Ubiquitin-mediated degradation a mechanism for fine-tuning TGF-beta signaling
- PMID: 15820671
- DOI: 10.1016/j.cell.2005.03.017
Ubiquitin-mediated degradation a mechanism for fine-tuning TGF-beta signaling
Abstract
Effects of the cytokine TGF-beta can be dampened by E3 ubiquitin ligases that target specific Smads, the TGF-beta signal transducers, for proteolytic destruction. Two papers in this issue of Cell highlight the importance of this mechanism in regulating the in vivo effects of TGF-beta. The first paper identifies and characterizes a novel Smad4 ubiquitin ligase, and the second paper redefines the role of a previously identified Smad1 ubiquitin ligase, Smurf-1 (Dupont et al., 2005; Yamashita et al., 2005).
Comment on
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Germ-layer specification and control of cell growth by Ectodermin, a Smad4 ubiquitin ligase.Cell. 2005 Apr 8;121(1):87-99. doi: 10.1016/j.cell.2005.01.033. Cell. 2005. PMID: 15820681
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Ubiquitin ligase Smurf1 controls osteoblast activity and bone homeostasis by targeting MEKK2 for degradation.Cell. 2005 Apr 8;121(1):101-13. doi: 10.1016/j.cell.2005.01.035. Cell. 2005. PMID: 15820682 Free PMC article.
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