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  Activation of transforming growth factor-beta signaling by SUMO-1 modification of tumor suppressor Smad4/DPC4

Lin, X., Liang, M., Liang, Y. Y., Brunicardi, F. C., Melchior, F., & Feng, X. H. (2003). Activation of transforming growth factor-beta signaling by SUMO-1 modification of tumor suppressor Smad4/DPC4. Journal of Biological Chemistry, 278(21), 18714-18719.

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Genre: Zeitschriftenartikel
Alternativer Titel : J. Biol. Chem.

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 Urheber:
Lin, X., Autor
Liang, M., Autor
Liang, Y. Y., Autor
Brunicardi, F. C., Autor
Melchior, F.1, Autor           
Feng, X. H., Autor
Affiliations:
1Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565145              

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 Zusammenfassung: Smads are important intracellular effectors in signaling pathways of the transforming growth factor-beta (TGF-beta) superfamily. Upon activation by TGF-beta, receptor- phosphorylated Smads form a complex with tumor suppressor Smad4/DPC4, and the Smad complexes then are imported into the nucleus. Although diverse pathways regulate the activity and expression of receptor-phosphorylated and inhibitory Smads, cellular factors modulating the activity of the common Smad4 remain unidentified. Here we describe the involvement of the small ubiquitin-like modifier-1 (SUMO-1) conjugation pathway in regulating the growth inhibitory and transcriptional responses of Smad4. The MH1 domain of Smad4 was shown to associate physically with Ubc9, the ubiquitin carrier protein (E2) conjugating enzyme in sumoylation. In cultured cells, Smad4 is modified by SUMO-1 at the endogenous level. The sumoylation sites were identified as two evolutionarily conserved lysine residues, Lys-113 and Lys-159, in the MH1 domain. We found that the mutations at Lys-113 and Lys-159 did not alter the ability of Smad4 to form a complex with Smad2 and FAST on the Mix. 2 promoter. Importantly, SUMO-1 overexpression enhanced TGF-beta- induced transcriptional responses. These findings identify sumoylation as a unique mechanism to modulate Smad4-dependent cellular responses.

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Sprache(n): eng - English
 Datum: 2003-05-23
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 28934
ISI: 000182932200003
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Titel: Journal of Biological Chemistry
  Alternativer Titel : J. Biol. Chem.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 278 (21) Artikelnummer: - Start- / Endseite: 18714 - 18719 Identifikator: ISSN: 0021-9258