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
PII S0021-9258(19)89381-X
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 4.238
Times Cited 169
WOS Category BIOCHEMISTRY & MOLECULAR BIOLOGY
Resource
Human and Animal Cells COS-7(RCB0539)