Immunogold electron microscopy reveals a concentration of DLC in the postsynaptic compartment of asymmetric synapses of brain in which it is associated with the PSD and the spine apparatus. We discuss the possibility that the GKAP/DLC interaction may be involved in trafficking of the PSD-95 complex by motor proteins.
Key words: postsynaptic density; motor protein; NMDA receptors; spine apparatus; receptor trafficking; cytoplasmic dynein
Copyright © 2000 Society for Neuroscience 0270-6474/00/20124524-11$05.00/0
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