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2016 Fiscal Year Final Research Report

Carboxyl-terminal tail-mediated homodimerizations of sphingomyelin synthases are responsible for efficient export from the endoplasmic reticulum

Research Project

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Project/Area Number 15K18868
Research Category

Grant-in-Aid for Young Scientists (B)

Allocation TypeMulti-year Fund
Research Field Biological pharmacy
Research InstitutionTeikyo University

Principal Investigator

Hayashi Yasuhiro  帝京大学, 薬学部, 助教 (70582857)

Project Period (FY) 2015-04-01 – 2017-03-31
Keywords脂質
Outline of Final Research Achievements

Sphingomyelin synthase (SMS) is the key enzyme for cross-talk between bioactive sphingolipids and glycerolipids. Here, we demonstrate that both SMS1 and SMS2 form homodimers. Homodimer formation was significantly decreased by C-terminal truncations, SMS1-ΔC22 and SMS2-ΔC30, indicating that the C-terminal tails of the SMSs are primarily responsible for homodimer formation. Interestingly, homodimer formation occurred in the endoplasmic reticulum (ER) membrane before trafficking to the Golgi apparatus. Reduced homodimerization caused by C-terminal truncations of SMSs significantly reduced ER-to-Golgi transport. Our findings suggest that the C-terminal tails of SMSs are involved in homodimer formation, which is required for efficient transport from the ER.

Free Research Field

脂質

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Published: 2018-03-22  

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