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¹ Laboratory of Cancer Genetics, Digestive Diseases, and GI Developmental Biology, Department of Surgery, Medicine and Lombardi Cancer Center, Georgetown University Medical Center, Medical/Dental Building, NW 213, 3900 Reservoir Road, NW, Washington, District of Columbia 20007, USA² Veterans Affairs Medical Center, 50 Irving Street, NW, Washington, District of Columbia 20422, USA

(Correspondence should be addressed to E Glasgow; Email: eg239{at}georgetown.edu)

Transforming growth factor-β (TGF-β) represents a large family of growth and differentiation factors that mobilize complex signaling networks to regulate cellular differentiation, proliferation, motility, adhesion, and apoptosis. TGF-β signaling is tightly regulated by multiple complex mechanisms, and its deregulation plays a key role in the progression of many forms of cancer. Upon ligand binding, TGF-β signals are transduced by Smad proteins, which in turn are tightly dependent on modulation by adaptor proteins such as embryonic liver fodrin, Smad anchor for receptor activation, filamin, and crkl. A further layer of regulation is imposed by ubiquitin-mediated targeting and proteasomal degradation of specific components of the TGF-β signaling pathway. This review focuses on the ubiquitinators that regulate TGF-β signaling and the association of these ubiquitin ligases with various forms of cancer. Delineating the role of ubiquitinators in the TGF-β signaling pathway could yield powerful novel therapeutic targets for designing new cancer treatments.

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