Clues to the evolution of complex signaling machinery

Mayer, Bruce J.

doi:10.1073/pnas.0804669105

Cited by 19 publications

(24 citation statements)

References 10 publications

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“…organisms to metazoans), there are few recognizable tyrosine kinases, protein tyrosine phosphatases, or SH2 domain-containing proteins in the protozoa (54,55,64). Then how is it that ROP16 can be a tyrosine kinase for this signaling module?…”

Section: Understanding Rop16 and In Vivo Stat3 And Stat6 Activationmentioning

confidence: 99%

An Inside Job: Hacking into Janus Kinase/Signal Transducer and Activator of Transcription Signaling Cascades by the Intracellular Protozoan Toxoplasma gondii

Denkers

Bzik²,

Fox³

et al. 2012

Infect Immun

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The intracellular protozoan Toxoplasma gondii is well known for its skill at invading and living within host cells. New discoveries are now also revealing the astounding ability of the parasite to inject effector proteins into the cytoplasm to seize control of the host cell. This review summarizes recent advances in our understanding of one such secretory protein called ROP16. This molecule is released from rhoptries into the host cell during invasion. The ROP16 molecule acts as a kinase, directly activating both signal transducer and activator of transcription 3 (STAT3) and STAT6 signaling pathways. In macrophages, an important and preferential target cell of parasite infection, the injection of ROP16 has multiple consequences, including downregulation of proinflammatory cytokine signaling and macrophage deviation to an alternatively activated phenotype.

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Section: Understanding Rop16 and In Vivo Stat3 And Stat6 Activationmentioning

confidence: 99%

An Inside Job: Hacking into Janus Kinase/Signal Transducer and Activator of Transcription Signaling Cascades by the Intracellular Protozoan Toxoplasma gondii

Denkers

Bzik²,

Fox³

et al. 2012

Infect Immun

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“…The covalent addition of a phosphate group to tyrosine residues in cellular proteins may occur as an appropriate response to a series of morphological and biochemical processes, with particular importance in complex functions such as growth, proliferation, differentiation, adhesion and motility. Protein tyrosine phosphorylation is regulated in the cell by the opposing activities of two classes of enzymes: protein tyrosine kinases, which phosphorylate specific tyrosine residues in protein using ATP as the phosphate source, and protein tyrosine phosphatases, which hydrolyze the phosphotyrosines yielding the restored amino acid residue and inorganic phosphate as products (Kolmodin & Åqvist, 2001;Mayer, 2008). The number of active protein phosphatases with the ability to dephosphorylate phosphotyrosine are very similar to the number of active tyrosine phosphatases.…”

Section: Introductionmentioning

confidence: 92%

Reversible Inhibition of Tyrosine Protein Phosphatases by Redox Reactions

Cosentino-Gomes¹,

Meyer‐Fernandes²

2012

Enzyme Inhibition and Bioapplications

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“…This signaling mechanism depends on the interplay of protein tyrosine kinases, which initiate signaling cascades through phosphorylating tyrosine residues in protein substrates, and by protein tyrosine phosphatases that terminate signaling via substrate dephosphorylation. Functionally, the most important effect of tyrosine phosphorylation is to create high-affinity binding sites for other proteins containing small modular phosphotyrosine (pTyr)-binding domains, most notably Src homology 2 (SH2) domains [5]. Any deviation in balance between PTP and PTK can promote abnormal cell proliferation and differentiation thereby resulting in different kinds of diseases [6][7][8].…”

Section: Introductionmentioning

confidence: 99%

Phosphotyrosine Phosphatases in Cancer Diagnostic and Treatment

Tiscornia

Riera²,

Lorenzati³

et al. 2010

DNAG

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The activation of proteins by post-translational modification represents an important cellular mechanism for regulating most aspects of biological organization and control, including growth, development, homeostasis, and cellular communication. The complexity of protein modification includes phosphorylation and dephosphorylation, on proteins of different signaling pathways corresponding to growth, development, disease states, and aging. Current patents in phosphotyrosine phosphatases signaling pathway are focusing in diagnosis, prognosis and treatment. Many, new diagnosis techniques detect changes in mRNA expression with microarray technologies and others introduced specific antibodies for detection proteins changes, introducing to Biomedicine at Transcriptomic and Proteomic era. Many recent invent development alternative therapy with antibodies and inhibitors to PTPs that demonstrate the need to deepen understanding of the molecular mechanisms involved in the development of cancer.

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Clues to the evolution of complex signaling machinery

Cited by 19 publications

References 10 publications

An Inside Job: Hacking into Janus Kinase/Signal Transducer and Activator of Transcription Signaling Cascades by the Intracellular Protozoan Toxoplasma gondii

An Inside Job: Hacking into Janus Kinase/Signal Transducer and Activator of Transcription Signaling Cascades by the Intracellular Protozoan Toxoplasma gondii

Reversible Inhibition of Tyrosine Protein Phosphatases by Redox Reactions

Phosphotyrosine Phosphatases in Cancer Diagnostic and Treatment

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