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Titolo:
Balance between activities of Rho kinase and type 1 protein phosphatase modulates turnover of phosphorylation and dynamics of desmin/vimentin filaments
Autore:
Inada, H; Togashi, H; Nakamura, Y; Kaibuchi, K; Nagata, K; Inagaki, M;
Indirizzi:
Aichi Canc Ctr, Res Inst, Div Biochem, Nagoya, Aichi 4648681, Japan Aichi Canc Ctr Nagoya Aichi Japan 4648681 m, Nagoya, Aichi 4648681, Japan Nagoya Univ, Grad Sch Sci, Div Biol Sci, Chikusa Ku, Nagoya, Aichi 4648602, Japan Nagoya Univ Nagoya Aichi Japan 4648602 a Ku, Nagoya, Aichi 4648602, Japan Osaka Univ, Sch Med, Dept Neuropsychiat, Suita, Osaka 5650871, Japan OsakaUniv Suita Osaka Japan 5650871 sychiat, Suita, Osaka 5650871, Japan Nara Inst Sci & Technol, Div Signal Transduct, Nara 6300101, Japan Nara Inst Sci & Technol Nara Japan 6300101 ransduct, Nara 6300101, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 49, volume: 274, anno: 1999,
pagine: 34932 - 34939
SICI:
0021-9258(199912)274:49<34932:BBAORK>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
KERATIN INTERMEDIATE FILAMENTS; SERINE-THREONINE KINASE; SMALL GTPASE RHO; MYOSIN PHOSPHATASE; PUTATIVE TARGET; SERINE/THREONINE KINASE; CYTOSKELETAL INTEGRITY; NEURITE RETRACTION; FOCAL ADHESIONS; OKADAIC ACID;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
56
Recensione:
Indirizzi per estratti:
Indirizzo: Inagaki, M Aichi Canc Ctr, Res Inst, Div Biochem, 1-1 Chikusa Ku, Nagoya, Aichi 4648681, Japan Aichi Canc Ctr 1-1 Chikusa Ku Nagoya Aichi Japan 4648681 Japan
Citazione:
H. Inada et al., "Balance between activities of Rho kinase and type 1 protein phosphatase modulates turnover of phosphorylation and dynamics of desmin/vimentin filaments", J BIOL CHEM, 274(49), 1999, pp. 34932-34939

Abstract

To analyze the cell cycle-dependent desmin phosphorylation by Rho kinase, we developed antibodies specifically recognizing the kinase-dependent phosphorylation of desmin at Thr-16, Thr-75, and Thr-76. With these antibodies, phosphorylation of desmin was observed specifically at the cleavage furrow in late mitotic Saos-2 cells. We then found that treatment of the interphase cells with calyculin A revealed phosphorylation at all the three sites ofdesmin. We also found that an antibody, which specifically recognizes vimentin phosphorylated at Ser-71 by Rho kinase, became immunoreactive after calyculin A treatment. This calyculin A-induced interphase phosphorylation ofvimentin at Ser-71 was blocked by Rho kinase inhibitor or by expression ofthe dominant-negative Rho kinase. Taken together, our results indicate that Rho kinase is activated not only in mitotic cells but also interphase ones, and phosphorylates intermediate filament proteins, although the apparentphosphorylation level is diminished to an undetectable level due to the constitutive action of type 1 protein phosphatase. The balance between intermediate filament protein phosphorylation by Rho kinase and dephosphorylationby type I protein phosphatase may affect the continuous exchange of intermediate filament subunits between a soluble pool and polymerized intermediate filaments.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 14:04:55