Vimentin-Ser82 as a memory phosphorylation site in astrocytes

In astrocytes, the PGF₂α 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. Viment...

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Bibliographic Details
Published in:Genes to cells : devoted to molecular & cellular mechanisms 2006-05, Vol.11 (5), p.531-540
Main Authors: Oguri, Takashi, Inoko, Akihito, Shima, Hiroshi, Izawa, Ichiro, Arimura, Nariko, Yamaguchi, Tomoya, Inagaki, Naoyuki, Kaibuchi, Kozo, Kikuchi, Kunimi, Inagaki, Masaki
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Animals
Astrocytes - cytology
Astrocytes - enzymology
Binding Sites
Calcium - metabolism
Calcium-Calmodulin-Dependent Protein Kinase Type 2
Calcium-Calmodulin-Dependent Protein Kinases - metabolism
Cells, Cultured
Dinoprost - metabolism
Dinoprost - pharmacology
Immunohistochemistry
Ionomycin - metabolism
Ionomycin - pharmacology
Models, Biological
Phosphoprotein Phosphatases - metabolism
Phosphorylation
Protein Phosphatase 1
Protein Subunits - metabolism
Rats
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Serine - metabolism
Time Factors
Vimentin - metabolism
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Summary:In astrocytes, the PGF₂α 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.
ISSN:1356-9597
1365-2443
DOI:10.1111/j.1365-2443.2006.00961.x