Phosphorylation of vimentin by RHO-associated kinase at a unique amino- terminal site that is specifically phosphorylated during cytokinesis

Hidemasa Goto, Hidetaka Kosako, Kazushi Tanabe, Maki Yanagida, Minoru Sakurai, Mutsuki Amano, Kozo Kaibuchi, Masaki Inagakii

Research output: Contribution to journalArticle

172 Citations (Scopus)

Abstract

We found that vimentin, the most widely expressed intermediate filament protein, served as an excellent substrate for Rho-associated kinase (Rho- kinase) and that vimentin phosphorylated by Rho-kinase lost its ability to form filaments in vitro. Two amino-terminal sites on vimentin, Ser38 and Ser71, were identified as the major phosphorylation sites for Rho-kinase, and Ser71 was the most favored and unique phosphorylation site for Rho- kinase in vitro. To analyze the vimentin phosphorylation by Rho-kinase in vivo, we prepared an antibody GK71 that specifically recognizes the phosphorylation of vimentin-Ser71. Ectopic expression of constitutively active Rho-kinase in COS-7 cells induced phosphorylation of vimentin at Ser71, followed by the reorganization of vimentin filament networks. During the cell cycle, the phosphorylation of vimentin-Ser71 occurred only at the cleavage furrow in late mitotic cells but not in interphase or early mitotic cells. This cleavage furrow-specific phosphorylation of vimentin-Ser71 was observed in the various types of cells we examined. All these accumulating observations increase the possibility that Rho-kinase may have a definite role in governing regulatory processes in assembly-disassembly and turnover of vimentin filaments at the cleavage furrow during cytokinesis.

Original languageEnglish
Pages (from-to)11728-11736
Number of pages9
JournalJournal of Biological Chemistry
Volume273
Issue number19
DOIs
Publication statusPublished - 08-05-1998
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Phosphorylation of vimentin by RHO-associated kinase at a unique amino- terminal site that is specifically phosphorylated during cytokinesis'. Together they form a unique fingerprint.

  • Cite this