Substrate specificity of protein tyrosine phosphatases 1B, RPTPα, SHP-1, and SHP-2

Biochemistry

Volumn 50, Issue 12, 2011, Pages 2339-2356

  Ren, Lige ^a,b   Chen, Xianwen ^a   Luechapanichkul, Rinrada ^a   Selner, Nicholas G ^a   Meyer, Tiffany M ^a   Wavreille, Anne Sophie ^a   Chan, Richard ^c   Iorio, Caterina ^c   Zhou, Xiang ^b   Neel, Benjamin G ^c   Pei, Dehua ^a  

^a OHIO STATE UNIVERSITY   (United States)

^b WUHAN UNIVERSITY   (China)

^c UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC RESIDUES; CATALYTIC DOMAINS; CATALYTIC EFFICIENCIES; COMBINATORIAL PEPTIDE LIBRARIES; DEPHOSPHORYLATIONS; HYDROPHOBIC AMINO ACIDS; IN-VITRO; IN-VIVO; LIBRARY SCREENING; N-TERMINALS; ORDERS OF MAGNITUDE; PHASE KINETICS; PHOSPHORYLATED PEPTIDES; PROTEIN SUBSTRATE; PROTEIN-TYROSINE PHOSPHATASE; SEQUENCE SPECIFICITY; SPECIFICITY PROFILE; SUBSTRATE SPECIFICITY; TERMINAL SIDES;

AMINO ACIDS; HYDROLASES; PEPTIDES; PHOSPHATASES; PHOSPHORYLATION;

SUBSTRATES;

AROMATIC AMINO ACID; PEPTIDE LIBRARY; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE 1B; PROTEIN TYROSINE PHOSPHATASE SHP 1; PROTEIN TYROSINE PHOSPHATASE SHP 2; RPTP ALPHA PROTEIN; UNCLASSIFIED DRUG;

ACIDITY; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; DEPHOSPHORYLATION; ENZYME SPECIFICITY; HYDROPHOBICITY; IN VITRO STUDY; IN VIVO STUDY; KINETICS; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; SEQUENCE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; COMPUTATIONAL BIOLOGY; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; KINETICS; MOLECULAR SEQUENCE DATA; PEPTIDE LIBRARY; PEPTIDES; PHOSPHORYLATION; PHOSPHOTYROSINE; PROTEIN TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 1; PROTEIN TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 11; PROTEIN TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 6; PROTEIN TYROSINE PHOSPHATASES; RECEPTOR-LIKE PROTEIN TYROSINE PHOSPHATASES, CLASS 4; SUBSTRATE SPECIFICITY;

EID: 79952957889     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1014453     Document Type: Article

References (107)

1. Alonso, A., Sasin, J., Bottini, N., Friedberg, I., Osterman, A., Godzik, A., Hunter, T., Dixon, J., and Mustelin, T. (2004) Protein tyrosine phosphatases in the human genome Cell 117, 699-711 (Pubitemid 38748887)
2. Tonks, N. K. and Neel, B. G. (2001) Combinatorial control of the specificity of protein tyrosine phosphatases Curr. Opin. Cell Biol. 13, 182-195 (Pubitemid 32209219)
3. Frangioni, J. V., Beahm, P. H., Shifrin, V., Jost, C. A., and Neel, B. G. (1992) The nontransmembrane tyrosine phosphatase PTP1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence Cell 68, 545-560
4. Elchelby, M., Payette, P., Michaliszyn, E., Cromlish, W., Collins, S., Lee Loy, A., Normandin, D., Cheng, A., Himms-Hagen, J., Chan, C.-C., Ramanchandran, C., Gresser, M. J., Tremblay, M. L., and Kennedy, B. P. (1999) Increased insulin sensitivity and obesity resistance in mice lacking the protein phosphatase-1B gene Science 283, 1544-1548
5. Julien, S. G., Dube, N., Read, M., Penney, J., Paquet, M., Han, Y.-X., Kennedy, B. P., Muller, W. J., and Tremblay, M. L. (2007) Protein tyrosine phosphatase 1B deficiency or inhibition delays Erb2-induced mammary tumorigenesis and protects from lung metastasis Nat. Genet. 39, 339-346
6. Bentires-Alj, M. and Neel, B, G. (2007) Protein-tyrosine phosphatase 1B is required for HER2/Neu-indeuced breast cancer Cancer Res. 67, 2420-2424 (Pubitemid 46548925)
7. Tiganis, T. and Bennett, A. M. (2007) Protein tyrosine phosphatase function: the substrate perspective Biochem. J. 402, 1-15
8. Neel, B. G., Gu, H., and Pao, L. I. ((2003)) SH2-domain-containing protein tyrosine phosphatases. Handbook of Cell Signaling (Bradshaw, R. A. and Dennis, E. A., Eds.) Vol. 1, pp 707 - 728, Elsevier.
