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

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)531-540
Number of pages10
JournalGenes to Cells
Volume11
Issue number5
DOIs
Publication statusPublished - 05-2006
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Genetics
  • Cell Biology

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