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Titolo:
THE TGF-P FAMILY MEDIATOR SMAD1 IS PHOSPHORYLATED DIRECTLY AND ACTIVATED FUNCTIONALLY BY THE BMP RECEPTOR KINASE
Autore:
KRETZSCHMAR M; LIU F; HATA A; DOODY J; MASSAGUE J;
Indirizzi:
MEM SLOAN KETTERING CANC CTR,CELL BIOL PROGRAM NEW YORK NY 10021 MEM SLOAN KETTERING CANC CTR,CELL BIOL PROGRAM NEW YORK NY 10021 MEM SLOAN KETTERING CANC CTR,HOWARD HUGHES MED INST NEW YORK NY 10021
Titolo Testata:
Genes & development
fascicolo: 8, volume: 11, anno: 1997,
pagine: 984 - 995
SICI:
0890-9369(1997)11:8<984:TTFMSI>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROWTH-FACTOR-BETA; I RECEPTORS; PROTEIN; COMPLEX; CLONING; IDENTIFICATION; MUTATION; ACTIVIN; ALPHA;
Keywords:
TGF-BETA; BMP; RECEPTOR; SMAD1; DPC4; PHOSPHORYLATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
61
Recensione:
Indirizzi per estratti:
Citazione:
M. Kretzschmar et al., "THE TGF-P FAMILY MEDIATOR SMAD1 IS PHOSPHORYLATED DIRECTLY AND ACTIVATED FUNCTIONALLY BY THE BMP RECEPTOR KINASE", Genes & development, 11(8), 1997, pp. 984-995

Abstract

Bone morphogenetic proteins (BMPs) are members of the TGP-P family that regulate cell proliferation, apoptosis, and differentiation, and participate in the development of most tissues and organs in vertebrates. Smad proteins function downstream of TGF-beta receptor serine/threonine kinases and undergo serine phosphorylation in response to receptoractivation. Smad1 is regulated in this fashion by BMP receptors, and Smad2 and Smad3 by TGF-beta and activin receptors. Here, we report that BMP receptors phosphorylate and activate Smad1 directly. Phosphorylation of Smad1 in vive involves serines in the carboxy-terminal motif SSXS. These residues are phosphorylated directly by a BMP type I receptor in vitro. Mutation of these carboxy-terminal serines prevents several Smad1 activation events, namely, Smad1 association with the relatedprotein DPC4, accumulation in the nucleus, and gain of transcriptional activity. Similar carboxy-terminal serines in Smad2 are required forits phosphorylation and association with DPC4 in response to TGF-beta, indicating the generality of this process of Smad activation. As a direct physiological substrate of BMP receptors, Smad1 provides a link between receptor serine/threonine kinases and the nucleus.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 17/01/21 alle ore 17:16:23