Does the dual-specificity MAPK phosphatase Pyst2-L lead a monogamous relationship with the Erk2 protein?

Levy-Nissenbaum, Orlev; Ehud, Barak; Tamar, Burg-Golani; Sagi‐Assif, Orit; Kloog, Y.; Witz, Isaac P.

doi:10.1016/j.imlet.2003.11.024

Cited by 12 publications

(10 citation statements)

References 40 publications

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“…It should be pointed out that the observation of low pERKs levels in contactinhibited culture was already reported [46]. These results are in accordance with our recent study, showing a negative correlation between Pyst2-L expression and pERK levels [22,24]. Since pERK is one of the known Pyst2-L substrates, it is expected that whenever the Pyst2-L phosphatase is active, the levels of pERK would decrease.…”

Section: Discussionsupporting

confidence: 92%

“…Other in vitro assays support the fact that the Pyst2-L phosphatase preferentially selects the ERK2 protein as its substrate [17,19]. However, utilizing the "Pull-Down" methodology, we were able to demonstrate that in addition to ERK2, Pyst2-L binds and dephosphorylates the JNKs proteins [24]. This was supported by further un-published results demonstrating that the Pyst2-L phosphatase plays a role in the JNK signaling pathway and in the cross-talk between the signaling pathways of ERK and JNK.…”

Section: Introductionmentioning

confidence: 61%

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The Pyst2-L phosphatase is involved in cell-crowding

et al. 2006

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Section: Discussionsupporting

confidence: 92%

Section: Introductionmentioning

confidence: 61%

The Pyst2-L phosphatase is involved in cell-crowding

et al. 2006

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“…DUSP7, DUSP12, DUSP13B, and DUSP18 have also been analyzed as dephosphorylating and inactivating regulators of JNK [73,83,95,114]. When DUSP12 was overexpressed in RAW264.7 cells that were stimulated with LPS, the level of p-JNK was significantly reduced over time compared with control cells [114].…”

Section: Negative Regulation Of Jnk By Duspsmentioning

confidence: 99%

Phosphorylation Dynamics of JNK Signaling: Effects of Dual-Specificity Phosphatases (DUSPs) on the JNK Pathway

Kang

Seo

et al. 2019

IJMS

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Protein phosphorylation affects conformational change, interaction, catalytic activity, and subcellular localization of proteins. Because the post-modification of proteins regulates diverse cellular signaling pathways, the precise control of phosphorylation states is essential for maintaining cellular homeostasis. Kinases function as phosphorylating enzymes, and phosphatases dephosphorylate their target substrates, typically in a much shorter time. The c-Jun N-terminal kinase (JNK) signaling pathway, a mitogen-activated protein kinase pathway, is regulated by a cascade of kinases and in turn regulates other physiological processes, such as cell differentiation, apoptosis, neuronal functions, and embryonic development. However, the activation of the JNK pathway is also implicated in human pathologies such as cancer, neurodegenerative diseases, and inflammatory diseases. Therefore, the proper balance between activation and inactivation of the JNK pathway needs to be tightly regulated. Dual specificity phosphatases (DUSPs) regulate the magnitude and duration of signal transduction of the JNK pathway by dephosphorylating their substrates. In this review, we will discuss the dynamics of phosphorylation/dephosphorylation, the mechanism of JNK pathway regulation by DUSPs, and the new possibilities of targeting DUSPs in JNK-related diseases elucidated in recent studies.

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“…Although regulation of MAPKs by a phosphorylation cascade has long been recognized as significant, their inactivation through the action of specific phosphatases has been less studied. An emerging family of structurally distinct dualspecificity serine, threonine, and tyrosine phosphatases that act on MAPKs consists of 10 members in mammals, and members have been found in animals, plants, and yeast [108].…”

Section: Mapk Signaling and Redox-mediated Regulation Of Kinases/phosmentioning

confidence: 99%

Hypoxia and the regulation of mitogen-activated protein kinases: gene transcription and the assessment of potential pharmacologic therapeutic interventions

Haddad

2004

International Immunopharmacology

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Does the dual-specificity MAPK phosphatase Pyst2-L lead a monogamous relationship with the Erk2 protein?

Cited by 12 publications

References 40 publications

The Pyst2-L phosphatase is involved in cell-crowding

The Pyst2-L phosphatase is involved in cell-crowding

Phosphorylation Dynamics of JNK Signaling: Effects of Dual-Specificity Phosphatases (DUSPs) on the JNK Pathway

Hypoxia and the regulation of mitogen-activated protein kinases: gene transcription and the assessment of potential pharmacologic therapeutic interventions

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