TY - JOUR
T1 - Specific accumulation of Rho-associated kinase at the cleavage furrow during cytokinesis
T2 - Cleavage furrow-specific phosphorylation of intermediate filaments
AU - Kosako, Hidetaka
AU - Goto, Hidemasa
AU - Yanagida, Maki
AU - Matsuzawa, Kaori
AU - Fujita, Masatoshi
AU - Tomono, Yasuko
AU - Okigaki, Tohru
AU - Odai, Hideharu
AU - Kaibuchi, Kozo
AU - Inagaki, Masaki
N1 - Funding Information:
We thank Drs S Yonemura and S Tsukita for providing anti-ERM mAb (CR22); Dr F Matsumura for providing anti-phosphorylated MLC-Ser19 (pp2b); N Takahashi for preparing GST-CAT; F Shigei for financial support to YT and TO; K Ando for technical assistance; K Kuromiya for the secretarial services and M Ohara for critique of the manuscript. This work was supported in part by Grants-in-Aid for Scientific Research and Cancer Research from the Ministry of Education, Science, Sports and Culture of Japan; Japan Society of the Promotion of Science Research for the Future; special coordination funds from the Science and Technology Agency of the Government of Japan; and a grant from Bristol-Myers-Squibb.
PY - 1999/4/29
Y1 - 1999/4/29
N2 - The small GTPase Rho and one of its targets, Rho-associated kinase (Rho-kinase), are implicated in a wide spectrum of cellular functions, including cytoskeletal rearrangements, transcriptional activation and smooth muscle contraction. Since Rho also plays an essential role in cytokinesis, Rho-kinase may possibly mediate some biological aspects of cytokinesis. Here, using a series of monoclonal antibodies that can specifically recognize distinct phosphorylated sites on glial fibrillary acidic protein (GFAP) and vimentin, phosphorylation sites by Rho-kinase in vitro were revealed to be identical to in vivo phosphorylation sites on these intermediate filament (IF) proteins at the cleavage furrow in dividing cells. We then found, by preparing two types of anti-Rho-kinase antibodies, that Rho-kinase accumulated highly and circumferentially at the cleavage furrow in various cell lines. This subcellular distribution during cytokinesis was very similar to that of ezrin/radixin/moesin (ERM) proteins and Ser19-phosphorylated myosin light chain. These results raise the possibility that Rho-kinase might be involved in the formation of the contractile ring by modulating these F-actin-binding proteins during cytokinesis and in the phosphorylation and regulation of IF proteins at the cleavage furrow.
AB - The small GTPase Rho and one of its targets, Rho-associated kinase (Rho-kinase), are implicated in a wide spectrum of cellular functions, including cytoskeletal rearrangements, transcriptional activation and smooth muscle contraction. Since Rho also plays an essential role in cytokinesis, Rho-kinase may possibly mediate some biological aspects of cytokinesis. Here, using a series of monoclonal antibodies that can specifically recognize distinct phosphorylated sites on glial fibrillary acidic protein (GFAP) and vimentin, phosphorylation sites by Rho-kinase in vitro were revealed to be identical to in vivo phosphorylation sites on these intermediate filament (IF) proteins at the cleavage furrow in dividing cells. We then found, by preparing two types of anti-Rho-kinase antibodies, that Rho-kinase accumulated highly and circumferentially at the cleavage furrow in various cell lines. This subcellular distribution during cytokinesis was very similar to that of ezrin/radixin/moesin (ERM) proteins and Ser19-phosphorylated myosin light chain. These results raise the possibility that Rho-kinase might be involved in the formation of the contractile ring by modulating these F-actin-binding proteins during cytokinesis and in the phosphorylation and regulation of IF proteins at the cleavage furrow.
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U2 - 10.1038/sj.onc.1202633
DO - 10.1038/sj.onc.1202633
M3 - Article
C2 - 10348354
AN - SCOPUS:0033614371
SN - 0950-9232
VL - 18
SP - 2783
EP - 2788
JO - Oncogene
JF - Oncogene
IS - 17
ER -