9. Mohi, M. G. and Neel, B. G. (2007) The role of Shp2 (PTPN11) in cancer Curr. Opin. Genet. Dev. 17, 23-30 (Pubitemid 46131442)
10. Hof, P., Pluskey, S., Dhe-Paganon, S., Eck, M. J., and Shoelson, S. E. (1998) Crystal structure of the tyrosine phosphatase SHP-2 Cell 92, 441-450 (Pubitemid 28101108)
11. Yang, J., Liu, L., He, D., Song, X., Liang, X., Zhao, Z. J., and Zhou, G. W. (2003) Crystal structure of human protein tyrosine phosphatase SHP-1 J. Biol. Chem. 278, 6516-6520 (Pubitemid 36800913)
12. Sweeney, M. C., Wavreille, A. S., Park, J., Butchar, J. P., Tridandapani, S., and Pei, D. (2005) Decoding protein-protein interactions through combinatorial chemistry: sequence specificity of SHP-1, SHP-2, and SHIP SH2 domains Biochemistry 44, 14932-14947 (Pubitemid 41612272)
13. O'Reilly, A. M. and Neel, B. G. (1998) Structural determinants of SHP-2 function and specificity in Xenopus mesoderm induction Mol. Cell. Biol. 18, 161-177 (Pubitemid 28021028)
14. Tenev, T., Keilhack, H., Tomic, S., Stoyanov, B., Stein-Gerlach, M., Lammers, R., Krivtsov, A. V., Ullrich, A., and Böhmer, F. D. (1997) Both SH2 domains are involved in interactions of SHO-1 with the epidermal growth factor receptor but cannot confer receptor-directed activity to SHP-1/SHP-2 chimera J. Biol. Chem. 272, 5966-5973 (Pubitemid 27102434)
15. Wang, Y. and Pallen, C. J. (1991) The receptor-like protein tyrosine phosphatase HPTP alpha has two active catalytic domains with distinct substrate specificities EMBO J. 10, 3231-3237 (Pubitemid 21905347)
16. Lim, K. L., Ng, C. H., and Pallen, C. J. (1999) Catalytic activation of the membrane distal domain of protein tyrosine phosphatase epsilon, but not CD45, by two point mutations Biochim. Biophys. Acta 1434, 275-283 (Pubitemid 29486750)
17. Wu, L., Buis, A., den Hertog, J., and Zhang, Z.-Y. (1997) Comparative kinetic analysis and substrate specificity of the tandem catalytic domains of the receptor-like protein tyrosine phosphatase α J. Biol. Chem. 272, 6994-7002 (Pubitemid 27166400)
18. Jiang, G. Q., den Hertog, J., and Hunter, T. (2000) Receptor-like protein tyrosine phosphatase alpha homodimerizes on the cell surface Mol. Cell. Biol. 20, 5917-5929 (Pubitemid 30613041)
19. Vacaru, A. M. and den Hertog, J. (2010) Catalytically active membrane-distal phosphatase domain of receptor protein-tyrosine phosphatase α is required for Src activation FEBS J. 277, 1562-1570
20. Ng, D. H. W., Jabali, M. D., Maiti, A., Borodchak, P., Harder, K. W., Brocker, T., Malissen, B., Jirik, F. R., and Johnson, P. (1997) CD45 and RPTPα display different protein tyrosine phosphatase activities in T lymphocytes Biochem. J. 327, 867-876 (Pubitemid 27487696)
21. Cho, H. J., Ramer, S. E., Itoh, M., Winkler, D. G., Kitas, E., Bannwarth, W., Burn, P., Saito, H., and Walsh, C. T. (1991) Purification and characterization of a soluble catalytic fragment of the human transmembrane leukocyte antigen related (LAR) protein tyrosine phosphatase from an Escherichia coli expression system Biochemistry 30, 6210-6216
22. Zhang, Z.-Y., Maclean, D., McNamara, D. J., Sawyer, T. K., and Dixon, J. E. (1994) Protein tyrosine phosphatase substrate specificity: size and phosphotyrosine positioning requirements in peptide substrates Biochemistry 33, 2285-2290 (Pubitemid 24099629)
