RRC ID 39112
Author Goto H, Kosako H, Tanabe K, Yanagida M, Sakurai M, Amano M, Kaibuchi K, Inagaki M.
Title Phosphorylation of vimentin by Rho-associated kinase at a unique amino-terminal site that is specifically phosphorylated during cytokinesis.
Journal J. Biol. Chem.
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.
Volume 273(19)
Pages 11728-36
Published 1998-5-8
DOI 10.1074/jbc.273.19.11728
PMID 9565595
MeSH Amino Acid Sequence Anaphase Animals COS Cells Cattle Cell Division* Fluorescent Antibody Technique, Indirect GTP-Binding Proteins / metabolism Guanosine Triphosphate / metabolism Immunologic Techniques Intermediate Filaments / ultrastructure Intracellular Signaling Peptides and Proteins Microscopy, Confocal Molecular Sequence Data Phosphorylation Phosphoserine / metabolism Protein-Serine-Threonine Kinases / metabolism* Vimentin / metabolism* rho GTP-Binding Proteins rho-Associated Kinases
IF 4.106
Times Cited 147
WOS Category BIOCHEMISTRY & MOLECULAR BIOLOGY
Resource
Human and Animal Cells