Crosstalk of intracellular post-translational modifications in cancer

Wu, Zheng; Huang, Rongting; Yuan, Leilei

doi:10.1016/j.abb.2019.108138

Cited by 61 publications

(42 citation statements)

References 128 publications

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“…Furthermore, these PTMs were also found for CREB and were associated either with increased or decreased CREB activity, which was mediated by distinct mechanisms, as summarized in Table 3. Several PTMs of CREB can affect the progression of cancer and have been recently extensively reviewed [63].…”

Section: Posttranslational Modifications With the Exception Of Phosphmentioning

confidence: 99%

What turns CREB on? And off? And why does it matter?

Steven

Friedrich

Jank

et al. 2020

Cell. Mol. Life Sci.

132

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Altered expression and function of the transcription factor cyclic AMP response-binding protein (CREB) has been identified to play an important role in cancer and is associated with the overall survival and therapy response of tumor patients. This review focuses on the expression and activation of CREB under physiologic conditions and in tumors of distinct origin as well as the underlying mechanisms of CREB regulation by diverse stimuli and inhibitors. In addition, the clinical relevance of CREB is summarized, including its use as a prognostic and/or predictive marker as well as a therapeutic target.

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Section: Posttranslational Modifications With the Exception Of Phosphmentioning

confidence: 99%

What turns CREB on? And off? And why does it matter?

Steven

Friedrich

Jank

et al. 2020

Cell. Mol. Life Sci.

132

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“…In addition to acetylation, a lysine residue in a protein can be subject to other PTMs, such as methylation, phosphorylation, ubiquitination, succinylation, and sumoylation. Modification of lysine residues by PTM may occur in a mutually exclusive manner suggesting an interplay between the different lysine modifications in the function of the regulatory protein [13,30,31].…”

Section: Acetylationmentioning

confidence: 99%

Role of acetylation in nonalcoholic fatty liver disease: a focus on SIRT1 and SIRT3

Nassir

2020

Exploration of Medicine

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Nonalcoholic fatty liver disease (NAFLD) has become the most prevalent liver chronic disease worldwide. The pathogenesis of NAFLD is complex and involves many metabolic enzymes and multiple pathways. Posttranslational modifications of proteins (PMPs) added another layer of complexity to the pathogenesis of NAFLD. PMPs change protein properties and regulate many biological functions, including cellular localization, stability, intracellular signaling, and protein function. Lysine acetylation is a common reversible PMP that consists of the transfer of an acetyl group from acetyl-coenzyme A (CoA) to a lysine residue on targeted proteins. The deacetylation reaction is catalyzed by deacetylases called sirtuins. This review summarizes the role of acetylation in NAFLD with a focus on sirtuins 1 and 3.

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“…Post-translational modifications (PTMs) of proteins play important roles in regulating protein conformation, localization, stability, and activity and ultimately induce a number of fundamental biological functions, including signal transduction, protein-protein interaction, protein trafficking, cell differentiation, and proliferation (Marcelli et al, 2018;Wu et al, 2019). To date, more than 450 PTMs have been identified, including phosphorylation, oxidation, ubiquitination, and SUMOylation (Venne et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

“…PTMs are reversible and tightly regulated during physiological conditions. However, gene mutations, increased cellular stresses, and deregulated cellular signals can modify PTMs or introduce non-specific PTMs and contribute to the development of human disease, notably cancer and neurodegeneration (Martin et al, 2011;Mowen and David, 2014;Marcelli et al, 2018;Wu et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

Post-translational Modifications of the Peptidyl-Prolyl Isomerase Pin1

Chen

Wang

Lee

2020

Front. Cell Dev. Biol.

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The peptidyl-prolyl cis/trans isomerase (PPIase) Pin1 is a unique enzyme that only binds to Ser/Thr-Pro peptide motifs after phosphorylation and regulates the conformational changes of the bond. The Pin1-catalyzed isomerization upon phosphorylation can have profound effects on substrate biological functions, including their activity, stability, assembly, and subcellular localization, affecting its role in intracellular signaling, transcription, and cell cycle progression. The functions of Pin1 are regulated by post-translational modifications (PTMs) in many biological processes, which include phosphorylation, ubiquitination, SUMOylation and oxidation. Phosphorylation of different Pin1 sites regulates Pin1 enzymatic activity, binding ability, localization, and ubiquitination by different kinases under various cellular contexts. Moreover, SUMOylation and oxidation have been shown to downregulate Pin1 activity. Although Pin1 is tightly regulated under physiological conditions, deregulation of Pin1 PTMs contributes to the development of human diseases including cancer and Alzheimer's disease (AD). Therefore, manipulating the PTMs of Pin1 may be a promising therapeutic option for treating various human diseases. In this review, we focus on the molecular mechanisms of Pin1 regulation by PTMs and the major impact of Pin1 PTMs on the progression of cancer and AD.

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Crosstalk of intracellular post-translational modifications in cancer

Cited by 61 publications

References 128 publications

What turns CREB on? And off? And why does it matter?

What turns CREB on? And off? And why does it matter?

Role of acetylation in nonalcoholic fatty liver disease: a focus on SIRT1 and SIRT3

Post-translational Modifications of the Peptidyl-Prolyl Isomerase Pin1

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