Identification of depalmitoylating enzymes

2016 Fiscal Year Final Research Report

• Project/Area Number: 26291045
• Research Category: Grant-in-Aid for Scientific Research (B)
• Allocation Type: Partial Multi-year Fund
• Section: 一般
• Research Field: Cell biology
• Research Institution: National Institute for Physiological Sciences
• Principal Investigator: FUKATA Masaki 生理学研究所, 分子細胞生理研究領域, 教授 (00335027)
• Research Collaborator: FUKATA Yuko 生理学研究所, 分子細胞生理研究領域, 准教授 (40416186) ; YOKOI Norihiko 生理学研究所, 分子細胞生理研究領域, 助教 (50710969) ; SEKIYA Atsushi ; MURAKAMI Tatsuro ; TAKAHASHI Naoki ; SUZUKI Yumi ; WATANABE Mie
• Project Period (FY): 2014-04-01 – 2017-03-31
• Keywords: パルミトイル化修飾 / シナプス / 脱パルミトイル化酵素

Outline of Final Research Achievements

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 still controversial palmitoyl-protein thioesterases (depalmitoylating enzymes). Here, we identified the membrane-anchored serine hydrolases, ABHD17A, 17B, and 17C, as the physiological PSD-95 depalmitoylating enzyme that regulates PSD-95 palmitoylation cycles in neurons. This study describes the first direct evidence for the neuronal depalmitoylating enzyme and provides a new aspect of the dynamic regulatory mechanisms of synaptic development and synaptic plasticity. In addition, our established APEGS assay, which provides unbiased and quantitative information about the palmitoylation state and dynamics, revealed the distinct regulatory mechanisms for synaptic palmitoylation.

Free Research Field

神経科学