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2017 | 77 | Suppl.1 |
Tytuł artykułu

Role of local palmitoylation machinery in the postsynaptic nanodomain organization

Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
Protein palmitoylation, the most common lipid modification, dynamically regulates neuronal protein localization and function. Its unique reversibility is conferred by DHHC-type palmitoyl acyl transferases (palmitoylating enzymes) and palmitoyl-protein thioesterases (depalmitoylating enzymes). PSD-95 represents a major palmitoylated postsynaptic scaffolding protein that assembles various synaptic components such as AMPA- and NMDA-type glutamate receptors at the postsynaptic specialized membrane domain (postsynaptic density, PSD). Recently, we found that PSD-95 is partitioned into subsynaptic nanodomains and that PSD-95 in nanodomains undergoes continuous de/repalmitoylation cycles, thereby defining the geometry of PSDs. We found that a subset of metabolic serine hydrolases, ABHD17A, 17B and 17C, specifically depalmitoylate PSD-95 in heterologous cells. Expression of the plasma membrane-localized ABHD17 in hippocampal neurons directly binds to PSD-95 through its catalytic region and dramatically disperses PSD-95 clusters. Furthermore, taking advantage of the acyl-PEGyl exchange gel shift (APEGS) method, we quantitatively monitored the palmitoylation stoichiometry and the depalmitoylation kinetics of representative synaptic proteins, PSD-95, GluA1, GluN2A, mGluR5, Gαq, and HRas. Uniquely, most of the PSD‑95 population undergoes rapid palmitoylation cycles. We also found that inhibition of ABHD17 expression dramatically delays the kinetics of PSD-95 depalmitoylation. We propose that local palmitoylation machinery composed of synaptic DHHC palmitoylating enzymes and ABHD17 finely controls the amount of synaptic PSD-95 and thereby organizes the postsynaptic nanodomains. FINANCIAL SUPPORT: This work was supported by the Ministry of Education, Culture, Sports, Science and Technology (Grant numbers 15H04279, 15H01299 to Y.F; 26291045, 15H01570, 16H01371, 16K14560 to M.F.); Takeda Science Foundation to Y.F and M.F.; and The Naito Foundations to M.F.
Słowa kluczowe
Wydawca
-
Rocznik
Tom
77
Numer
Opis fizyczny
p.31-32
Twórcy
autor
  • National Institutes of Natural Sciences, National Institute for Physiological Sciences, Department of Molecular and Cellular Physiology, Division of Membrane Physiology, Okazaki, Japan
  • SOKENDAI, The Graduate University for Advanced Studies, School of Life Science Department of Physiological Sciences, Okazaki, Japan
autor
  • National Institutes of Natural Sciences, National Institute for Physiological Sciences, Department of Molecular and Cellular Physiology, Division of Membrane Physiology, Okazaki, Japan,
  • SOKENDAI, The Graduate University for Advanced Studies, School of Life Science Department of Physiological Sciences, Okazaki, Japan
autor
  • National Institutes of Natural Sciences, National Institute for Physiological Sciences, Department of Molecular and Cellular Physiology, Division of Membrane Physiology, Okazaki, Japan
  • SOKENDAI, The Graduate University for Advanced Studies, School of Life Science Department of Physiological Sciences, Okazaki, Japan
Bibliografia
Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
bwmeta1.element.agro-915d715f-6d00-428c-948c-6d86bf5469c3
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