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Titolo:
Calmodulin is essential for cyclin-dependent kinase 4 (Cdk4) activity and nuclear accumulation of cyclin D1-Cdk4 during G(1)
Autore:
Taules, M; Rius, E; Talaya, D; Lopez-Girona, A; Bachs, O; Agell, N;
Indirizzi:
Univiol,celona, Fac Med, Inst Invest Biomed August Pi & Sunyer, Dept Cell B Univ Barcelona Barcelona Spain E-08036 d August Pi & Sunyer, Dept Cell B
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 50, volume: 273, anno: 1998,
pagine: 33279 - 33286
SICI:
0021-9258(199812)273:50<33279:CIEFCK>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
DNA-POLYMERASE-ALPHA; CELL-CYCLE; ACTIVATING KINASE; NRK CELLS; RETINOBLASTOMA PROTEIN; GENE-PRODUCT; G1; LOCALIZATION; PROGRESSION; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
64
Recensione:
Indirizzi per estratti:
Indirizzo: Agell, N Univiol,celona, Fac Med, Inst Invest Biomed August Pi & Sunyer, Dept Cell B Univ Barcelona Casanova 143 Barcelona Spain E-08036 Dept Cell B
Citazione:
M. Taules et al., "Calmodulin is essential for cyclin-dependent kinase 4 (Cdk4) activity and nuclear accumulation of cyclin D1-Cdk4 during G(1)", J BIOL CHEM, 273(50), 1998, pp. 33279-33286

Abstract

Although it is known that calmodulin is involved in G(1) progression, the calmodulin-dependent G(1) events are not well understood. We have analyzed here the role of calmodulin in the activity, the expression, and the intracellular location of proteins involved in G(1) progression. The addition of anti-calmodulin drugs to normal rat kidney cells in early G(1) inhibited cyclin-dependent kinase 4 (Cdk4) and Cdk2 activities, as well as retinoblastoma protein phosphorylation. Protein levels of cdk4, cyclin D1, cyclin D2, cyclin E, p21, and p27 were not affected after CaM inhibition, whereas decreases in the amount of cyclin A and Cdc2 were observed. The decrease of Cdk4activity was due neither to changes in its association to cyclin D1 nor tochanges in the amount of p21 or p27 bound to cyclin D1-Cdk4 complexes. Calmodulin inhibition also produced a translocation of nuclear cyclin D1 and Cdk4 to the cytoplasm.. This translocation could be responsible for the decreased Cdk4 activity upon calmodulin inhibition, Immuno:precipitation, calmodulin affinity chromatography, and direct binding experiments indicated that calmodulin associates with Cdk4 and cyclin D1 through a calmodulin-binding protein. The facts that Hsp90 interacts with Cdk4 and that its inhibitioninduced Cdk4 and cyclin D1 translocation to the cytoplasm point to Hsp90 as a good candidate for being the calmodulin-binding protein involved in thenuclear accumulation of Cdk4 and cyclin D1.

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Documento generato il 25/11/20 alle ore 15:27:59