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Titolo:
Rho-kinase-mediated contraction of isolated stress fibers
Autore:
Katoh, K; Kano, Y; Amano, M; Onishi, H; Kaibuchi, K; Fujiwara, K;
Indirizzi:
Natl Cardiovasc Ctr, Res Inst, Dept Struct Anal, Suita, Osaka 565, Japan Natl Cardiovasc Ctr Suita Osaka Japan 565 t Anal, Suita, Osaka 565, Japan Nara Inst Sci & Technol, Div Signal Transduct, Nara 6300101, Japan Nara Inst Sci & Technol Nara Japan 6300101 ransduct, Nara 6300101, Japan Nagoya Univ, Sch Med, Dept Cell Pharmacol, Nagoya, Aichi 4668550, Japan Nagoya Univ Nagoya Aichi Japan 4668550 acol, Nagoya, Aichi 4668550, Japan Univ Rochester, Cardiovasc Res Ctr, Rochester, NY 14642 USA Univ Rochester Rochester NY USA 14642 sc Res Ctr, Rochester, NY 14642 USA
Titolo Testata:
JOURNAL OF CELL BIOLOGY
fascicolo: 3, volume: 153, anno: 2001,
pagine: 569 - 583
SICI:
0021-9525(20010430)153:3<569:RCOISF>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
LIGHT-CHAIN KINASE; MYOSIN-BINDING SUBUNIT; SERINE-THREONINE KINASE; CELL ADHESION SITES; SMOOTH-MUSCLE; PROTEIN-KINASE; FOCAL ADHESIONS; EPITHELIAL-CELLS; PUTATIVE TARGET; CLEAVAGE FURROW;
Keywords:
Rho; Rho-kinase; stress fiber; contraction; myosin regulatory light chain;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
55
Recensione:
Indirizzi per estratti:
Indirizzo: Katoh, K Natl Cardiovasc Ctr, Res Inst, Dept Struct Anal, 5 Fujishirodai, Suita, Osaka 565, Japan Natl Cardiovasc Ctr 5 Fujishirodai Suita Osaka Japan 565 5, Japan
Citazione:
K. Katoh et al., "Rho-kinase-mediated contraction of isolated stress fibers", J CELL BIOL, 153(3), 2001, pp. 569-583

Abstract

It is widely accepted that actin filaments and the conventional double-headed myosin interact to generate force for many types of nonmuscle cell motility, and that this interaction occurs when the myosin regulatory light chain (MLC) is phosphorylated by MLC kinase (MLCK) together with calmodulin and Ca2+. However, recent studies indicate that Rho-kinase is also involved in regulating the smooth muscle and nonmuscle cell contractility. We have recently isolated reactivatable stress fibers from cultured cells and established them as a model system For actomyosin-based contraction in nonmuscle cells. Here, using isolated stress fibers, we show that Rho-kinase mediates MLC phosphorylation and their contraction in the absence of Ca2+. More rapid and extensive stress fiber contraction was induced by MLCK than was by Rho-kinase. When the activity of Rho-kinase but not MLCK was inhibited, cellsnot only lost their stress fibers and focal adhesions but also appeared tolose cytoplasmic tension. Our study suggests that actomyosin-based nonmuscle contractility is regulated by two kinase systems: the Ca2+-dependent MLCK and the Rho-kinase systems. We propose that Ca2+ is used to generate rapid contraction, whereas Rho-kinase plays a major role in maintaining sustained contraction in cells.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 08:26:41