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Titolo:
Elongation factor-1 alpha is a novel substrate of Rho-associated kinase
Autore:
Izawa, T; Fukata, Y; Kimura, T; Iwamatsu, A; Dohi, K; Kaibuchi, K;
Indirizzi:
Nara Inst Sci & Technol, Div Signal Transduct, Nara 6300101, Japan Nara Inst Sci & Technol Nara Japan 6300101 ransduct, Nara 6300101, Japan Nara Med Univ, Dept Internal Med 1, Kashihara, Nara 6348522, Japan Nara Med Univ Kashihara Nara Japan 6348522 Kashihara, Nara 6348522, Japan Nagoya Univ, Grad Sch Med, Dept Cell Pharmacol, Nagoya, Aichi 4668550, Japan Nagoya Univ Nagoya Aichi Japan 4668550 acol, Nagoya, Aichi 4668550, Japan Kirin Brewery Co Ltd, Cent Labs Key Technol, Yokohama, Kanagawa 2360004, Japan Kirin Brewery Co Ltd Yokohama Kanagawa Japan 2360004 agawa 2360004, Japan
Titolo Testata:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
fascicolo: 1, volume: 278, anno: 2000,
pagine: 72 - 78
SICI:
0006-291X(20001111)278:1<72:EFAIAN>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
MYOSIN-BINDING SUBUNIT; SERINE-THREONINE KINASE; ACTIN MESSENGER-RNA; PROTEIN-KINASE; FACTOR 1-ALPHA; PUTATIVE TARGET; SACCHAROMYCES-CEREVISIAE; NEURITE RETRACTION; MUSCLE-CONTRACTION; FOCAL ADHESIONS;
Keywords:
Rho; Rho-kinase; myosin-binding subunit of myosin phosphatase; EF-1 alpha; F-actin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Kaibuchi, K Nara Inst Sci & Technol, Div Signal Transduct, 8916-5 Takayama, Nara 6300101, Japan Nara Inst Sci & Technol 8916-5 Takayama Nara Japan 6300101 an
Citazione:
T. Izawa et al., "Elongation factor-1 alpha is a novel substrate of Rho-associated kinase", BIOC BIOP R, 278(1), 2000, pp. 72-78

Abstract

Rho-associated kinase (Rho-kinase), which is activated by the Rho small GTPase, phosphorylates the myosin-binding subunit (MBS) of myosin phosphatase, myosin light chain (MLC), the ERM family proteins, and adducin, thereby regulating the formation of stress fibers, focal adhesions, microvillus formation, and cell motility. Here, to further understand the role of Rho-kinase in the regulation of the numerous cellular processes by Rho, we purified a novel substrate of Rho-kinase having a molecular mass of 48 kDa (p48) from a rat liver cytosol extract. Mass spectral analysis revealed p48 to be elongation factor-1 alpha (EF-1 alpha), which is known as an actin-binding protein besides a cofactor of polypeptide elongation. Rho-kinase directly phosphorylated recombinant EF-1 alpha in vitro. A high- speed cosedimentation assay revealed that phosphorylation of EF-1 alpha by Rho-kinase decreased the binding activity of EF-1 alpha to filamentous actin (F-actin). A low-speed sedimentation assay revealed that phosphorylation of EF-1 alpha by Rho-kinase decreased the F-actin-bundling activity. In addition, EF-1 alpha bound to MBS of myosin phosphatase, suggesting that both Rho-kinase and myosin phosphatase regulate the phosphorylation state of EF-1 alpha downstream of Rho as other substrates of Rho-kinase, i.e., MLC, adducin, and the ERM family. These results suggest that the Rho/Rho-kinase pathway regulates the organization of actin cytoskeleton via the phosphorylation of EF-1 alpha. (C) 2000 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/21 alle ore 02:50:19