Global Proteomic Assessment of the Classical Protein-Tyrosine Phosphatome and “Redoxome”

作者: Robert Karisch , Minerva Fernandez , Paul Taylor , Carl Virtanen , Jonathan R. St-Germain

DOI: 10.1016/J.CELL.2011.07.020

关键词: ProteomicsKinaseCancer cellBiologyBiochemistryProtein tyrosine phosphatasePhosphataseTyrosineCell signalingPhosphorylation

摘要: Protein-tyrosine phosphatases (PTPs), along with protein-tyrosine kinases, play key roles in cellular signaling. All Class I PTPs contain an essential active site cysteinyl residue, which executes a nucleophilic attack on substrate phosphotyrosyl residues. The high reactivity of the catalytic cysteine also predisposes to oxidation by reactive oxygen species, such as H2O2. Reversible PTP is emerging important regulatory mechanism and might contribute diseases cancer. We exploited these unique features enzymology develop proteomic methods, broadly applicable cell tissue samples, that enable comprehensive identification quantification expressed classical (PTPome) oxidized subset PTPome (oxPTPome). find mouse human cells tissues, including cancer cells, display distinctive PTPomes oxPTPomes, revealing additional levels complexity regulation phosphorylation normal malignant cells.

参考文章(75)
Kimberly J. Nelson, Chananat Klomsiri, Simona G. Codreanu, Laura Soito, Daniel C. Liebler, LeAnn C. Rogers, Larry W. Daniel, Leslie B. Poole, Use of dimedone-based chemical probes for sulfenic acid detection methods to visualize and identify labeled proteins. Methods in Enzymology. ,vol. 473, pp. 95- 115 ,(2010) , 10.1016/S0076-6879(10)73004-4
Michael P. Myers, Jannik N. Andersen, Alan Cheng, Michel L. Tremblay, Curt M. Horvath, Jean-Patrick Parisien, Annette Salmeen, David Barford, Nicholas K. Tonks, TYK2 and JAK2 Are Substrates of Protein-tyrosine Phosphatase 1B Journal of Biological Chemistry. ,vol. 276, pp. 47771- 47774 ,(2001) , 10.1074/JBC.C100583200
Yi-Wei Lou, Yi-Yun Chen, Shu-Fan Hsu, Ren-Kun Chen, Chih-Lei Lee, Kay-Hooi Khoo, Nicholas K. Tonks, Tzu-Ching Meng, Redox regulation of the protein tyrosine phosphatase PTP1B in cancer cells. FEBS Journal. ,vol. 275, pp. 69- 88 ,(2008) , 10.1111/J.1742-4658.2007.06173.X
K Mizuno, K Hasegawa, T Katagiri, M Ogimoto, T Ichikawa, H Yakura, MPTP delta, a putative murine homolog of HPTP delta, is expressed in specialized regions of the brain and in the B-cell lineage. Molecular and Cellular Biology. ,vol. 13, pp. 5513- 5523 ,(1993) , 10.1128/MCB.13.9.5513
Dinesh Kumar Singh, Dhiraj Kumar, Zaved Siddiqui, Sandip Kumar Basu, Vikas Kumar, Kanury VS Rao, None, The Strength of Receptor Signaling Is Centrally Controlled through a Cooperative Loop between Ca2+ and an Oxidant Signal Cell. ,vol. 121, pp. 281- 293 ,(2005) , 10.1016/J.CELL.2005.02.036
Nicholas K. Tonks, Protein tyrosine phosphatases: from genes, to function, to disease Nature Reviews Molecular Cell Biology. ,vol. 7, pp. 833- 846 ,(2006) , 10.1038/NRM2039
Arnoud Groen, Simone Lemeer, Thea van der Wijk, John Overvoorde, Albert J. R. Heck, Arne Ostman, David Barford, Monique Slijper, Jeroen den Hertog, Differential oxidation of protein-tyrosine phosphatases. Journal of Biological Chemistry. ,vol. 280, pp. 10298- 10304 ,(2005) , 10.1074/JBC.M412424200
Natalie G. Ahn, John B. Shabb, William M. Old, Katheryn A. Resing, Achieving in-depth proteomics profiling by mass spectrometry. ACS Chemical Biology. ,vol. 2, pp. 39- 52 ,(2007) , 10.1021/CB600357D
Matthias Gstaiger, Ruedi Aebersold, Applying mass spectrometry-based proteomics to genetics, genomics and network biology Nature Reviews Genetics. ,vol. 10, pp. 617- 627 ,(2009) , 10.1038/NRG2633
David N. Perkins, Darryl J. C. Pappin, David M. Creasy, John S. Cottrell, Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis. ,vol. 20, pp. 3551- 3567 ,(1999) , 10.1002/(SICI)1522-2683(19991201)20:18<3551::AID-ELPS3551>3.0.CO;2-2