Structure and catalytic mechanism of human protein tyrosine phosphatome

Kim, Seung Jun; Ryu, Seong Eon

doi:10.5483/bmbrep.2012.45.12.240

Cited by 19 publications

(17 citation statements)

References 55 publications

(59 reference statements)

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“…Such clas sification is confirmed with the results of experimental genomics [6]. Some protein phosphatases that were determined as serine/threonine specific, are able to dephosphorylate tyrosine residues [1,7,8]. Besides, it was found that certain animal phosphatases with dual specificity are able to dephosphorylate proteins on cysteine, arginine, lysine, asparagine, histidine, and glutamic acid residues [1,[9][10][11][12][13].…”

Section: Introductionsupporting

confidence: 70%

Bioinformatic comparison of human and higher plant phosphatomes

2015

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The study presents the results of bioinformatic comparison of protein phosphatases from higher plants and human phosphatome (150 proteins). Based on sequence and profile comparison with known cat alytic domains, 204 plant homologues were selected from Physcomitrella patens and Arabidopsis thaliana. Clustering of joint group of plant and animal protein phosphatases revealed fundamental differences in plant and human phosphatomes. At the same time, significant differences in the sets of protein phosphatases in P. patens, A. thaliana, Orysa sativa, and Zea mays were shown. The percent indicators (Ident. (%) -identity, Simil. (%) -similarity, Gap. (%) -gaps) of sequence similarity are given based on the results of pairwise alignment of catalytic domain of human protein phosphatase and appropriate region of the plant homologue. The percent indicators (Ident. (%) -identity, Simil. (%) -similarity, Gap. (%) -gaps) of sequence similarity are given based on the results of pairwise alignment of catalytic domain of human protein phosphatase and appropriate region of the plant homologue.

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Section: Introductionsupporting

confidence: 70%

Bioinformatic comparison of human and higher plant phosphatomes

2015

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“…The presence of the thiophosphate bond was further confirmed by stability to hydroxylamine and lability to iodine‐treatment, all of which serve to differentiate thiophosphates from acylphosphates . A mechanism was proposed whereby the active site cysteine nucleophilically attacks the phosphorus atom of the phosphotyrosine to generate the pCys‐intermediate, which is then subject to hydrolysis by water . This cysteine‐dependent hydrolysis mechanism is now generally accepted and although transient, the pCys on PTPs are known to exist long enough to facilitate detection by gel‐based methods…”

Section: Cysteine Phosphorylationmentioning

confidence: 99%

Orphan PTMs: Rare, yet functionally important modifications of cysteine

Shannon

Weerapana

2013

Biopolymers

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The enhanced nucleophilicity and redox sensitivity of the thiol group renders cysteine residues susceptible to numerous electrophilic and oxidative post-translational modifications to form disulfides, sulfenic acids, nitrosothiols, and lipid-modified species. Outside of these well-characterized modifications of cysteine, there are reports of cysteine modification through phosphorylation, methylation, and ubiquitination. Although these post-translational modifications are highly abundant on other amino acids, they play a less pervasive role in cysteine biology. Despite the rarity of these modifications of cysteine, they have been shown to play critical roles in catalysis and regulation. Here we describe these rare post-translational modifications of cysteine in detail, by describing their discovery and functional characterization on diverse proteins. Furthermore, we highlight potential proteomic tools that may aid in globally identifying these modifications to fully elucidate their abundance in biological systems.

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“…This observation suggests that the new complex could have some selectivity towards specific CBPs compared to others, inhibiting better phosphatases with a large catalytic pocket (e.g. PTEN), 33 or interacting with specific secondary substrate binding sites (e.g. in the case of SHP2 and LMW-PTP).…”

Section: Synthesis Of the Trifunctional Optical Probementioning

confidence: 99%

A tri-functional vanadium(iv) complex to detect cysteine oxidation

et al. 2017

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The development of effective molecular probes to detect and image the levels of oxidative stress in cells remains a challenge. Herein we report the design, synthesis and preliminary biological evaluation of a novel optical probe to monitor oxidation of thiol groups in cysteine-based phosphatases (CBPs). Following orthogonal protecting approaches we synthesised a new vanadyl complex designed to bind to CBPs. This complex is functionalised with a well-known dimedone derivative (to covalently trap sulfenic acids, SOHs) and a coumarin-based fluorophore for optical visualization. We show that this new probe efficiently binds to a range of phosphatases in vitro with nanomolar affinity. Moreover, preliminary flow cytometry and microscopy studies in live HCT116 cells show that this probe can successfully image cellular levels of sulfenic acids -one of the species resulting from protein oxidative damage.

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Structure and catalytic mechanism of human protein tyrosine phosphatome

Cited by 19 publications

References 55 publications

Bioinformatic comparison of human and higher plant phosphatomes

Bioinformatic comparison of human and higher plant phosphatomes

Orphan PTMs: Rare, yet functionally important modifications of cysteine

A tri-functional vanadium(iv) complex to detect cysteine oxidation

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