Control of synaptic transmission by a novel mechanism regulating SUMOylation

2017 Fiscal Year Final Research Report

• Project/Area Number: 16K14583
• Research Category: Grant-in-Aid for Challenging Exploratory Research
• Allocation Type: Multi-year Fund
• Research Field: Neurochemistry/Neuropharmacology
• Research Institution: Waseda University
• Principal Investigator: Akiyama Hiroki 早稲田大学, 人間科学学術院, 講師(任期付) (40568854)
• Project Period (FY): 2016-04-01 – 2018-03-31
• Keywords: SUMO / SENP

Outline of Final Research Achievements

Covalent conjugation of small ubiquitin-like modifiers (SUMOs) or SUMOylation is a reversible post-translational modification that regulates the stability and function of target proteins. Numerous studies have implicated SUMOylation in various physiological and pathological processes in cells and organs; however, SUMOylation-regulating machinery remains elusive. The balance between ligase-mediated conjugation and protease-mediated deconjugation is regarded as a determinant of SUMOylation state of target proteins. We identified a novel isoform of sentrin/SUMO-specific protease 5 (SENP5, referred to as SENP5S) that lacks the catalytic domain. Expression of SENP5S increased the amount of SUMOylated proteins, likely by competing with endogenous SENPs. This finding demonstrates a novel mechanism by which SUMO-interacting molecule like SENP5S can modulate SUMOylation state of target proteins in an enzymatic activity-independent manner.

Free Research Field

神経細胞生物学