How ubiquitination regulates the TGF-β signalling pathway: New insights and new players

Surinder M. Soond, Andrew Chantry

Research output: Contribution to journalArticlepeer-review

25 Citations (Scopus)
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Ubiquitination of protein species in regulating signal transduction pathways is universally accepted as of fundamental importance for normal development, and defects in this process have been implicated in the progression of many human diseases. One pathway that has received much attention in this context is transforming growth factor-beta (TGF-ß) signalling, particularly during the regulation of epithelial-mesenchymal transition (EMT) and tumour progression. While E3-ubiquitin ligases offer themselves as potential therapeutic targets, much remains to be unveiled regarding mechanisms that culminate in their regulation. With this in mind, the focus of this review highlights the regulation of the ubiquitination pathway and the significance of a recently described group of NEDD4 E3-ubiquitin ligase isoforms in the context of TGF-ß pathway regulation. Moreover, we now broaden these observations to incorporate a growing number of protein isoforms within the ubiquitin ligase superfamily as a whole, and discuss their relevance in defining a new ‘iso-ubiquitinome’.
Original languageEnglish
Pages (from-to)749-758
Number of pages10
Issue number10
Early online date17 Aug 2011
Publication statusPublished - Oct 2011

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