Biochemical and functional studies of Lymphoid-specific tyrosine phosphatase (Lyp) variants S201F and R266W

PLoS ONE

Volumn 7, Issue 8, 2012, Pages

  Liu, Jing ^a   Chen, Ming ^b   Li, Rong ^a   Yang, Fan ^a   Shi, Xuanren ^a   Zhu, Lichao ^a   Wang, Hong Mei ^a   Yao, Wei ^a   Liu, Qiji ^a   Meng, Fan Guo ^c   Sun, Jin Peng ^a,d   Pang, Qi ^d   Yu, Xiao ^a  

^a SHANDONG UNIVERSITY SCHOOL OF MEDICINE   (China)

^b 309TH HOSPITAL OF PLA   (China)

^c TSINGHUA UNIVERSITY   (China)

^d SHANDONG UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; GLUTAMINE; LYMPHOID SPECIFIC TYROSINE PHOSPHATASE; PHENYLALANINE; PHOSPHATASE; SERINE; TRYPTOPHAN; UNCLASSIFIED DRUG;

ARTICLE; AUTOIMMUNE DISEASE; ENZYME ACTIVITY; ENZYME STRUCTURE; GENETIC POLYMORPHISM; LOSS OF FUNCTION MUTATION; MUTANT; PROTEIN FUNCTION; RHEUMATOID ARTHRITIS; SIGNAL TRANSDUCTION; SYSTEMIC LUPUS ERYTHEMATOSUS; T LYMPHOCYTE; ULCERATIVE COLITIS;

AMINO ACID SEQUENCE; CATALYTIC DOMAIN; HUMANS; JURKAT CELLS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NITROPHENOLS; PHOSPHOPROTEINS; POLYMORPHISM, SINGLE NUCLEOTIDE; PROTEIN TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 22; PROTO-ONCOGENE PROTEINS PP60(C-SRC); SIGNAL TRANSDUCTION; T-LYMPHOCYTES;

EID: 84865422376     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0043631     Document Type: Article

References (41)