23. Harder, K. W., Owen, P., Wong, L. K. H., Aebersold, R., Clark-Lewis, I., and Jirik, F. R. (1993) Characterization and kinetic analysis of the intracellular domain of human protein tyrosine phosphatase β (HPTPβ) using synthetic phosphopeptides Biochem. J. 298, 395-401
24. Bobko, M., Wolfe, H. R., Saha, A., Dolle, R. E., Fisher, D. K., and Higgins, T. J. (1995) CD45 protein tyrosine phosphatase: determination of minimal peptide length for substrate recognition and synthesis of some tyrosine-based electrophiles as potential active-site directed irreversible inhibitors Bioorg. Med. Chem. Lett. 5, 353-356
25. Dechert, U., Affolter, M., Harder, K. W., Matthews, J., Owen, P., Clark-Lewis, I., Thomas, M. L., Aebersold, R., and Jirik, F. R. (1995) Comparison of the specificity of bacterially expressed cytoplasmic protein-tyrosine phosphatases SHP and SH-PTP2 towards synthetic phosphopeptide substrates Eur. J. Biochem. 231, 673-681
26. Sun, H., Tan, L. P., Gao, L., and Yao, S. Q. (2009) High-throughput screening of catalytically inactive mutants of protein tyrosine phosphatases (PTPs) in a phosphopeptide microarray Chem. Commun. 6, 677-679
27. Kohn, M., Gutierrez-Rodriguez, M., Jonkheijm, P., Wetzel, S., Wacker, R., Schroeder, H., Prinz, H., Niemeyer, C. M., Breinbauer, R., Szedlacsek, S. E., and Waldmann, H. (2007) A microarray strategy for mapping the substrate specificity of protein tyrosine phosphatase Angew. Chem., Int. Ed. 46, 7700-7703 (Pubitemid 47557030)
28. Jia, Z., Barford, D., Flint, A. J., and Tonks, N. K. (1995) Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B Science 268, 1754-1758
29. Yang, J., Cheng, Z., Niu, T., Liang, X., Zhao, Z. J., and Zhou, G. W. (2000) Structural basis for substrate specificity of protien-tyrosine phosphatase SHP-1 J. Biol. Chem. 275, 4066-4071 (Pubitemid 30094637)
30. Salmeen, A., Andersen, J. N., Myers, M. P., Tonks, N. K., and 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 (Pubitemid 32045932)
31. Sarmiento, M., Puius, Y. A., Vetter, S. W., Keng, Y.-F., Wu, L., Zhao, Y., Lawrence, D. S., Almo, S. C., and Zhang, Z.-Y. (2000) Structural basis of plasticity in protein tyrosine phosphatase 1B substrate recognition Biochemistry 39, 8171-8179 (Pubitemid 30460966)
32. Pellegrini, M. C., Liang, H., Mandiyan, S., Wang, K., Yuyev, A., Vlattas, I., Sytwu, T., Li, Y.-C., and Wennogle, L. P. (1998) Mapping the subsite preferences of protein tyrosine phosphatase PTP1B using combinatorial chemistry approaches Biochemistry 37, 15598-15606 (Pubitemid 28524730)
33. Huyer, G., Kelly, J., Moffat, J., Zamboni, R., Jia, Z., Gresser, M. J., and Ramachandran, C. (1998) Affinity selection from peptide libraries to determine substrate specificity of protein tyrosine phosphatases Anal. Biochem. 258, 19-30 (Pubitemid 28163138)
34. Espanel, X. and van Huijsduijnen, R. H. (2005) Applying the SPOT peptide synthesis procedure to the study of protein tyrosine phosphatase substrate specificity: probing for the heavenly match in vitro Methods 35, 64-72 (Pubitemid 39647580)
35. Walchli, S., Espanel, X., Harrenga, A., Rossi, M., Cesareni, G., and van Huijsduijnen, H. R. (2004) Probing protein tyrosine phosphatase substrate specificity using a phosphotyrosine-containing phage library J. Biol. Chem. 279, 311-318 (Pubitemid 38044829)
