Regulation of the TGF-β pathway by deubiquitinases in cancer. (July 2016)

• Record Type: Journal Article
• Authors: Liu, Sijia; de Boeck, Miriam; van Dam, Hans; ten Dijke, Peter
• Is Part Of: International journal of biochemistry & cell biology. Volume 76(2016:Jul.)
• Page Start: 135
• Page End: 145
• Publication Date: 2016-07
• Subjects: AMSH Associated molecule with SH3 domain proteases -- AMSH-LP Associated molecule with SH3 domain-like proteases -- ATXN3 ataxin-3 -- ATXN3L ataxin 3-like -- BMPs bone morphogenetic proteins -- BRCC36 BRCA1/BRCA2-containing complex subunit 36 -- CHIP carboxy terminus of Hsc70-interacting protein -- CSN5/JAB1 COP9 signalosome subunit 5/Jun activating binding protein -- DUBs deubiquitinases -- E1 ubiquitin-activating enzymes -- E2 ubiquitin conjugating enzymes -- E3 ubiquitin ligase enzymes -- Ecto Ectodermin -- EMT epithelial-to-mesenchymal transition -- HECT homologous to the E6AP carboxyl terminus -- HNSCC head and neck squamous cell carcinoma -- IGF-I insulin like growth factor 1 -- IKK IκB kinase -- JAMMs JAB1/MPN/MOV34 proteases -- JNK c-Jun NH2-terminal kinase -- JOSD1 Josephin domain containing 1 -- LPS lipopolysaccharide -- MAPKs mitogen-activated protein kinases -- MJDs Machado-Joseph disease proteases -- MPN Mpr1-Pad1-N-terminal -- MPND MPN domain-containing protein -- MYSM1 Myb-like with SWIRM and MPN domains 1 -- OTUs ovarian tumour proteases -- p53 tumour protein p53 -- PI proteasome inhibitor -- PI3K phosphoinositide 3 kinase -- POH1/PSMD14 proteasome-associated PAD1 homolog1/Proteasome 26S Subunit Non-ATPase 14 -- RING really interesting new gene -- Smad Sma and Mad related protein -- Smurf Smad ubiquitin regulatory factor -- TAK1 transforming growth factor-β-activated kinase 1 -- TGF-β transforming growth factor-β -- TNFα Tumour necrosis factor-α -- TRAFs tumor necrosis factor receptor-associated factors -- Ub ubiquitin -- UBA ubiquitin-associated domain -- UCHs ubiquitin COOH-terminal hydrolases -- UIM ubiquitin-interacting motif -- USPs ubiquitin specific proteases; TGF-β -- Smad -- Ubiquitin -- Deubiquitinase -- Cancer; Biochemistry -- Periodicals; Cytology -- Periodicals; Biochemistry -- Periodicals; Cell Biology -- Periodicals; Biochimie -- Périodiques; Cytologie -- Périodiques; Biochimie; Cytologie; Biochemistry; Cytology; Ressource Internet (Descripteur de forme); Périodique électronique (Descripteur de forme); Periodicals; 572.05
• DOI: 10.1016/j.biocel.2016.05.001
• Languages: English
• ISSNs: 1357-2725

Abstract

Abstract: The transforming growth factor-β (TGF-β) pathway regulates diverse cellular processes. It signals via serine/threonine kinase receptors and intracellular Smad and non-Smad effector proteins. In cancer cells, aberrant TGF-β signalling can lead to loss of growth inhibition and an increase in invasion, epithelial-to-mesenchymal transition (EMT) and metastasis. Therapeutic targeting of the pro-oncogenic TGF-β responses is currently being explored as a potential therapy against certain invasive and metastatic cancer types. The ubiquitin post-translational regulation system is emerging as a key regulatory mechanism for the control of TGF-β pathway components. In this review, we focus on the role of deubiquitinases (DUBs), which counteract the activity of E3 ubiquitin ligases. We will discuss the mechanisms by which specific DUBs control Smad and non-Smad TGF-β signalling routes, and how perturbation of the expression and function of DUBs contributes to misregulation of TGF-β signalling in cancer.