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Titolo:
TRANSFORMING-GROWTH-FACTOR BETA-INDUCED PHOSPHORYLATION OF SMAD3 IS REQUIRED FOR GROWTH-INHIBITION AND TRANSCRIPTIONAL INDUCTION IN EPITHELIAL-CELLS
Autore:
LIU XD; SUN Y; CONSTANTINESCU SN; KARAM E; WEINBERG RA; LODISH HF;
Indirizzi:
WHITEHEAD INST BIOMED RES,CAMBRIDGE CTR 9 CAMBRIDGE MA 02142 WHITEHEAD INST BIOMED RES,CAMBRIDGE CTR 9 CAMBRIDGE MA 02142 MIT,DEPT BIOL CAMBRIDGE MA 02139
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 20, volume: 94, anno: 1997,
pagine: 10669 - 10674
SICI:
0027-8424(1997)94:20<10669:TBPOSI>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
MAD-RELATED PROTEIN; SIGNAL-TRANSDUCTION; FAMILY SIGNALS; RECEPTOR; MOTHERS; GENE; SUPERFAMILY; MEDIATORS; PATHWAYS; CLONING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
X.D. Liu et al., "TRANSFORMING-GROWTH-FACTOR BETA-INDUCED PHOSPHORYLATION OF SMAD3 IS REQUIRED FOR GROWTH-INHIBITION AND TRANSCRIPTIONAL INDUCTION IN EPITHELIAL-CELLS", Proceedings of the National Academy of Sciences of the United Statesof America, 94(20), 1997, pp. 10669-10674

Abstract

Drosophila Mad proteins are intracellular signal transducers of decapentaplegic (dpp), the Drosophila transforming growth factor beta (TGF-beta)/bone morphogenic protein (BMP) homolog. Studies in which the mammalian Smad homologs were transiently overexpressed in cultured cells have implicated Smad2 in TGF-beta signaling, but the physiological relevance of the Smad3 protein in signaling by TGF-beta receptors has notbeen established, Here me stably expressed Smad proteins at controlled levels in epithelial cells using a novel approach that combines highly efficient retroviral gene transfer and quantitative cell sorting. We show that upon TGF-beta treatment Smad3 becomes rapidly phosphorylated at the SSVS motif at its very C terminus. Either attachment of an epitope tag to the C terminus or replacement of these three serine residues with alanine abolishes TGF-beta-induced Smad3 phosphorylation; these proteins act in a dominant-negative fashion to block the antiproliferative effect of TGF-beta in mink lung epithelial cells. A Smad3 protein in which the three C-terminal serines have been replaced by aspartic acids is also a dominant inhibitor of TGF-beta signaling, but can activate plasminogen activator inhibitor 1 (PAI-1) transcription in a ligand-independent fashion when its nuclear localization is forced by transient overexpression, Phosphorylation of the three C-terminal serine residues of Smad3 by an activated TGF-beta receptor complex is an essential step in signal transduction by TGF-beta for both inhibition of cell proliferation and activation of the PAI-1 promoter.

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Documento generato il 04/07/20 alle ore 16:58:25