36. Vetter, S. W., Keng, Y. F., Lawrence, D. S., and Zhang, Z.-Y. (2000) Assessment of protein tyrosine phosphatase 1B substrate specificity using "inverse alanine scanning" J. Biol. Chem. 275, 2265-2268 (Pubitemid 30081980)
37. Wang, P., Fu, H., Snavley, D. F., Freitas, M. A., and Pei, D. (2002) Screening combinatorial libraries by mass spectrometry. 2. Identification of optimal substrates of protein tyrosine phosphatase SHP-1 Biochemistry 41, 6202-6210 (Pubitemid 34498928)
38. Cheung, Y. W., Abell, C., and Balasubramanian, S. (1997) A combinatorial approach to identifying protein tyrosine phosphatase substrates from a phosphotyrosine peptide library J. Am. Chem. Soc. 119, 9568-9569 (Pubitemid 27460547)
39. Mitra, S. and Barrios, A. M. (2008) Identifying selective protein tyrosine phosphatase substrates and inhibitors from a fluorogenic, combinatorial peptide library ChemBioChem 9, 1216-1219
40. Mishra, A. K., Zhang, A., Niu, T., Yang, J., Liang, X., Zhao, Z. J., and Zhou, G. W. (2002) Substrate specificity of protein tyrosine phosphatase: Differential behavior of SHP-1 and SHP-2 towards signal regulation protein SIRPα1 J. Cell. Biochem. 84, 840-846 (Pubitemid 34113122)
41. Garaud, M. and Pei, D. (2007) Substrate profiling of protein tyrosine phosphatase PTP1B by screening a combinatorial peptide library J. Am. Chem. Soc. 129, 5366-5367 (Pubitemid 46697617)
42. Gopishetty, B., Ren, L., Waller, T. M., Wavreille, A. S., Lopez, M., Thakkar, A., Zhu, J., and Pei, D. (2008) Synthesis of 3,5-difluorotyrosine- containing peptides: application in substrate profiling of protein tyrosine phosphatases Org. Lett. 10, 4605-4608
43. Chen, X., Ren, L., Kim, S., Carpino, N., Daniel, J. L., Kunapuli, S. P., Tsygankov, A. Y., and Pei, D. (2010) Determination of the substrate specificity of protein tyrosine phosphatase TULA-2 and identification of Syk as a TULA-2 substrate J. Biol. Chem. 285, 31268-31276
44. Li, S. and Zeng, D. (2007) Chemoenzymatic enrichment of phosphotyrosine-containing peptides Angew. Chem., Int. Ed. 46, 4751-4753 (Pubitemid 46997479)
45. Pei, D., Neel, B. G., and Walsh, C. T. (1993) Overexpression, purification, and characterization of SHPTP1, a Src homology 2-containing protein-tyrosine-phosphatase Proc. Natl. Acad. Sci. U.S.A. 90, 1092-1096 (Pubitemid 23053957)
46. Park, J. and Pei, D. (2004) trans -β-Nitrostyrene derivatives as slow-binding inhibitors of protein tyrosine phosphatases Biochemistry 43, 15014-15021 (Pubitemid 39587478)
47. Barr, A. J., Ugochukwu, E., Lee, W. H., King, O. N., Filippakopoulos, P., Alfano, I., Savitsky, P., Burgess-Brown, N. A., Müller, S., and Knapp., S. (2009) Large-scale structural analysis of the classical human protein tyrosine phosphatome Cell 136, 352-363
48. Thakkar, A., Wavreille, A. S., and Pei, D. (2006) Traceless capping agent for peptide sequencing by partial Edman degradation and mass spectrometry Anal. Chem. 78, 5935-5938
49. Zhang, Z.-Y., Maclean, D., Thieme-Sefler, A. M., Roeske, R. W., and Dixon, J. E. (1993) A continuous spectrophotometric and fluorimetric assay for protein tyrosine phosphatase using phosphotyrosine-containing peptides Anal. Biochem. 211, 7-15 (Pubitemid 23189321)
