ArticleMolecules and cells2013
Structure of the catalytic domain of protein tyrosine phosphatase sigma in the sulfenic acid form.
Article in Molecules and cells, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 12 citations in OpenAlex.
- Receptor Protein Tyrosine Phosphatases (RPTPs): Structure and Biological Roles in Cancer.Kinases and phosphatases · 2026Article
- Protein Tyrosine Phosphatase regulation by Reactive Oxygen Species.Advances in cancer research · 2024Review
- RPTPα phosphatase activity is allosterically regulated by the membrane-distal catalytic domain.The Journal of biological chemistry · 2020Article
- PTPσ inhibitors promote hematopoietic stem cell regeneration.Nature communications · 2019Article
- Biological chemistry and functionality of protein sulfenic acids and related thiol modifications.Free radical research · 2016Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein tyrosine phosphatase sigma (PTPσ) plays a vital role in neural development. The extracellular domain of PTPσ binds to various proteoglycans, which control the activity of 2 intracellular PTP domains (D1 and D2). To understand the regulatory mechanism of PTPσ, we carried out structural and biochemical analyses of PTPσ D1D2. In the crystal structure analysis of a mutant form of D1D2 of PTPσ, we unexpectedly found that the catalytic cysteine of D1 is oxidized to cysteine sulfenic acid, while that of D2 remained in its reduced form, suggesting that D1 is more sensitive to oxidation than D2. This finding contrasts previous observations on PTPα. The cysteine sulfenic acid of D1 was further confirmed by immunoblot and mass spectrometric analyses. The stabilization of the cysteine sulfenic acid in the active site of PTP suggests that the formation of cysteine sulfenic acid may function as a stable intermediate during the redox-regulation of PTPs.
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