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Protein Serine/Threonine Phosphatase PPM1A Dephosphorylates Smadi in the Bone Morphogenetic Protein Signaling Pathway*.
- Source :
-
Journal of Biological Chemistry . 12/1/2006, Vol. 281 Issue 48, p36526-36532. 7p. 4 Diagrams. - Publication Year :
- 2006
-
Abstract
- Bone morphogenetic proteins (BMPs) are secreted polypeptides belonging to the transforming growth factor-α (TGF-β) superfamily that activates a broad range of biological responses in the metazoan organism. The BMP-initiated signaling pathway is under tight control by processes including regulation of the ligands, the receptors, and the key downstream intracellular effector Smads. A critical point of control in BMP signaling is the phosphorylation of Smad1, Smad5, and Smad8 in their C-terminal SXS motif. Although such phosphorylation, which is mediated by the type I BMP receptor kinases in response to BMP stimulation, is well characterized, biochemical mechanisms underlying Smad dephosphorylation remain to be elucidated. In this study, we have found that PPM1A, a metal ion-dependent protein serine/threonine phosphatase, physically interacts with and dephosphorylates Smad1 both in vitro and in vivo. Functionally, overexpression of PPM1A abolishes BMP-induced transcriptional responses, whereas RNA interference-mediated knockdown of PPM1A enhances BMP signaling. Collectively, our study suggests that PPM1A plays an important role in controlling BMP signaling through catalyzing Smad dephosphorylation. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00219258
- Volume :
- 281
- Issue :
- 48
- Database :
- Academic Search Index
- Journal :
- Journal of Biological Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 23576095
- Full Text :
- https://doi.org/10.1074/jbc.M605169200