1. Weiss A, (1993) T cell antigen receptor signal transduction: a tale of tails and cytoplasmic protein-tyrosine kinases. Cell 73: 209-212.
2. Mustelin T, Vang T, Bottini N, (2005) Protein tyrosine phosphatases and the immune response. Nat Rev Immunol 5: 43-57.
3. Zhu JW, Doan K, Park J, Chau AH, Zhang H, et al. (2011) Receptor-like tyrosine phosphatases CD45 and CD148 have distinct functions in chemoattractant-mediated neutrophil migration and response to S. aureus. Immunity 35: 757-769.
4. Kleppe M, Soulier J, Asnafi V, Mentens N, Hornakova T, et al. (2011) PTPN2 negatively regulates oncogenic JAK1 in T-cell acute lymphoblastic leukemia. Blood 117: 7090-7098.
5. Bottini N, Musumeci L, Alonso A, Rahmouni S, Nika K, et al. (2004) A functional variant of lymphoid tyrosine phosphatase is associated with type I diabetes. Nat Genet 36: 337-338.
6. Maziarz M, Janer M, Roach JC, Hagopian W, Palmer JP, et al. (2010) The association between the PTPN22 1858C>T variant and type 1 diabetes depends on HLA risk and GAD65 autoantibodies. Genes Immun 11: 406-415.
7. Begovich AB, Carlton VE, Honigberg LA, Schrodi SJ, Chokkalingam AP, et al. (2004) A missense single-nucleotide polymorphism in a gene encoding a protein tyrosine phosphatase (PTPN22) is associated with rheumatoid arthritis. Am J Hum Genet 75: 330-337.
8. Totaro MC, Tolusso B, Napolioni V, Faustini F, Canestri S, et al. (2011) PTPN22 1858C>T polymorphism distribution in Europe and association with rheumatoid arthritis: case-control study and meta-analysis. PLoS One 6: e24292.
9. Kyogoku C, Langefeld CD, Ortmann WA, Lee A, Selby S, et al. (2004) Genetic association of the R620W polymorphism of protein tyrosine phosphatase PTPN22 with human SLE. Am J Hum Genet 75: 504-507.
10. Lea WW, Lee YH, (2011) The association between the PTPN22 C1858T polymorphism and systemic lupus erythematosus: a meta-analysis update. Lupus 20: 51-57.
11. Vang T, Congia M, Macis MD, Musumeci L, Orru V, et al. (2005) Autoimmune-associated lymphoid tyrosine phosphatase is a gain-of-function variant. Nat Genet 37: 1317-1319.
12. Yu X, Sun JP, He Y, Guo X, Liu S, et al. (2007) Structure, inhibitor, and regulatory mechanism of Lyp, a lymphoid-specific tyrosine phosphatase implicated in autoimmune diseases. Proc Natl Acad Sci U S A 104: 19767-19772.
13. Fiorillo E, Orru V, Stanford SM, Liu Y, Salek M, et al. (2010) Autoimmune-associated PTPN22 R620W variation reduces phosphorylation of lymphoid phosphatase on an inhibitory tyrosine residue. J Biol Chem 285: 26506-26518.
14. Yu X, Chen M, Zhang S, Yu ZH, Sun JP, et al. (2011) Substrate specificity of lymphoid-specific tyrosine phosphatase (Lyp) and identification of Src kinase-associated protein of 55 kDa homolog (SKAP-HOM) as a Lyp substrate. J Biol Chem 286: 30526-30534.
15. Menard L, Saadoun D, Isnardi I, Ng YS, Meyers G, et al. (2011) The PTPN22 allele encoding an R620W variant interferes with the removal of developing autoreactive B cells in humans. J Clin Invest 121: 3635-3644.
16. Zhang J, Zahir N, Jiang Q, Miliotis H, Heyraud S, et al. (2011) The autoimmune disease-associated PTPN22 variant promotes calpain-mediated Lyp/Pep degradation associated with lymphocyte and dendritic cell hyperresponsiveness. Nat Genet 43: 902-907.
17. Cohen S, Dadi H, Shaoul E, Sharfe N, Roifman CM, (1999) Cloning and characterization of a lymphoid-specific, inducible human protein tyrosine phosphatase, Lyp. Blood 93: 2013-2024.
18. Wu J, Katrekar A, Honigberg LA, Smith AM, Conn MT, et al. (2006) Identification of substrates of human protein-tyrosine phosphatase PTPN22. J Biol Chem 281: 11002-11010.
19. Gjorloff-Wingren A, Saxena M, Williams S, Hammi D, Mustelin T, (1999) Characterization of TCR-induced receptor-proximal signaling events negatively regulated by the protein tyrosine phosphatase PEP. Eur J Immunol 29: 3845-3854.
20. Cloutier JF, Veillette A, (1999) Cooperative inhibition of T-cell antigen receptor signaling by a complex between a kinase and a phosphatase. J Exp Med 189: 111-121.