50. Kress, J., Zanaletti, R., Amour, A., Ladlow, M., Frey, J. G., and Bradley, M. (2002) Enzyme accessibility and solid supports: which molecular weight enzymes can be used on solid support? An investigation using confocal Raman microscopy Chem.-Eur. J. 8, 3769-3772 (Pubitemid 34951462)
51. Ulijn, R. V., Baragaña, B., Halling, P. J., and Flitsch, S. L. (2002) Protease-catalyzed peptide synthesis on solid support J. Am. Chem. Soc. 124, 10988-10989 (Pubitemid 35025652)
52. Ulijn, R. V., Bisek, N., Halling, P., and Flitsch., S. L. (2003) Understanding protease catalyzed solid phase peptide synthesis Org. Biomol. Chem. 1, 1277-1281
53. Jolley, R. L., Jr., Nelson, R. M., and Robb, D. A. (1969) The multiple forms of tyrosinase J. Biol. Chem. 244, 3251-3257
54. Xiao, Q., Zhang, F., Nacev, B. A., Liu, J. O., and Pei, D. (2010) Protein N-terminal processing: substrate specificity of Escherichia coli and human methionine aminopeptidases Biochemistry 49, 5588-5599
55. Chen, X., Tan, P. H., Zhang, Y., and Pei, D. (2009) On-bead screening of combinatorial libraries: reduction of nonspecific binding by decreasing surface ligand density J. Comb. Chem. 11, 604-611
56. Puius, Y. A., Zhao, Y., Sullivan, M., Lawrence, D. S., Almo, S. C., and Zhang, Z.-Y. (1997) Identification of second aryl phosphate-binding site in protein-tyrosine phosphates 1B: a paradigm for inhibitor design Proc. Natl. Acad. Sci. U.S.A. 94, 13420-13425
57. Lee, H., Xie, L. P, Luo, Y., Lee, S. Y., Lawrence, D. S., Wang, X. B., Sotgia, F., Lisanti, M. P., and Zhang, Z.-Y. (2006) Identification of phosphocaveolin-1 as a novel protein tyrosine phosphatase 1B substrate Biochemistry 45, 234-240 (Pubitemid 43054101)
58. Stuible, M., Dube, N., and Tremblay, M. L. (2008) PTP1B regulates cortactin tyrosine phosphorylation by targeting Tyr446 J. Biol. Chem. 283, 15740-15746
59. Mertins, P., Eberl, H. C., Renkawitz, J., Olsen, J. V., Tremblay, M. L., Mann, M., Ullrich, A., and Daub, H. (2008) Investigation of protein-tyrosine phosphatase 1B function by quantitative proteomics Mol. Cell. Proteomics 7.9, 1763-1777
60. Heinonen, K. M., Dube, N., Bourdeau, A., Lapp, W. S., and Tremblay, M. L. (2006) Protein tyrosine phosphatase 1B negatively regulates macrophage development in intact cells Proc. Natl. Acad. Sci. U.S.A. 103, 2776-2781
61. Myers, M. P., Andersen, J. N., Cheng, A., Tremblay, M. L., Horvath, C. M., Parisien, J. P., Salmeen, A., Barford, D., and Tonks, N. K. (2001) TYK2 and JAK2 are substrates of protein-tyrosine phosphatase 1B J. Biol. Chem. 276, 47771-47774
62. Liang, F., Lee, S. Y., Liang, J., Lawrence, D. S., and Zhang, Z.-Y. (2005) The role of protein-tyrosine phosphatase 1B in integrin signaling J. Biol. Chem. 280, 24857-24863 (Pubitemid 40934576)
63. Bjorge, J. D., Pang, A., and Fujita, D. J. (2000) Identification of protein-tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human cancer cell lines J. Biol. Chem. 275, 41439-41446 (Pubitemid 32054980)
64. Stuible, M., Abella, J. V., Feldhammer, M., Nossov, M., Sangwan, V., Blagoev, B., Park, M., and Tremblay, M. L. (2010) PTP1B targets the endosomal sorting machinery J. Biol. Chem. 285, 23899-23907
