Activity-regulated trafficking of the palmitoyl-acyl transferase DHHC5

G. Stefano Brigidi, Brendan Santyr, Jordan Shimell, Blair Jovellar and Shernaz X. Bamji ()
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G. Stefano Brigidi: and the Djavad Mowafaghian Center for Brain Health, University of British Columbia
Brendan Santyr: and the Djavad Mowafaghian Center for Brain Health, University of British Columbia
Jordan Shimell: and the Djavad Mowafaghian Center for Brain Health, University of British Columbia
Blair Jovellar: and the Djavad Mowafaghian Center for Brain Health, University of British Columbia
Shernaz X. Bamji: and the Djavad Mowafaghian Center for Brain Health, University of British Columbia

Nature Communications, 2015, vol. 6, issue 1, 1-17

Abstract: Abstract Synaptic plasticity is mediated by the dynamic localization of proteins to and from synapses. This is controlled, in part, through activity-induced palmitoylation of synaptic proteins. Here we report that the ability of the palmitoyl-acyl transferase, DHHC5, to palmitoylate substrates in an activity-dependent manner is dependent on changes in its subcellular localization. Under basal conditions, DHHC5 is bound to PSD-95 and Fyn kinase, and is stabilized at the synaptic membrane through Fyn-mediated phosphorylation of a tyrosine residue within the endocytic motif of DHHC5. In contrast, DHHC5’s substrate, δ-catenin, is highly localized to dendritic shafts, resulting in the segregation of the enzyme/substrate pair. Neuronal activity disrupts DHHC5/PSD-95/Fyn kinase complexes, enhancing DHHC5 endocytosis, its translocation to dendritic shafts and its association with δ-catenin. Following DHHC5-mediated palmitoylation of δ-catenin, DHHC5 and δ-catenin are trafficked together back into spines where δ-catenin increases cadherin stabilization and recruitment of AMPA receptors to the synaptic membrane.

Date: 2015
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DOI: 10.1038/ncomms9200

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