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Titolo:
Inhibition of myosin/moesin phosphatase by expression of the phosphoinhibitor protein CPI-17 alters microfilament organization and retards cell spreading
Autore:
Eto, M; Wong, L; Yazawa, M; Brautigan, DL;
Indirizzi:
Univ Virginia, Sch Med, Ctr Cell Signaling, Charlottesville, VA 22908 USA Univ Virginia Charlottesville VA USA 22908 Charlottesville, VA 22908 USA Hokkaido Univ, Grad Sch Sci, Div Chem, Sapporo, Hokkaido, Japan Hokkaido Univ Sapporo Hokkaido Japan Div Chem, Sapporo, Hokkaido, Japan
Titolo Testata:
CELL MOTILITY AND THE CYTOSKELETON
fascicolo: 3, volume: 46, anno: 2000,
pagine: 222 - 234
SICI:
0886-1544(200007)46:3<222:IOMPBE>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
RHO-ASSOCIATED KINASE; SMOOTH-MUSCLE CELLS; LIGHT CHAIN PHOSPHORYLATION; MYOSIN-BINDING SUBUNIT; FOCAL ADHESIONS; ACTIN-FILAMENTS; STRESS FIBERS; ERM PROTEINS; CALYCULIN-A; IN-VIVO;
Keywords:
RhoA; F-actin; phosphatase inhibitor; kinase inhibitor; fibronectin; phalloidin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
53
Recensione:
Indirizzi per estratti:
Indirizzo: Brautigan, DL Univ Virginia, Sch Med, Ctr Cell Signaling, Box 800577, Charlottesville, VA 22908 USA Univ Virginia Box 800577 Charlottesville VA USA 22908 08 USA
Citazione:
M. Eto et al., "Inhibition of myosin/moesin phosphatase by expression of the phosphoinhibitor protein CPI-17 alters microfilament organization and retards cell spreading", CELL MOTIL, 46(3), 2000, pp. 222-234

Abstract

Cell migration and cytokinesis require reorganization of the cytoskeleton,involving phosphorylation and dephosphorylation of proteins such as myosinII and moesin. Myosin and moesin bind directly to a regulatory subunit of myosin/moesin phosphatase (MMP) that contains a protein type-1 phosphatase (PP1) catalytic subunit. Here we examined the role of MMP in cytoskeletal dynamics using a phosphorylation-dependent inhibitor protein specific fur MMP, called CPI-17. Fibroblasts do not express CPI-17, making them a null background to study effects of expression. Wild type CPI-17 in rat embryo fibroblasts caused (1) abnormal accumulation of cortical F-actin fibers, distinct from the stress fibers induced by expression of active RhoA; (2) progressive contraction of cell area, leaving behind filamentous extensions that stained for F-actin and moesin, but not myosin; and (3) significantly retarded spreading of fibroblasts on fibronectin with elevated myosin II light chain phosphorylation. A phosphorylation site mutant CPI-17(T38A) and inhibitor-2, (Inh2), another PP1-specific inhibitor protein, served as controls and did not elicit these same responses when expressed at the same level as CPI-17. Inhibition of myosin light chain kinase by ML-9 prevented the abnormal accumulation of cortical microfilaments by CPI-17, but did not reverse shrinkage in area, whereas kinase inhibitors HA1077 and H7 prevented CPI-17-induced changes in microfilament distribution and cell contraction. These results highlight the physiological importance of myosin/moesin phosphatase regulation to dynamic remodeling of the cytoskeleton. Cell Motil. Cytoskeleton 46: 222-234, 2000. (C) 2000 Wiley-Liss, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 12:59:21