65. Aoki, N. and Matsuda, T. (2000) A cytosolic protein-tyrosine phosphatase PTP1B specifically dephosphorylates and deactivates prolactin-activated STAT5a and STAT5b J. Biol. Chem. 275, 39718-39726 (Pubitemid 32059000)
66. Agazie, Y. M. and Hayman, M. J. (2003) Molecular mechanism for a role of SHP2 in epidermal growth factor receptor signaling Mol. Cell. Biol. 23, 7875-7886 (Pubitemid 37271483)
67. Tsutsumi, R., Takahashi, A., Azuma, T., Higashi, H., and Hatakeyama, M. (2006) Focal adhesion kinase is a substrate and downstream effector of SHP-2 complexed with Helicobacter pylori CagA Mol. Cell. Biol. 26, 261-276
68. Zhou, X. D. and Agazie, Y. M. (2009) Molecular mechanism for SHP2 in promoting HER2-induced signaling and transformation J. Biol. Chem. 284, 12226-12234
69. Klinghoffer, R. A. and Kazlauskas, A. (1995) Identification of a putative Syp substrate, the PDGFβ receptor J. Biol. Chem. 270, 22208-22217
70. Bregeon, J., Loirand, G., Pacaud, P., and Rolli-Derkinderen, M. (2009) Angiotensin II induces RhoA activation through SHP2-dependent dephosphorylation of the RhoGAP p190A in vascular smooth muscle cells Am. J. Physiol. Cell Physiol. 297, C1062-C1070
71. Lesley, A. J., Stephanie, J. T., Michael, A. S., Mark, A. K., and Rachel, K. S. (2006) Sprouty proteins are in vivo targets of Corkscrew/SHP-2 tyrosine phosphatases Development 133, 1133-1142
72. Bard-Chapeau, E. A., Yuan, J., Droin, N., Long, S., Zhang, E. E., Nguyen, T. V., and Feng, G. S. (2006) Concerted functions of Gab1 and Shp2 in liver regeneration and hepatoprotection Mol. Cell. Biol. 26, 4664-4674 (Pubitemid 43877583)
73. Zhang, S. Q., Yang, W., Kontaridis, M. I., Bivona, T. G., Wen, G., Araki, T., Luo, J., Thompson, J. A., Schraven, B. L., Philips, M. R., and Neel, B. G. (2004) Shp2 regulates Src family kinase activity and Ras/Erk activation by controlling Csk recruitment Mol. Cell 13, 341-355 (Pubitemid 38229807)
74. Ren, Y, Meng, S., Mei, L., Zhao, Z. J., Jove, R., and Wu, J. (2004) Roles of Gab1 and SHP2 in Paxillin tyrosine dephosphorylation and Src activation in response to epidermal growth factor J. Biol. Chem. 279, 8497-8505 (Pubitemid 38294743)
75. Zhao, Z. J. and Zhao, R. (1998) Purification and cloning of PZR, a binding protein and putative physiological substrate of tyrosine phosphatase SHP-2 J. Biol. Chem. 273, 29367-29372 (Pubitemid 28509936)
76. Kontaridis, M. I., Eminaga, S., Fornaro, M., Zito, C. I., Sordella, R., Settleman, J., and Bennett, A. M. (2004) SHP-2 positively regulates myogenesis by coupling to the rho GTPase signaling pathway Mol. Cell. Biol. 24, 5340-5352 (Pubitemid 38738169)
77. Kharitonenkov, A., Chen, Z., Sures, I., Wang, H., Schilling, J., and Ullrich, A. (1997) A family of proteins that inhibit signaling through tyrosine kinase receptors Nature 386, 181-186 (Pubitemid 27131446)
78. Noguchi, T., Matozaki, T., Fujioka, Y., Yamao, T., Tsuda, M., Takada, T., and Kasuga, M. (1996) Characterization of a 115-kDa protein that binds to SH-PTP2, a protein-tyrosine phosphatase with Src homology 2 domains, in Chinese hamster ovary cells J. Biol. Chem. 271, 27652-27658 (Pubitemid 26367333)
79. Yu, L., Min, W., He, Y., Qin, L., Zhang, H., Bennett, A. M., and Chen, H. (2009) JAK2 and SHP2 reciprocally regulate tyrosine phosphorylation and stability of proapoptotic protein ASK1 J. Biol. Chem. 284, 13481-13488
