QUICK identification and SPR validation of signal transducers and activators of transcription 3 (Stat3) interacting proteins

Journal of Proteomics

Volumn 75, Issue 3, 2012, Pages 1055-1066

  Zheng, Peng ^a   Zhong, Qiu ^b   Xiong, Qian ^a   Yang, Mingkun ^a   Zhang, Jia ^a,c   Li, Chongyang ^a   Bi, Li Jun ^c   Ge, Feng ^a  

^a INSTITUTE OF HYDROBIOLOGY   (China)

^b Antituberculosis Research Institute of Guangdong Province   (China)

^c INSTITUTE OF BIOPHYSICS   (China)

Author keywords

14 3 3 ; Multiple myeloma; Quantitative immunoprecipitation combined with knockdown (QUICK); Stable isotope labeling with amino acids in cell culture (SILAC); Stat3; Surface plasmon resonance (SPR)

Indexed keywords

AMINO ACID; HEAT SHOCK PROTEIN 90; PROTEIN 14 3 3; PROTEIN KINASE C BETA; RNA; STABLE ISOTOPE; STAT3 PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CELL CULTURE; CELL FUNCTION; CONTROLLED STUDY; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; ISOTOPE LABELING; MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN INTERACTION; PROTEOMICS; QUANTITATIVE ANALYSIS; QUANTITATIVE IMMUNOPRECIPITATION COMBINED WITH KNOCKDOWN; RNA INTERFERENCE; SIGNAL TRANSDUCTION; SURFACE PLASMON RESONANCE;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; CELL LINE, TUMOR; HUMANS; MULTIPLE MYELOMA; NEOPLASM PROTEINS; PROTEOMICS; STAT3 TRANSCRIPTION FACTOR; SURFACE PLASMON RESONANCE;

EID: 84355166425     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2011.10.020     Document Type: Article

References (51)

