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Titolo:
THE AMINO-TERMINUS OF THE RETINOBLASTOMA (RB) PROTEIN ASSOCIATES WITHA CYCLIN-DEPENDENT KINASE-LIKE KINASE VIA RB AMINO-ACIDS REQUIRED FORGROWTH SUPPRESSION
Autore:
STERNER JM; TAO YX; KENNETT SB; KIM HG; HOROWITZ JM;
Indirizzi:
DUKE UNIV,MED CTR,DEPT MOLEC CANC BIOL,BOX 3686 DURHAM NC 27710 DUKE UNIV,MED CTR,DEPT MOLEC CANC BIOL DURHAM NC 27710 DUKE UNIV,MED CTR,DEPT MICROBIOL DURHAM NC 27710
Titolo Testata:
Cell growth & differentiation
fascicolo: 1, volume: 7, anno: 1996,
pagine: 53 - 64
SICI:
1044-9523(1996)7:1<53:TAOTR(>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
CARCINOMA CELL-LINES; LARGE T-ANTIGENS; GENE-PRODUCT; TRANSCRIPTION FACTOR; SUSCEPTIBILITY GENE; C-MYC; BINDING PROTEIN; G1 PHASE; EXPRESSION; PHOSPHORYLATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
83
Recensione:
Indirizzi per estratti:
Citazione:
J.M. Sterner et al., "THE AMINO-TERMINUS OF THE RETINOBLASTOMA (RB) PROTEIN ASSOCIATES WITHA CYCLIN-DEPENDENT KINASE-LIKE KINASE VIA RB AMINO-ACIDS REQUIRED FORGROWTH SUPPRESSION", Cell growth & differentiation, 7(1), 1996, pp. 53-64

Abstract

We have shown previously that a novel cell cycle-regulated histone H1kinase activity, retinoblastoma kinase (RbK), associates with and phosphorylates the amino terminus of the Rb protein in G(2)-M. We have shown also that the amino terminus of p107, a Rb-related protein, does not associate with a similar kinase in vitro or in vivo. Here, we report that a RbK-like kinase associates with the amino terminus of p130, another Rb-related protein, only marginally, Moreover, the association of RbK with Rb in vitro is shown to require a discrete portion of the Rb amino terminus, amino acids 89-202. This region has been shown previously to be subject to inactivating mutations in retinoblastoma and to be required for Rb-mediated growth suppression in vitro, Taken together, these data indicate that the formation of Rb-RbK complexes may play an important role in Rb-mediated growth suppression. We have mappedtwo in vitro sites of Rb phosphorylation by RbK to sites that are phosphorylated in vivo and are targets of cyclin-dependent kinase phosphorylation in vitro, As such, at least some sites of RbK phosphorylationoverlap with those of other proline-directed serine and threonine kinases, Consistent with this latter observation, we report that the trans-activation domain of c-myc is phosphorylated specifically by RbK in vitro at a site (serine 62) that is phosphorylated in vivo during G(2)-M, cell-cycle phases in which RbK activity is maximal.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/09/20 alle ore 07:04:52