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Mobile DHHC palmitoylating enzyme mediates activity-sensitive synaptic targeting of PSD-95.

Authors: Noritake, Jun  Fukata, Yuko  Iwanaga, Tsuyoshi  Hosomi, Naoki  Tsutsumi, Ryouhei  Matsuda, Naoto  Tani, Hideki  Iwanari, Hiroko  Mochizuki, Yasuhiro  Kodama, Tatsuhiko  Matsuura, Yoshiharu  Bredt, David S  Hamakubo, Takao  Fukata, Masaki 
Citation: Noritake J, etal., J Cell Biol. 2009 Jul 13;186(1):147-60. doi: 10.1083/jcb.200903101.
Pubmed: (View Article at PubMed) PMID:19596852
DOI: Full-text: DOI:10.1083/jcb.200903101

Protein palmitoylation is the most common posttranslational lipid modification; its reversibility mediates protein shuttling between intracellular compartments. A large family of DHHC (Asp-His-His-Cys) proteins has emerged as protein palmitoyl acyltransferases (PATs). However, mechanisms that regulate these PATs in a physiological context remain unknown. In this study, we efficiently monitored the dynamic palmitate cycling on synaptic scaffold PSD-95. We found that blocking synaptic activity rapidly induces PSD-95 palmitoylation and mediates synaptic clustering of PSD-95 and associated AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid)-type glutamate receptors. A dendritically localized DHHC2 but not the Golgi-resident DHHC3 mediates this activity-sensitive palmitoylation. Upon activity blockade, DHHC2 translocates to the postsynaptic density to transduce this effect. These data demonstrate that individual DHHC members are differentially regulated and that dynamic recruitment of protein palmitoylation machinery enables compartmentalized regulation of protein trafficking in response to extracellular signals.

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RGD ID: 21201259
Created: 2020-02-29
Species: All species
Last Modified: 2020-02-29
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.