Dual Specificity Phosphatases: From Molecular Mechanisms to Biological Function

Dual specificity phosphatases (DUSPs) constitute a heterogeneous group of protein tyrosine phosphatases with the ability to dephosphorylate Ser/Thr and Tyr residues from proteins, as well as from other non-proteinaceous substrates including signaling lipids. DUSPs include, among others, MAP kinase (...

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Main Author: Pulido, Rafael (auth)
Other Authors: Lang, Roland (auth)
Format: Electronic Book Chapter
Language:English
Published: MDPI - Multidisciplinary Digital Publishing Institute 2019
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DOAB: description of the publication
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520 |a Dual specificity phosphatases (DUSPs) constitute a heterogeneous group of protein tyrosine phosphatases with the ability to dephosphorylate Ser/Thr and Tyr residues from proteins, as well as from other non-proteinaceous substrates including signaling lipids. DUSPs include, among others, MAP kinase (MAPK) phosphatases (MKPs) and small-size atypical DUSPs. MKPs are enzymes specialized in regulating the activity and subcellular location of MAPKs, whereas the function of small-size atypical DUSPs seems to be more diverse. DUSPs have emerged as key players in the regulation of cell growth, differentiation, stress response, and apoptosis. DUSPs regulate essential physiological processes, including immunity, neurobiology and metabolic homeostasis, and have been implicated in tumorigenesis, pathological inflammation and metabolic disorders. Accordingly, alterations in the expression or function of MKPs and small-size atypical DUSPs have consequences essential to human disease, making these enzymes potential biological markers and therapeutic targets. This Special Issue covers recent advances in the molecular mechanisms and biological functions of MKPs and small-size atypical DUSPs, and their relevance in human disease. 
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653 |a hematopoietic cells 
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653 |a liver steatosis 
653 |a MAPK phosphatase 
653 |a DUSP-4 
653 |a granule neurons 
653 |a neuronal differentiation 
653 |a DUSP10 
653 |a cytokines 
653 |a MAPKs 
653 |a single cell analysis 
653 |a macrophage 
653 |a asthma 
653 |a E. coli infection 
653 |a MAPK 
653 |a Cpp1 
653 |a nucleotide receptors 
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653 |a RSV 
653 |a Pmp1 
653 |a cannabinoids 
653 |a astrocytes 
653 |a sepsis 
653 |a influenza 
653 |a signaling 
653 |a triple-negative breast cancer (TNBC) 
653 |a differentiation 
653 |a HDAC6 (histone deacetylase isoform 6) 
653 |a atypical dual-specificity phosphatases 
653 |a microtubules 
653 |a respiratory viruses 
653 |a MK-STYX (MAPK (mitogen-activated protein kinase) phosphoserine/threonine/tyrosine-binding protein) 
653 |a dual-specificity phosphatase 
653 |a Msg5 
653 |a TLR signaling 
653 |a mitogen-activated protein kinase 
653 |a fungal MKPs 
653 |a macrophages 
653 |a MAP Kinase Phosphatase-2 
653 |a inflammation 
653 |a Sdp1 
653 |a circulating tumor cells (CTCs) 
653 |a MAP kinases 
653 |a MAP kinase phosphatases 
653 |a P2X7 
653 |a proliferation 
653 |a BDNF 
653 |a P2Y13 
653 |a T cell 
653 |a hypertriglyceridemia 
653 |a integrated omics analysis 
653 |a post-translational modification 
653 |a rhinovirus 
653 |a protein stability 
653 |a ubiquitination 
653 |a dual-specificity phosphatases 
653 |a Mkp-1 
653 |a cancer 
653 |a brain metastasis 
653 |a HER2 
653 |a COPD 
653 |a pseudophosphatase 
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