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Mol. Cells 2013; 36(1): 55-61

Published online May 30, 2013

https://doi.org/10.1007/s10059-013-0033-x

© The Korean Society for Molecular and Cellular Biology

Structure of the Catalytic Domain of Protein Tyrosine Phosphatase Sigma in the Sulfenic Acid Form

Tae Jin Jeon, Pham Ngoc Chien, Ha-Jung Chun, and Seong Eon Ryu

1Department of Bioengineering, College of Engineering, 2Department of Radiation Oncology, College of Medicine, Hanyang University, Seoul 133-070, Korea, 3These authors contributed equally to this work.

Received: January 30, 2013; Revised: April 15, 2013; Accepted: April 18, 2013

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.

Keywords crystal structure, protein tyrosine phosphatase sigma, proteoglycan, redox regulation, sulfenic acid

Article

Research Article

Mol. Cells 2013; 36(1): 55-61

Published online July 31, 2013 https://doi.org/10.1007/s10059-013-0033-x

Copyright © The Korean Society for Molecular and Cellular Biology.

Structure of the Catalytic Domain of Protein Tyrosine Phosphatase Sigma in the Sulfenic Acid Form

Tae Jin Jeon, Pham Ngoc Chien, Ha-Jung Chun, and Seong Eon Ryu

1Department of Bioengineering, College of Engineering, 2Department of Radiation Oncology, College of Medicine, Hanyang University, Seoul 133-070, Korea, 3These authors contributed equally to this work.

Received: January 30, 2013; Revised: April 15, 2013; Accepted: April 18, 2013

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.

Keywords: crystal structure, protein tyrosine phosphatase sigma, proteoglycan, redox regulation, sulfenic acid

Mol. Cells
Feb 28, 2023 Vol.46 No.2, pp. 69~129
COVER PICTURE
The bulk tissue is a heterogeneous mixture of various cell types, which is depicted as a skein of intertwined threads with diverse colors each of which represents a unique cell type. Single-cell omics analysis untangles efficiently the skein according to the color by providing information of molecules at individual cells and interpretation of such information based on different cell types. The molecules that can be profiled at the individual cell by single-cell omics analysis includes DNA (bottom middle), RNA (bottom right), and protein (bottom left). This special issue reviews single-cell technologies and computational methods that have been developed for the single-cell omics analysis and how they have been applied to improve our understanding of the underlying mechanisms of biological and pathological phenomena at the single-cell level.

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