Hypoxia-driven cell motility reflects the interplay between JMY and HIF-1α

Coutts, Amanda S.; Pires, Isabel; Weston, Louise; Buffa, Francesca M.; Milani, Manuela; Li, JL; Harris, Adrian L.; Hammond, Ester M.; Thangue, N B La

doi:10.1038/onc.2011.188

Cited by 36 publications

(37 citation statements)

References 26 publications

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“…As a protein promoting cell invasion [12], it might have therapeutic relevance [8]. However, its role is dichotomous as it also has a tumor suppressive activity in enhancing P53 activity [1].…”

Section: Discussionmentioning

confidence: 99%

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JMY protein, a regulator of P53 and cytoplasmic actin filaments, is expressed in normal and neoplastic tissues

et al. 2014

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JMY is a p300-binding protein with dual action: by enhancing P53 transcription in the nucleus, it plays an important role in the cellular response to DNA damage, while by promoting actin filament assembly in the cytoplasm; it induces cell motility in vitro. Therefore, it has been argued that, depending of the cellular setting, it might act either as tumor suppressor or as oncogene. In order to further determine its relevance to human cancer, we produced the monoclonal antibody HMY 117 against a synthetic peptide from the N-terminus region and characterized it on two JMY positive cell lines, MCF7 and HeLa, wild type and after transfection with siRNA to switch off JMY expression. JMY was expressed in normal tissues and heterogeneously in different tumor types, with close correlation between cytoplasmic and nuclear expression. Most noticeable was the loss of expression in some infiltrating carcinomas compared to normal tissue and in in situ carcinomas of the breast, which is consistent with a putative suppressor role. However, as in lymph node metastases, expression of JMY was higher than in primary colorectal and head and neck carcinomas, it might also have oncogenic properties depending on the cellular context by increasing motility and metastatic potential.

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Section: Discussionmentioning

confidence: 99%

“…JMY over-expression is associated with increased speed of cellular migration [5]. Finally, following exposure to hypoxia, JMY expression and cytoplasmic colocalization with actin are increased under HIF1 stimulation, which induces cell motility [8].…”

Section: Introductionmentioning

confidence: 99%

JMY protein, a regulator of P53 and cytoplasmic actin filaments, is expressed in normal and neoplastic tissues

et al. 2014

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“…Cell migration was assessed using 16-well CIM-plates 16 as described. 28,43 DMEM/10% FBS was added to the lower chamber as chemotractant and cells were seeded into the upper chamber at 40 000/well in serum free medium.…”

Section: Measurement Of Cellular Proliferation and Motility Using Thementioning

confidence: 99%

HIF-1α-independent hypoxia-induced rapid PTK6 stabilization is associated with increased motility and invasion

Pires

Blokland

Broos

et al. 2014

Cancer Biology & Therapy

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“…JMY over expression was found to be associated with increased speed of migrating cells [12]. Additionally, JMY expression and cytoplasmic co-localization with actin is increased under HIF1 stimulation [25]. Of note is that actin filament facilitates cell motility and migration.…”

Section: Jmy and Cell Motilitymentioning

confidence: 92%

The Role of JMY in p53 Regulation.

Adighibe¹

2018

Preprint

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Abstract:Following the event of DNA damage the levels of tumour suppressor protein p53 increases inducing either cell cycle arrest or apoptosis. Junctional Mediating and Regulating Y protein (JMY) is a transcription co-factor involved in p53 regulation. Hence in the event of DNA damage, JMY levels are also upregulated in the nucleus where JMY forms a complex with p300/CREB-binding protein (p300/CBP), Apoptosis-stimulating protein of p53 (ASPP) and Stress responsive activator of p53 (Strap). This co-activator complex then binds to and increases the ability of p53 to induce transcription of proteins triggering apoptosis but not cell cycle arrest. This then suggests that the increase of JMY levels due to DNA damage putatively "direct" p53 activity toward triggering apoptosis. JMY expression is also linked to increased cell motility as it: downregulates the expression of adhesion molecules of the Cadherin family and induces actin nucleation; making cells less adhesive and more mobile, favouring metastasis.All these characteristics taken together imply that JMY therefore possesses both tumour suppressive and tumour promoting capabilities.

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Hypoxia-driven cell motility reflects the interplay between JMY and HIF-1α

Cited by 36 publications

References 26 publications

JMY protein, a regulator of P53 and cytoplasmic actin filaments, is expressed in normal and neoplastic tissues

JMY protein, a regulator of P53 and cytoplasmic actin filaments, is expressed in normal and neoplastic tissues

HIF-1α-independent hypoxia-induced rapid PTK6 stabilization is associated with increased motility and invasion

The Role of JMY in p53 Regulation.

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