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The Journal of Neuroscience, June 1, 1999, 19(11):4189-4199
Characterization of MALS/Velis-1, -2, and -3: a Family of Mammalian LIN-7 Homologs Enriched at Brain Synapses in Association with the Postsynaptic Density-95/NMDA Receptor Postsynaptic Complex
Kiwon Jo1, Rachel Derin2, Min Li2, and David S. Bredt1 1 Department of Physiology, School of Medicine, University of California at San Francisco, San Francisco, California 94143-0444, and 2 Department of Physiology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205
Protein assembly at the postsynaptic density (PSD) of neuronal synapses is mediated in part by protein interactions with PSD-95/discs large/zona occludens-1 (PDZ) motifs. Here, we identify MALS-1, -2, -3, a family of small synaptic proteins containing little more than a single PDZ domain. MALS-1, -2, and -3 are mammalian homologs LIN-7, a Caenorhabditis elegans protein essential for vulval development. In contrast to functions for LIN-7 in epithelial cells, MALS-1 and -2 are selectively expressed in specific neuronal populations in brain and are enriched in PSD fractions. In cultured hippocampal neurons, MALS proteins are clustered together with PSD-95 and NMDA type glutamate receptors, consistent with a postsynaptic localization for MALS proteins. Immunoprecipitation and affinity chromatography studies readily identify association of MALS with PSD-95 and an NMDA receptor subunit. The PDZ domain of MALS selectively binds to peptides terminating in E-T/S-R/X-V/I/L, which corresponds to the C terminus of NMDA type 2 receptors and numerous other ion channels at the PSD. This work suggests a role for MALS proteins in regulating recruitment of neurotransmitter receptors to the PSD.
Key words: MALS; PDZ; LIN-7; PSD-95; NMDA receptor; postsynaptic density; C. elegans
Copyright © 1999 Society for Neuroscience 0270-6474/99/19114189-11$05.00/0
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