Vimentin-Ser82 as a memory phosphorylation site in astrocytes

T. Takashi Oguri, Akihito Inoko, Hiroshi Shima, Ichiro Izawa, Nariko Arimura, Tomoya Yamaguchi, Naoyuki Inagaki, Kozo Kaibuchi, Kunimi Kikuchi, Masaki Inagaki

研究成果: Article査読

13 被引用数 (Scopus)

抄録

In astrocytes, the PGF or ionomycin treatment induces the phosphorylation at Ser38 and Ser82 of vimentin, a type III intermediate filament, by Ca2+ /calmodulin-dependent protein kinase II (CaMKII). We found here that vimentin phospho-Ser82 was dephosphorylated much slower than phospho-Ser38. Vimentin phospho-Ser38 was dephosphorylated quickly by purified PP1 catalytic subunit (PP1c) in vitro, whereas phospho-Ser82 was insensitive to PP1c. Because PP1c directly bound to vimentin through a VxF motif (Val83-Asp84-Phe85), the PP1c active site appeared to be unable to approach phospho-Ser82, leading to the prolongation of the phosphorylation at Ser-82. In astrocytes, PP1cα was in vivo associated with vimentin filaments. The repetitive treatment by ionomycin at a short interval resulted in the sustained elevation of Ser82 phosphorylation, leading to the marked disassembly of vimentin filaments. Taken together, these results suggest that vimentin is a novel member of binding partner of PP1c in astrocytes, and vimentin-Ser82 may act as a memory phosphorylation site.

本文言語English
ページ(範囲)531-540
ページ数10
ジャーナルGenes to Cells
11
5
DOI
出版ステータスPublished - 05-2006

All Science Journal Classification (ASJC) codes

  • Genetics
  • Cell Biology

フィンガープリント 「Vimentin-Ser82 as a memory phosphorylation site in astrocytes」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル