Specific accumulation of Rho-associated kinase at the cleavage furrow during cytokinesis: Cleavage furrow-specific phosphorylation of intermediate filaments

Hidetaka Kosako, Hidemasa Goto, Maki Yanagida, Kaori Matsuzawa, Masatoshi Fujita, Yasuko Tomono, Tohru Okigaki, Hideharu Odai, Kozo Kaibuchi, Masaki Inagaki

研究成果: ジャーナルへの寄稿記事

102 引用 (Scopus)

抄録

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.

元の言語英語
ページ(範囲)2783-2788
ページ数6
ジャーナルOncogene
18
発行部数17
DOI
出版物ステータス出版済み - 4 29 1999
外部発表Yes

Fingerprint

rho-Associated Kinases
Cytokinesis
Intermediate Filaments
Phosphorylation
Intermediate Filament Proteins
Myosin Light Chains
Monomeric GTP-Binding Proteins
Glial Fibrillary Acidic Protein
Vimentin
Muscle Contraction
Transcriptional Activation
Smooth Muscle
Monoclonal Antibodies
Cell Line
Antibodies
Proteins

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics
  • Cancer Research

これを引用

Specific accumulation of Rho-associated kinase at the cleavage furrow during cytokinesis : Cleavage furrow-specific phosphorylation of intermediate filaments. / Kosako, Hidetaka; Goto, Hidemasa; Yanagida, Maki; Matsuzawa, Kaori; Fujita, Masatoshi; Tomono, Yasuko; Okigaki, Tohru; Odai, Hideharu; Kaibuchi, Kozo; Inagaki, Masaki.

:: Oncogene, 巻 18, 番号 17, 29.04.1999, p. 2783-2788.

研究成果: ジャーナルへの寄稿記事

Kosako, H, Goto, H, Yanagida, M, Matsuzawa, K, Fujita, M, Tomono, Y, Okigaki, T, Odai, H, Kaibuchi, K & Inagaki, M 1999, 'Specific accumulation of Rho-associated kinase at the cleavage furrow during cytokinesis: Cleavage furrow-specific phosphorylation of intermediate filaments', Oncogene, 巻. 18, 番号 17, pp. 2783-2788. https://doi.org/10.1038/sj.onc.1202633
Kosako, Hidetaka ; Goto, Hidemasa ; Yanagida, Maki ; Matsuzawa, Kaori ; Fujita, Masatoshi ; Tomono, Yasuko ; Okigaki, Tohru ; Odai, Hideharu ; Kaibuchi, Kozo ; Inagaki, Masaki. / Specific accumulation of Rho-associated kinase at the cleavage furrow during cytokinesis : Cleavage furrow-specific phosphorylation of intermediate filaments. :: Oncogene. 1999 ; 巻 18, 番号 17. pp. 2783-2788.
@article{6e03dfcb420e4c63bd646ace3a096bf1,
title = "Specific accumulation of Rho-associated kinase at the cleavage furrow during cytokinesis: Cleavage furrow-specific phosphorylation of intermediate filaments",
abstract = "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.",
author = "Hidetaka Kosako and Hidemasa Goto and Maki Yanagida and Kaori Matsuzawa and Masatoshi Fujita and Yasuko Tomono and Tohru Okigaki and Hideharu Odai and Kozo Kaibuchi and Masaki Inagaki",
year = "1999",
month = "4",
day = "29",
doi = "10.1038/sj.onc.1202633",
language = "English",
volume = "18",
pages = "2783--2788",
journal = "Oncogene",
issn = "0950-9232",
publisher = "Nature Publishing Group",
number = "17",

}

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

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.

UR - http://www.scopus.com/inward/record.url?scp=0033614371&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033614371&partnerID=8YFLogxK

U2 - 10.1038/sj.onc.1202633

DO - 10.1038/sj.onc.1202633

M3 - Article

C2 - 10348354

AN - SCOPUS:0033614371

VL - 18

SP - 2783

EP - 2788

JO - Oncogene

JF - Oncogene

SN - 0950-9232

IS - 17

ER -