Ontology highlight
ABSTRACT:
SUBMITTER: Noritake J
PROVIDER: S-EPMC2712995 | biostudies-literature | 2009 Jul
REPOSITORIES: biostudies-literature
Noritake Jun J Fukata Yuko Y Iwanaga Tsuyoshi T Hosomi Naoki N Tsutsumi Ryouhei R Matsuda Naoto N Tani Hideki H Iwanari Hiroko H Mochizuki Yasuhiro Y Kodama Tatsuhiko T Matsuura Yoshiharu Y Bredt David S DS Hamakubo Takao T Fukata Masaki M
The Journal of cell biology 20090701 1
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 rap ...[more]