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Titolo:
Activation of LIM kinases by myotonic dystrophy kinase-related Cdc42-binding kinase alpha
Autore:
Sumi, T; Matsumoto, K; Shibuya, A; Nakamura, T;
Indirizzi:
Osaka Univ, Grad Sch Med, Div Mol Regenerat Med, Course Adv Med, Suita, Osaka 5650871, Japan Osaka Univ Suita Osaka Japan 5650871 Adv Med, Suita, Osaka 5650871, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 25, volume: 276, anno: 2001,
pagine: 23092 - 23096
SICI:
0021-9258(20010622)276:25<23092:AOLKBM>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACTIN CYTOSKELETAL DYNAMICS; CONTAINING PROTEIN-KINASE; ZINC-FINGER; COFILIN PHOSPHORYLATION; GENOMIC ORGANIZATION; CELL MOTILITY; CDNA CLONING; FAMILY; MOTIF; RHO;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Nakamura, T Osaka Univ, Grad Sch Med, Div Mol Regenerat Med, Course Adv Med, 2-2 Yamadaoka, Suita, Osaka 5650871, Japan Osaka Univ 2-2 Yamadaoka Suita Osaka Japan 5650871 0871, Japan
Citazione:
T. Sumi et al., "Activation of LIM kinases by myotonic dystrophy kinase-related Cdc42-binding kinase alpha", J BIOL CHEM, 276(25), 2001, pp. 23092-23096

Abstract

LIM kinases (LIMK1 and LIMK2) regulate actin cytoskeletal reorganization through cofilin phosphorylation downstream of distinct Rho family GTPases. Pak1 and ROCK, respectively, activate LIMK1 and LIMK2 downstream of Rac and Rho; however, an effector protein kinase for LIMKs downstream of Cdc42 remains to be defined. We now report evidence that LIMK1 and LIMK2 activities toward cofilin phosphorylation are stimulated in cells by the co-expression of myotonic dystrophy kinase-related Cdc42-binding kinase alpha (MRCK alpha), an effector protein kinase of Cdc42. In vitro, MRCK alpha phosphorylatedthe protein kinase domain of LIM kinases, and the site in LIMK2 phosphorylated by MRCK alpha proved to be threonine 505 within the activation segment. Expression of MRCK alpha induced phosphorylation of actin depolymerizing factor (ADF)/cofilin in cells, whereas MRCK alpha -induced ADF/cofilin phosphorylation was inhibited by the co expression with the protein kinase-deficient form of LIM kinases. These results indicate that MRCK alpha phosphorylates and activates LIM kinases downstream of Cdc42, which in turn regulates the actin cytoskeletal reorganization through the phosphorylation and inactivation of ADF/cofilin.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 09:41:32