Phosphorylation of p37 is important for Golgi disassembly at mitosis

Yayoi Kaneko, Kaori Tamura, Go Totsukawa, Hisao Kondo

研究成果: ジャーナルへの寄稿学術誌査読

13 被引用数 (Scopus)

抄録

In mammals, the Golgi apparatus is disassembled at early mitosis and reassembled at the end of mitosis. For Golgi disassembly, membrane fusion needs to be blocked. Golgi biogenesis requires two distinct p97ATPase-mediated membrane fusion, the p97/p47 and p97/p37 pathways. We previously reported that p47 phosphorylation on Serine-140 by Cdc2 results in mitotic inhibition of the p97/p47 pathway [11]. In this study, we demonstrate that p37 is phosphorylated on Serine-56 and Threonine-59 by Cdc2 at mitosis, and this phosphorylated p37 does not bind to Golgi membranes. Using an in vitro Golgi reassembly assay, we show that mutated p37(S56D, T59D), which mimics mitotic phosphorylation, does not cause any cisternal regrowth, indicating that p37 phosphorylation inhibits the p97/p37 pathway. Our results demonstrate that p37 phosphorylation on Serine-56 and Threonine-59 is important for Golgi disassembly at mitosis.

本文言語英語
ページ(範囲)37-41
ページ数5
ジャーナルBiochemical and Biophysical Research Communications
402
1
DOI
出版ステータス出版済み - 11月 5 2010

!!!All Science Journal Classification (ASJC) codes

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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