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

Published online July 31, 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
Jul 31, 2022 Vol.45 No.7, pp. 435~512
COVER PICTURE
Mesenchymal stem cells (MSCs) are multipotent stem cells capable of differentiating into mesodermal lineages like adipogenic, osteogenic, and chondrogenic. Alcian blue-positive extracellular matrix secreted by chondrocytes in the lacuna confirmed the chondrogenic differentiation of MSCs (Bashyal et al., pp. 479-494).

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