SnoN in TGF-&amp;#946; Signaling and Cancer Biology

Pot, Isabelle; Bonni, Shirin

doi:10.2174/156652408784533797

Cited by 28 publications

(48 citation statements)

References 130 publications

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“…Because SnoN is a negative regulator of the Smad proteins, one would predict that SnoN may operate in the opposite direction as TGF-␤ 1 during tumorigenesis particularly if these activities are dependent upon its ability to bind to the Smad proteins. Within the setting of cancer, the role of the SnoN-antagonistic TGF-␤ 1-induced EMT has been defined in several epithelial cell cancer lines [22,[25][26][27] . Several mechanisms have been proposed to explain how SnoN blocks Smad-mediated gene transcription.…”

Section: Discussionmentioning

confidence: 99%

SnoN as a Key Regulator of the High Glucose-Induced Epithelial-Mesenchymal Transition in Cells of the Proximal Tubule

Liu

Wang²,

Xiao³

et al. 2012

Kidney Blood Press Res

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Section: Discussionmentioning

confidence: 99%

SnoN as a Key Regulator of the High Glucose-Induced Epithelial-Mesenchymal Transition in Cells of the Proximal Tubule

Liu

Wang²,

Xiao³

et al. 2012

Kidney Blood Press Res

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“…Each of these pathological conditions is accompanied by increased levels of TGF␤1 and/or abnormal expression of SnoN (31,(51)(52)(53)(54). It is tempting to speculate that up-regulation of ADAM12 expression in cardiac hypertrophy, in inflammatory responses related to osteolysis, or in experimental autoimmune encephalomyelitis is directly linked to activation of TGF␤1 signaling.…”

Section: Discussionmentioning

confidence: 99%

The Role of SnoN in Transforming Growth Factor β1-induced Expression of Metalloprotease-Disintegrin ADAM12

Solomon

Muggy

et al. 2010

Journal of Biological Chemistry

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Increased expression of metalloprotease-disintegrin ADAM12 is a hallmark of several pathological conditions, including cancer, cardiovascular disease, and certain inflammatory diseases of the central nervous system or the muscoskeletal system. We show that transforming growth factor ␤1 (TGF␤1) is a potent inducer of ADAM12 mRNA and protein in mouse fibroblasts and in mouse and human mammary epithelial cells. Induction of ADAM12 is detected within 2 h of treatment with TGF␤1, is Smad2/Smad3-dependent, and is a result of derepression of the ADAM12, a member of the metalloprotease-disintegrin family of proteins, has been implicated in the progression of cancer, cardiovascular disease, osteoarthritis, and neurological disorders (1). The ADAM12 gene is frequently mutated in human breast cancers (2, 3), and cancer-associated mutations cause mislocalization of the ADAM12 protein in cells and alter its function (4). Missense single nuclear polymorphism in the ADAM12 gene shows strong association with osteoarthritis (5, 6). In addition to changes in its amino acid sequence, expression levels of ADAM12 are significantly increased in many pathological states. For example, ADAM12 expression levels are 20 -30-fold higher in human breast tumors than in normal mammary epithelium (7-12). ADAM12 expression is also markedly up-regulated in cancers of the liver, lung, stomach, colon, prostate, bladder, and in glioblastoma (13-18). Increased ADAM12 expression levels are found in the cardiac tissue of patients with hypertrophic obstructive cardiomyopathy (19) and in mice with angiotensin II-induced hypertension and cardiac hypertrophy (20,21). During inflammatory responses and aseptic osteolysis associated with loosened hip replacement implants, ADAM12 is up-regulated in the interface tissue around loosening implants (22). In experimental autoimmune encephalomyelitis, an animal model of multiple sclerosis, ADAM12 level is markedly increased in the T cells that infiltrate spinal cords (23).The mechanisms regulating ADAM12 expression, in particular those that may be responsible for altered levels of ADAM12 in various pathological states, are poorly understood. Previous studies employing hepatic stellate cells, a mesenchymal cell type in hepatic parenchyma, have indicated that ADAM12 expression is induced by transforming growth factor ␤ (TGF␤) 2 (13, 24). The TGF␤ signaling pathway is initiated when one of the family members, e.g. TGF␤1, -␤2, or -␤3, binds to a complex of TGF␤ type I and type II serine/threonine kinase receptors (T␤RI and T␤RII, respectively) and induces phosphorylation and activation of T␤RI by T␤RII. T␤RI then phosphorylates receptor Smads (R-Smads), Smad2 and Smad3. Phosphorylated Smad2/3 associate with the common partner Smad4 and translocate to the nucleus, where they regulate transcription of target genes (25,26). In addition, receptor activation in certain cell types leads to Smad-independent responses via the activation of mitogen-activated protein kinases (MAPKs), phosphoinositide 3-kinase, and Rho family memb...

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“…Surprisingly, whereas SnoN typically operates as a transcriptional corepressor (Luo 2004;Pot and Bonni 2008), SnoN acts as a transcriptional activator in promoting axon growth ). SnoN forms a complex with the transcriptional coactivator p300 and stimulates expression of the signaling scaffold protein Ccd1 (Fig.…”

Section: Regulation Of Neuronal Morphogenesis By Cdh1-apc and Cdc20-apcmentioning

confidence: 99%

A decade of the anaphase-promoting complex in the nervous system

Huang

Bonni

2016

Genes Dev.

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Control of protein abundance by the ubiquitin-proteasome system is essential for normal brain development and function. Just over a decade ago, the first post-mitotic function of the anaphase-promoting complex, a major cell cycle-regulated E3 ubiquitin ligase, was discovered in the control of axon growth and patterning in the mammalian brain. Since then, a large number of studies have identified additional novel roles for the anaphase-promoting complex in diverse aspects of neuronal connectivity and plasticity in the developing and mature nervous system. In this review, we discuss the functions and mechanisms of the anaphase-promoting complex in neurogenesis, glial differentiation and migration, neuronal survival and metabolism, neuronal morphogenesis, synapse formation and plasticity, and learning and memory. We also provide a perspective on future investigations of the anaphase-promoting complex in neurobiology.Protein degradation regulates diverse biological processes in the developing and mature nervous system. Spatial and temporal control of protein turnover and abundance influences distinct stages of neural development and function from neurogenesis and neuronal morphogenesis to synapse formation and pruning to plasticity and learning (Hegde and Upadhya 2007;Yi and Ehlers 2007;Segref and Hoppe 2009;Yamada et al. 2013). Protein degradation by the proteasome requires ubiquitination, which is mediated by the sequential action of an E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzyme, and E3 ubiquitin ligase (Hershko and Ciechanover 1992;Scheffner et al. 1995;Ciechanover 2005;Hershko 2005;Weissman et al.

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SnoN in TGF-β Signaling and Cancer Biology

Cited by 28 publications

References 130 publications

SnoN as a Key Regulator of the High Glucose-Induced Epithelial-Mesenchymal Transition in Cells of the Proximal Tubule

SnoN as a Key Regulator of the High Glucose-Induced Epithelial-Mesenchymal Transition in Cells of the Proximal Tubule

The Role of SnoN in Transforming Growth Factor β1-induced Expression of Metalloprotease-Disintegrin ADAM12

A decade of the anaphase-promoting complex in the nervous system

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