80. Koli, S., Zito, C. I., Mossink, M. H., Wiemer, E. A. C., and Bennett, A. M. (2004) The major vault protein is a novel substrate for the tyrosine phosphatase SHP-2 and scaffold protein in epidermal growth factor signaling J. Biol. Chem. 279, 29374-29385 (Pubitemid 38915816)
81. Wu, T. R., Hong, Y. K., Wang, X. D., Ling, M. Y., Dragoi, A. M., Chung, A. S., Campbell, A. G., Han, Z. Y., Feng, G. S., and Chin, Y. E. (2002) SHP-2 is a dual-specificity phosphatase involved in Stat1 dephosphorylation at both tyrosine and serine residues in nuclei J. Biol. Chem. 277, 47572-47580 (Pubitemid 36159277)
82. Chen, Y., Wen, R., Yang, S., Schuman, J., Zhang, E. E., Yi, T., Feng, G. S., and Wang, D. (2003) Identification of shp-2 as a stat5A phosphatase J. Biol. Chem. 278, 16520-16527 (Pubitemid 36799512)
83. Chiang, G. G. and Sefton, B. M. (2001) Specific dephosphorylation of tyrosine protein kinase at Tyr-394 by the SHP-1 protein-tyrosine phosphatase J. Biol. Chem. 276, 23173-23178
84. Ozawa, T., Nakata, K., Mizuno, K., and Yakura, H. (2007) Negative autoregulation of Src homology region 2-containing phosphatase 1 in rat basophilic leukemia-2H3 cells Int. Immunol. 19, 1049-1061 (Pubitemid 47434238)
85. 2-terminal kinase activation in B cells J. Immunol. 165, 1344-1351 (Pubitemid 30604564)
86. Keilhack, H., Hellman, U., van Hengel, J., van Roy, F., Godovac-Zimmermann, J., and Böhmer, F. D. (2000) The protein-tyrosine phosphatase SHP-1 binds to and dephosphorylates p120 catenin J. Biol. Chem. 275, 26376-26384
87. Law, C. L., Sidorenko, S. P., Chandran, K. A., Zhao, Z., Shen, S. H., Fischer, E. H., and Clark, E. A. (1996) CD22 associates with protein tyrosine phosphatase 1C, Syk, and phospholipase C-γ1 upon B cell activation J. Exp. Med. 183, 547-560 (Pubitemid 26059518)
88. Wu, Y., Nadler, M. J., Brennan, L. A., Gish, G. D., Timms, J. F., Fusaki, N., Jongstra-Bilen, J., Tada, N., Pawson, T., Wither, J., Neel, B. G., and Hozumi, N. (1998) The B-cell transmembrane protein CD72 binds to and is an in vivo substrate of the protein tyrosine phosphatase SHP-1 Curr. Biol. 8, 1009-1017 (Pubitemid 28448073)
89. DOK tyrosine phosphorylation in macrophages J. Biol. Chem. 274, 35855-35865 (Pubitemid 129512891)
90. Timms, J. F., Carlberg, K., Gu, H., Chen, H., Kamatkar, S., Nadler, M. J., Rohrschneider, L. R., and Neel, B. G. (1998) Identification of major binding protein and substrates for the SH2-containing protein tyrosine phosphatase SHP-1 in macrophages Mol. Cell. Biol. 18, 3838-3850 (Pubitemid 28287907)
91. Binstadt, B. A., Billadeau, D. D., Jevremović, D., Williams, B. L., Fang, N., Yi, T., Koretzky, G. A, Abraham, R. T., and Leibson, P. J. (1998) SLP-76 is a direct substrate of SHP-1 recruited to killer cell inhibitory receptors J. Biol. Chem. 273, 27518-27523 (Pubitemid 28500472)
92. Dustin, L. B., Plas, D. R., Wong, J., Hu, Y. T., Soto, C., Chan, A. C., and Thomas, M. L. (1999) Expression of dominant negative src-homology domain 2-containing protein tyrosine phosphatase-1 results in increased Syk tyrosine kinase activity and B cell activation J. Immunol. 162, 2717-2724 (Pubitemid 29309294)
