Protein tyrosine phosphatases

Mustelin, Tomas

doi:10.2741/mustelin

Cited by 34 publications

(3 citation statements)

References 453 publications

(674 reference statements)

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“…Protein phosphorylation occurs on serine, threonine or tyrosine residues. Although the extent of phosphorylation on tyrosine residues is found to be the least compared to the other two (3), tyrosine phosphorylation is a unique characteristic of eukaryote and multicellular signaling (4). Protein tyrosine phosphatases (PTPs) constitute a large protein family with more than ∼100 genes in human (5-7).…”

Section: Introductionmentioning

confidence: 99%

Structure and catalytic mechanism of human protein tyrosine phosphatome

Kim

Ryu

2012

BMB Reports

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Together with protein tyrosine kinases (PTKs), protein tyrosine phosphatases (PTPs) serve as hallmarks in cellular signal transduction by controlling the reversible phosphorylation of their substrates. The human genome is estimated to encode more than 100 PTPs, which can be divided into eleven sub-groups according to their structural and functional characteristics. All the crystal structures of catalytic domains of sub-groups have been elucidated, enabling us to understand their precise catalytic mechanism and to compare their structures across all sub-groups. In this review, I describe the structure and mechanism of catalytic domains of PTPs in the structural context. [BMB Reports 2012; 45(12): 693-699]

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Section: Introductionmentioning

confidence: 99%

Structure and catalytic mechanism of human protein tyrosine phosphatome

Kim

Ryu

2012

BMB Reports

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“…Reversible tyrosine phosphorylation regulates important signaling pathways involved in the control of adhesion, differentiation, and proliferation. Although equal and balanced activities of PTKs and PTPs have been reported in many physiological processes, the recent findings of several studies contribute to the idea that PTPs have specific, active and even dominant roles in tyrosine phosphorylation (6,7). Furthermore, several PTPs seem to act as biochemical “on” or “off” switches and as key regulators in many intracellular signaling pathways (8).…”

Section: Introductionmentioning

confidence: 99%

Involvement of protein tyrosine phosphatases in adipogenesis: New anti-obesity targets?

Bae¹,

Kim²,

Lee³

2012

BMB Reports

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Obesity is a worldwide epidemic as well as being a major risk factor for diabetes, cardiovascular diseases and several types of cancers. Obesity is mainly due to the overgrowth of adipose tissue arising from an imbalance between energy intake and energy expenditure. Adipose tissue, primarily composed of adipocytes, plays a key role in maintaining whole body energy homeostasis. In view of the treatment of obesity and obesity-related diseases, it is critical to understand the detailed signal transduction mechanisms of adipogenic differentiation. Adipogenic differentiation is tightly regulated by many key signal cascades, including insulin signaling. These signal cascades generally transfer or amplify the signal by using serial tyrosine phosphorylations. Thus, protein tyrosine kinases and protein tyrosine phosphatases are closely related to adipogenic differentiation. Compared to protein tyrosine kinases, protein tyrosine phosphatases have received little attention in adipogenic differentiation. This review aims to highlight the involvement of protein tyrosine phosphatases in adipogenic differentiation and the possibility of protein tyrosine phosphatases as drugs to target obesity. [BMB Reports 2012; 45(12): 700-706]

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“…Protein tyrosine phosphatases (PTPs) are a sort of fundamental phosphatases responsible for the dephosphorylation of phosphorylated tyrosines in proteins that are involved in various biological processes including embryogenesis, organ development, tissue homeostasis, and the immune defenses in multicellular eukaryotes ( 1 , 2 ). To date, more than 100 PTPs have been identified in the human genome and most of them possess non-redundant functions verified by the unique phenotypes of many reported gene deletions in mice ( 3 , 4 ).…”

Section: Introductionmentioning

confidence: 99%

The Non-Receptor Protein Tyrosine Phosphatase PTPN6 Mediates a Positive Regulatory Approach From the Interferon Regulatory Factor to the JAK/STAT Pathway in Litopenaeus vannamei

Luo

Liu

et al. 2022

Front. Immunol.

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SH2-domain-containing protein tyrosine phosphatases (PTPs), belonging to the class I PTP superfamily, are responsible for the dephosphorylation on the phosphorylated tyrosine residues in some proteins that are involved in multiple biological processes in eukaryotes. The Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway transduce signaling responding to interferons and initiate cellular antiviral responses. The activity of the JAK/STAT pathway is generally orchestrated by the de-/phosphorylation of the tyrosine and serine residues of JAKs and STATs, in which the dephosphorylation processes are mainly controlled by PTPs. In the present study, an SH2-domian-contianing PTP, temporally named as LvPTPN6, was identified in Litopenaeus vannamei. LvPTPN6 shares high similarity with PTPN6s from other organisms and was phylogenetically categorized into the clade of arthropods that differs from those of fishes and mammals. LvPTPN6 was constitutively expressed in all detected tissues, located mainly in the cytoplasm, and differentially induced in hemocyte and gill after the challenge of stimulants, indicating its complicated regulatory roles in shrimp immune responses. Intriguingly, the expression of LvPTPN6 was regulated by interferon regulatory factor (IRF), which could directly bind to the LvPTPN6 promoter. Surprisingly, unlike other PTPN6s, LvPTPN6 could promote the dimerization of STAT and facilitate its nuclear localization, which further elevated the expression of STAT-targeting immune effector genes and enhanced the antiviral immunity of shrimp. Therefore, this study suggests a PTPN6-mediated regulatory approach from IRF to the JAK/STAT signaling pathway in shrimp, which provides new insights into the regulatory roles of PTPs in the JAK/STAT signaling pathway and contributes to the further understanding of the mechanisms of antiviral immunity in invertebrates.

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Protein tyrosine phosphatases

Cited by 34 publications

References 453 publications

Structure and catalytic mechanism of human protein tyrosine phosphatome

Structure and catalytic mechanism of human protein tyrosine phosphatome

Involvement of protein tyrosine phosphatases in adipogenesis: New anti-obesity targets?

The Non-Receptor Protein Tyrosine Phosphatase PTPN6 Mediates a Positive Regulatory Approach From the Interferon Regulatory Factor to the JAK/STAT Pathway in Litopenaeus vannamei

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