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J Biol Chem. 2000 Jun 30;275(26):20045-51.

Synaptic targeting of the postsynaptic density protein PSD-95 mediated by a tyrosine-based trafficking signal.

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  • 1Department of Physiology and Program in Neuroscience, University of California, San Francisco, San Francisco, California 94143-0444, USA.

Abstract

Synaptic function requires proper localization of proteins at synaptic sites. Targeting of the postsynaptic density protein 95 (PSD-95) relies on multiple signals within the protein, including twelve C-terminal amino acids. We now show that this C-terminal targeting domain of PSD-95 mediates postsynaptic localization through a short tyrosine-based motif followed by a pair of hydrophobic amino acids. Consistent with a role in cellular trafficking, the tyrosine motif resembles the canonical motif for interactions with clathrin adaptor proteins. In fact, we find that the C-terminal targeting domain of PSD-95 is sufficient to mediate clathrin-dependent endocytosis when appended to a transmembrane protein. Furthermore, systematic mutagenesis reveals that endocytosis mediated by this domain depends on both the tyrosine motif and the dihydrophobic amino acid pair. Thus, postsynaptic targeting of PSD-95 requires a tyrosine-based signal that can mediate clathrin-coated vesicle formation.

PMID:
10748194
[PubMed - indexed for MEDLINE]
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