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Titolo:
Functional association of TGF-beta receptor II with cyclin B
Autore:
Liu, JH; Wei, S; Burnette, PK; Gamero, AM; Hutton, M; Djeu, JY;
Indirizzi:
UnivProgramida, Dept Biochem & Mol Biol, H Lee Moffit Canc Ctr & Res Inst,Univ S Florida Tampa FL USA 33612 Biol, H Lee Moffit Canc Ctr & Res Inst, Mayo Clin, Jacksonville, FL 32224 USA Mayo Clin Jacksonville FL USA 32224Mayo Clin, Jacksonville, FL 32224 USA
Titolo Testata:
ONCOGENE
fascicolo: 1, volume: 18, anno: 1999,
pagine: 269 - 275
SICI:
0950-9232(19990107)18:1<269:FAOTRI>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROWTH-FACTOR-BETA; CELL-CYCLE; SACCHAROMYCES-CEREVISIAE; DEPENDENT KINASE; PROTEIN-KINASE; HUMAN WEE1; PHOSPHORYLATION; INHIBITION; G1; ACTIVATION;
Keywords:
transforming growth factor receptor; cyclin B; cdc-2; cell cycle control;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Djeu, JY UnivProgramida, Dept Biochem & Mol Biol, H Lee Moffit Canc Ctr & Res Inst, Univ S Florida Tampa FL USA 33612 ee Moffit Canc Ctr & Res Inst,
Citazione:
J.H. Liu et al., "Functional association of TGF-beta receptor II with cyclin B", ONCOGENE, 18(1), 1999, pp. 269-275

Abstract

Utilizing the cytoplasmic tail of Transforming Growth Factor Receptor TypeII (TGF beta RII) as bait in a yeast two hybrid system, we have identifiedhuman cyclin B2 as a direct physical partner of TGF beta RII. Analysis of deletion mutants of glutathione-S-transferase (GST)-cyclin B2 mapped its binding domain for TGF beta RII to the C-terminal and revealed a negative regulatory region immediately upstream of the cyclin box. Using recombinant proteins, Cdc2 was demonstrated to indirectly interact with TGF beta RII via cyclin B2. This interaction was reproduced in THP-1 monocytic cells, where TGF beta treatment markedly enhanced the ability of cyclin B2 and, correspondingly, Cdc2 from TGF beta-treated THP-1 cells, to bind the GST-TGF beta RII fusion protein. More importantly, TGF beta RII co-precipitated with cyclin B2 in TGF beta-treated THP-1 cells. TGF beta treatment also caused threonine phosphorylation of Cdc2 in the TGF beta RII-cyclin B2-Cdc2 complex in THP1 cells, in parallel with down regulation of Cdc2 function as measured by histone H1 kinase activity. Cyclin B1 had the same capacity to bind TGF beta RII and mediate indirect Cdc2 binding. These results suggest an alternative mechanism that cell cycle arrest in the G1/S phase caused by TGF beta may, in part, be due to inactivation of cyclin B/Cdc2 kinase, which is needed for entry into the G2/M phase.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 18:04:25