Abstract
Protein post-translational modification by the small ubiquitin-like modifier (SUMO), or SUMOylation, can regulate the stability, subcellular localization or interactome of a protein substrate with key consequences for cellular processes including the Epithelial-Mesenchymal Transition (EMT). The secreted protein Transforming Growth Factor beta (TGFβ) is a potent inducer of EMT in development and homeostasis. Importantly, the ability of TGFβ to induce EMT has been implicated in promoting cancer invasion and metastasis, resistance to chemo/radio therapy, and maintenance of cancer stem cells. Interestingly, TGFβ-induced EMT and the SUMO system intersect with important implications for cancer formation and progression, and novel therapeutics identification.
Highlights
Response to intrinsic and extrinsic cues is a hallmark of living cells
Protein SUMOylation is a rapidly expanding field with novel substrates and regulators being discovered on a regular basis
SUMOylation is a tightly controlled process and aberrations have been implicated in various diseases including cardiac, neurodegenerative, and malignant diseases [12,22,96]
Summary
Response to intrinsic and extrinsic cues is a hallmark of living cells. Cells need to respond to diverse signals using a limited set of molecular components of which proteins form a major cellular constituent [1]. Identification, characterization, and mapping of proteins’ modifications including phosphorylation, glycosylation and ubiquitination, to specific amino acid residues on target proteins are critical in understanding functional significance of such modifications in a biological context [3,4]. It is becoming clear that SUMOylation can affect a wide array of biological responses during development and homeostasis including cell differentiation, apoptosis and senescence [5]. C-terminal carboxyl group of the protein Small Ubiquitin-like Modifier (SUMO) and ε-amino group of a lysine residue on a specific protein substrate [7]. Hendriks and Vertegaal have curated data from several studies and found that 18% of the human proteome, which corresponds to approximately 3700 human proteins, is targeted by the SUMO machinery [11]. Cancers 2018, 10, 264 and biological significance of SUMOylation in living organisms has been the subject of numerous studies [5,11,12]
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