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J Biol Chem, Vol. 274, Issue 25, 17431-17436, June 18, 1999
From the Department of Physiology and Program in Neuroscience,
University of California at San Francisco,
San Francisco, California 94143-0444
Postsynaptic density-95 (PSD-95/SAP-90) is a
member of the membrane-associated guanylate kinase (MAGUK) family of
proteins that assemble protein complexes at synapses and other cell
junctions. MAGUKs comprise multiple protein-protein interaction motifs
including PDZ, SH3 and guanylate kinase (GK) domains, and these binding sites mediate the scaffolding function of MAGUK proteins. Synaptic binding partners for the PDZ and GK domains of PSD-95 have been identified, but the role of the SH3 domain remains elusive. We now
report that the SH3 domain of PSD-95 mediates a specific interaction with the GK domain. The GK domain lacks a poly-proline motif that typically binds to SH3 domains; instead, SH3/GK binding is a bi-domain interaction that requires both intact motifs. Although isolated SH3 and
GK domains can bind in trans, experiments with intact PSD-95 molecules indicate that intramolecular SH3/GK binding dominates and prevents intermolecular associations. SH3/GK binding is conserved in the related Drosophila MAGUK protein DLG but is not
detectable for Caenorhabditis elegans LIN-2. Many
previously identified genetic mutations of MAGUKs in invertebrates
occur in the SH3 or GK domains, and all of these mutations disrupt
intramolecular SH3/GK binding.
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