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2014 Fiscal Year Final Research Report

The function of VCIP135 in p97ATPase-mediated membrane fusion.

Research Project

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Project/Area Number 24370082
Research Category

Grant-in-Aid for Scientific Research (B)

Allocation TypePartial Multi-year Fund
Section一般
Research Field Cell biology
Research InstitutionKyushu University

Principal Investigator

KONDO Hisao  九州大学, 医学(系)研究科(研究院), 教授 (20205561)

Project Period (FY) 2012-04-01 – 2015-03-31
Keywords膜融合 / ゴルジ体
Outline of Final Research Achievements

The Golgi apparatus is disassembled early mitosis. For Golgi disassembly, membrane fusion needs to be blocked. Golgi biogenesis requires the p97/p47 pathway. We previously reported that p47 phosphorylation on Serine-140 result in mitotic inhibition of the p97/p47 pathway. In this study, we show another mechanism of mitotic inhibition of p97-mediated Golgi membrane fusion. We clarified that VCIP135, an essential factor in both p97 membrane fusion pathways, is phosphorylated on Threonine-760 and Serine-767 by Cdc2 at mitosis and that this phosphorylated VCIP135 does not bind to p97. An in vitro Golgi reassembly assay revealed that VCIP135(T760E,S767E), which mimics mitotic phosphorylation, caused no cisternal regrowth. Our results indicate that the phosphorylation of VCIP135 on Threonine-760 and Serine-767 inhibits p97-mediated Golgi membrane fusion at mitosis.

Free Research Field

細胞生物学

URL: 

Published: 2016-06-03  

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