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Titolo:
Calmodulin binds to p21(Cip1) and is involved in the regulation of its nuclear localization
Autore:
Taules, M; Rodriguez-Vilarrupla, A; Rius, E; Estanyol, JM; Casanovas, O; Sacks, DB; Perez-Paya, E; Bachs, O; Agell, N;
Indirizzi:
Univ Barcelona, Fac Med, IDIBAPS, Dept Biol Cellular & Anat Patol, Barcelona 08036, Spain Univ Barcelona Barcelona Spain 08036 Anat Patol, Barcelona 08036, Spain Brigham & Womens Hosp, Dept Pathol, Boston, MA 02115 USA Brigham & Womens Hosp Boston MA USA 02115 pt Pathol, Boston, MA 02115 USA Harvard Univ, Sch Med, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 vard Univ, Sch Med, Boston, MA 02115 USA Univ Valencia, Dept Bioquim & Biol Mol, E-46100 Valencia, Spain Univ Valencia Valencia Spain E-46100 & Biol Mol, E-46100 Valencia, Spain
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 35, volume: 274, anno: 1999,
pagine: 24445 - 24448
SICI:
0021-9258(19990827)274:35<24445:CBTPAI>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
CYCLIN-DEPENDENT KINASES; DNA-POLYMERASE-ALPHA; CELL-CYCLE; NRK CELLS; CDK4; G1; PHOSPHORYLATION; INHIBITOR; PROTEIN; P21;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Agell, N Univ Barcelona, Fac Med, Dept Cellular Biol, C Casanova 143, Barcelona 08036, Spain Univ Barcelona C Casanova 143 Barcelona Spain 08036 08036, Spain
Citazione:
M. Taules et al., "Calmodulin binds to p21(Cip1) and is involved in the regulation of its nuclear localization", J BIOL CHEM, 274(35), 1999, pp. 24445-24448

Abstract

p21(Cip1), first described as an inhibitor of cyclin-dependent kinases, has recently been shown to have a function in the formation of cyclin D-Cdk4 complexes and in their nuclear translocation. The dual behavior of p21(Cip1) may be due to its association with other proteins. Different evidence presented here indicate an in vitro and in vivo interaction of p21(Cip1) With calmodulin: 1) purified p21(Cip1) is able to bind to calmodulin-Sepharose in a Ca2+-dependent manner, and this binding is inhibited by the calmodulin-binding domain of calmodulin-dependent kinase II; 2) both molecules coimmunoprecipitate when extracted from cellular lysates; and 3) colocalization ofcalmodulin and p21(Cip1) can be detected in vivo by electron microscopy immunogold analysis. The carboxyl-terminal domain of p21(Cip1) is responsiblefor the calmodulin interaction, since p21(145-164) peptide is also able tobind calmodulin and to compete with full-length p21(Cip1) for the calmodulin binding. Because treatment of cells with anti-calmodulin drugs decreasesthe nuclear accumulation of p21(Cip1), We hypothesize that calmodulin interaction with p21(Cip1) is important for p21(Cip1), and in consequence for cyclin D-Cdk4, translocation into the cell nucleus.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 15:50:24