21. Ghose R, Shekhtman A, Goger MJ, Ji H, Cowburn D, (2001) A novel, specific interaction involving the Csk SH3 domain and its natural ligand. Nat Struct Biol 8: 998-1004.
22. Davidson D, Cloutier JF, Gregorieff A, Veillette A, (1997) Inhibitory tyrosine protein kinase p50csk is associated with protein-tyrosine phosphatase PTP-PEST in hemopoietic and non-hemopoietic cells. J Biol Chem 272: 23455-23462.
23. Cloutier JF, Veillette A, (1996) Association of inhibitory tyrosine protein kinase p50csk with protein tyrosine phosphatase PEP in T cells and other hemopoietic cells. Embo J 15: 4909-4918.
24. Arechiga AF, Habib T, He Y, Zhang X, Zhang ZY, et al. (2009) Cutting edge: the PTPN22 allelic variant associated with autoimmunity impairs B cell signaling. J Immunol 182: 3343-3347.
25. Orru V, Tsai SJ, Rueda B, Fiorillo E, Stanford SM, et al. (2009) A loss-of-function variant of PTPN22 is associated with reduced risk of systemic lupus erythematosus. Hum Mol Genet 18: 569-579.
26. Nejentsev S, Walker N, Riches D, Egholm M, Todd JA, (2009) Rare variants of IFIH1, a gene implicated in antiviral responses, protect against type 1 diabetes. Science 324: 387-389.
27. Rodriguez-Rodriguez L, Taib WR, Topless R, Steer S, Gonzalez-Escribano MF, et al. (2011) The PTPN22 R263Q polymorphism is a risk factor for rheumatoid arthritis in Caucasian case-control samples. Arthritis Rheum 63: 365-372.
28. Diaz-Gallo LM, Espino-Paisan L, Fransen K, Gomez-Garcia M, van Sommeren S, et al. (2011) Differential association of two PTPN22 coding variants with Crohn's disease and ulcerative colitis. Inflamm Bowel Dis 17: 2287-2294.
29. Lamsyah H, Rueda B, Baassi L, Elaouad R, Bottini N, et al. (2009) Association of PTPN22 gene functional variants with development of pulmonary tuberculosis in Moroccan population. Tissue Antigens 74: 228-232.
30. Kosco KA, Cerignoli F, Williams S, Abraham RT, Mustelin T, (2008) SKAP55 modulates T cell antigen receptor-induced activation of the Ras-Erk-AP1 pathway by binding RasGRP1. Mol Immunol 45: 510-522.
31. Pedersen AK, Guo XL, Moller KB, Peters GH, Andersen HS, et al. (2004) Residue 182 influences the second step of protein-tyrosine phosphatase-mediated catalysis. Biochem J 378: 421-433.
32. Zhang ZY, Wang Y, Dixon JE, (1994) Dissecting the catalytic mechanism of protein-tyrosine phosphatases. Proc Natl Acad Sci U S A 91: 1624-1627.
33. Keng YF, Wu L, Zhang ZY, (1999) Probing the function of the conserved tryptophan in the flexible loop of the Yersinia protein-tyrosine phosphatase. Eur J Biochem 259: 809-814.
34. Wang WQ, Bembenek J, Gee KR, Yu H, Charbonneau H, et al. (2004) Kinetic and mechanistic studies of a cell cycle protein phosphatase Cdc14. J Biol Chem 279: 30459-30468.
35. Salmeen A, Andersen JN, Myers MP, Tonks NK, Barford D, (2000) Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B. Mol Cell 6: 1401-1412.
36. Zhang YL, Hollfelder F, Gordon SJ, Chen L, Keng YF, et al. (1999) Impaired transition state complementarity in the hydrolysis of O-arylphosphorothioates by protein-tyrosine phosphatases. Biochemistry 38: 12111-12123.
37. Pannifer AD, Flint AJ, Tonks NK, Barford D, (1998) Visualization of the cysteinyl-phosphate intermediate of a protein-tyrosine phosphatase by x-ray crystallography. J Biol Chem 273: 10454-10462.
38. Xie L, Zhang YL, Zhang ZY, (2002) Design and characterization of an improved protein tyrosine phosphatase substrate-trapping mutant. Biochemistry 41: 4032-4039.
39. Seeliger MA, Young M, Henderson MN, Pellicena P, King DS, et al. (2005) High yield bacterial expression of active c-Abl and c-Src tyrosine kinases. Protein Sci 14: 3135-3139.
40. Sun JP, Fedorov AA, Lee SY, Guo XL, Shen K, et al. (2003) Crystal structure of PTP1B complexed with a potent and selective bidentate inhibitor. J Biol Chem 278: 12406-12414.
41. Zhang ZY, (2003) Mechanistic studies on protein tyrosine phosphatases. Prog Nucleic Acid Res Mol Biol 73: 171-220.