93. Stebbins, C. C., Watzl, C., Billadeau, D. D., Leibson, P. J., Burshtyn, D. N., and Long, E. O. (2003) Vav1 dephosphorylation by the tyrosine phosphatase SHP-1 as a mechanism for inhibition of cellular cytotoxicity Mol. Cell. Biol. 23, 6291-6299 (Pubitemid 37013105)
94. Baba, T., Fusaki, N., Shinya, N., Iwamatsu, A., and Hozumi, N. (2003) Actin tyrosine dephosphorylation by the Src homology 1-containing protein tyrosine phosphatase is essential for actin depolymerization after membrane IgM cross-linking J. Immunol. 170, 3762-3768 (Pubitemid 36359246)
95. Zheng, X. M., Wang, Y., and Pallen, C. J. (1992) Cell transformation and activation of pp60c-src by overexpression of protein tyrosine phosphatase Nature 359, 336-339
96. Samayawardhena, L. A. and Pallen, C. J. (2010) PTPα activates Lyn and Fyn and suppresses Hck to negatively regulate FcεRI-dependent mast cell activation and allergic responses J. Immunol. 185, 5993-6002
97. Le, H. T., Maksumova, L., Wang, J., and Pallen, C. J. (2006) Reduced NMDA receptor tyrosine phosphorylation in PTPα-deficient mouse synaptosomes is accompanied by inhibition of four src family kinases and Pyk2: an upstream role for PTPα in NMDA receptor regulation J. Neurochem. 98, 1798-1809 (Pubitemid 44298246)
98. Imbrici, P., Tucker, S. J., D'Adamo, M. C., and Pessia, M. (2000) Role of receptor tyrosine phosphatase α (RPTPα) and tyrosine phosphorylation in the serotonergic inhibition of voltage-dependent potassium channels Eur. J. Physiol. 441, 257-262 (Pubitemid 32128165)
99. cas as an in vivo substrate of receptor protein-tyrosine phosphatase α J. Biol. Chem. 275, 20754-20761 (Pubitemid 30457665)
100. Woodford-Thomas, T. A., Rhodes, J. D., and Dixon, J. E. (1992) Expression of a protein tyrosine phosphatase in normal and v-src-transformed mouse 3T3 fibroblasts J. Cell Biol. 117, 401-414
101. Frangioni, J. V., Oda, A., Smith, M., Salzman, E. W., and Neel, B. G. (1993) Calpain-catalyzed cleavage and subcellular relocation of protein phosphotyrosine phosphatase 1B (PTP-1B) in human platelets EMBO J. 12, 4843-4856 (Pubitemid 23330291)
102. Kucahy, S. M., Kim, N., Grunz, E. A., Fay, W. P., and Chishti, A. H. (2007) Double knockouts reveal that protein tyrosine phosphatase 1B is a physiological target of calpain-1 in platelets Mol. Cell. Biol. 27, 6038-6052 (Pubitemid 47326693)
103. Li, S., Depetris, R. S., Barford, D., Chernoff, J., and Hubbard, S. R. (2005) Crystal structure of a complex between protein tyrosine phosphatase 1B and the insulin receptor tyrosine kinase Structure 13, 1643-1651 (Pubitemid 41571827)
104. Yudushkin, I. A., Schleifenbaum, A., Kinkhabwala, A., Neel, B. G., Schultz, C., and Bastiaens, P. I. H. (2007) Live-cell imaging of enzyme-substrate interaction reveals spatial regulation of PTP1B Science 315, 115-119 (Pubitemid 46196993)
105. Salmeen, A. and Barford, D. (2005) Functions and mechanisms of redox regulation of cysteine-based phosphatases Antioxid. Redox Signaling 7, 560-577 (Pubitemid 40563195)
106. Flint, A. J., Tiganis, T., Barford, D., and Neel, B. G. (1997) Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases Proc. Natl. Acad. Sci. U.S.A. 94, 1680-1685
107. cas as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST Mol. Cell. Biol. 16, 6408-6418 (Pubitemid 26360999)