1. Raab M.S., Podar K., Breitkreutz I., Richardson P.G., Anderson K.C. Multiple myeloma. Lancet 2009, 374:324-339.
2. Neumann C., Zehentmaier G., Danhauser-Riedl S., Emmerich B., Hallek M. Interleukin-6 induces tyrosine phosphorylation of the Ras activating protein Shc, and its complex formation with Grb2 in the human multiple myeloma cell line LP-1. Eur J Immunol 1996, 26:379-384.
3. Klein B., Zhang X.G., Lu Z.Y., Bataille R. Interleukin-6 in human multiple myeloma. Blood 1995, 85:863-872.
4. Brocke-Heidrich K., Kretzschmar A.K., Pfeifer G., Henze C., Loffler D., Koczan D., et al. Interleukin-6-dependent gene expression profiles in multiple myeloma INA-6 cells reveal a Bcl-2 family-independent survival pathway closely associated with Stat3 activation. Blood 2004, 103:242-251.
5. Wang L.H., Yang X.Y., Mihalic K., Xiao W., Li D., Farrar W.L. Activation of estrogen receptor blocks interleukin-6-inducible cell growth of human multiple myeloma involving molecular cross-talk between estrogen receptor and STAT3 mediated by co-regulator PIAS3. J Biol Chem 2001, 276:31839-31844.
6. Levy D.E., Darnell J.E. Stats: transcriptional control and biological impact. Nat Rev Mol Cell Biol 2002, 3:651-662.
7. Levy D.E., Lee C.K. What does Stat3 do?. J Clin Invest 2002, 109:1143-1148.
8. Catlett-Falcone R., Landowski T.H., Oshiro M.M., Turkson J., Levitzki A., Savino R., et al. Constitutive activation of Stat3 signaling confers resistance to apoptosis in human U266 myeloma cells. Immunity 1999, 10:105-115.
9. Mora L.B., Buettner R., Seigne J., Diaz J., Ahmad N., Garcia R., et al. Constitutive activation of Stat3 in human prostate tumors and cell lines: direct inhibition of Stat3 signaling induces apoptosis of prostate cancer cells. Cancer Res 2002, 62:6659-6666.
10. Grandis J.R., Drenning S.D., Zeng Q., Watkins S.C., Melhem M.F., Endo S., et al. Constitutive activation of Stat3 signaling abrogates apoptosis in squamous cell carcinogenesis in vivo. Proc Natl Acad Sci U S A 2000, 97:4227-4232.
11. Buettner R., Mora L.B., Jove R. Activated STAT signaling in human tumors provides novel molecular targets for therapeutic intervention. Clin Cancer Res 2002, 8:945-954.
12. Yu H., Pardoll D., Jove R. STATs in cancer inflammation and immunity: a leading role for STAT3. Nat Rev Cancer 2009, 9:798-809.
13. Yu H., Kortylewski M., Pardoll D. Crosstalk between cancer and immune cells: role of STAT3 in the tumour microenvironment. Nat Rev Immunol 2007, 7:41-51.
14. Selbach M., Mann M. Protein interaction screening by quantitative immunoprecipitation combined with knockdown (QUICK). Nat Methods 2006, 3:981-983.
15. Ong S.E., Mann M. A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC). Nat Protoc 2006, 1:2650-2660.
16. Ge F., Li W.L., Bi L.J., Tao S.C., Zhang Z.P., Zhang X.E. Identification of novel 14-3-3zeta interacting proteins by quantitative immunoprecipitation combined with knockdown (QUICK). J Proteome Res 2010, 9:5848-5858.
17. Meixner A., Boldt K., Van Troys M., Askenazi M., Gloeckner C.J., Bauer M., et al. A QUICK screen for Lrrk2 interaction partners - leucine-rich repeat kinase 2 is involved in actin cytoskeleton dynamics. Mol Cell Proteomics 2011, 10. M110.001172.
18. Chatterjee M., Stuhmer T., Herrmann P., Bommert K., Dorken B., Bargou R.C. Combined disruption of both the MEK/ERK and the IL-6R/STAT3 pathways is required to induce apoptosis of multiple myeloma cells in the presence of bone marrow stromal cells. Blood 2004, 104:3712-3721.
19. Park S.K., Venable J.D., Xu T., Yates J.R. A quantitative analysis software tool for mass spectrometry-based proteomics. Nat Methods 2008, 5:319-322.
20. Thomas P.D., Campbell M.J., Kejariwal A., Mi H., Karlak B., Daverman R., et al. PANTHER: a library of protein families and subfamilies indexed by function. Genome Res 2003, 13:2129-2141.
21. von Mering C., Jensen L.J., Snel B., Hooper S.D., Krupp M., Foglierini M., et al. STRING: known and predicted protein-protein associations, integrated and transferred across organisms. Nucleic Acids Res 2005, 33:D433-D437.
22. Ashburner M., Ball C.A., Blake J.A., Botstein D., Butler H., Cherry J.M., et al. Gene ontology: tool for the unification of biology. The Gene Ontology Consortium. Nat Genet 2000, 25:25-29.
23. Kanehisa M., Goto S. KEGG: Kyoto Encyclopedia of Genes and Genomes. Nucleic Acids Res 2000, 28:27-30.
24. Huang da W., Sherman B.T., Lempicki R.A. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat Protoc 2009, 4:44-57.
25. Huang da W., Sherman B.T., Lempicki R.A. Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists. Nucleic Acids Res 2009, 37:1-13.
26. Maere S., Heymans K., Kuiper M. BiNGO: a Cytoscape plugin to assess overrepresentation of gene ontology categories in biological networks. Bioinformatics 2005, 21:3448-3449.
27. Ge F., Zhang L., Tao S.C., Kitazato K., Zhang Z.P., Zhang X.E., et al. Quantitative proteomic analysis of tumor reversion in multiple myeloma cells. J Proteome Res 2011, 10:845-855.
28. Nelson E.A., Walker S.R., Kepich A., Gashin L.B., Hideshima T., Ikeda H., et al. Nifuroxazide inhibits survival of multiple myeloma cells by directly inhibiting STAT3. Blood 2008, 112:5095-5102.
29. Aitken A., Howell S., Jones D., Madrazo J., Patel Y. 14-3-3 alpha and delta are the phosphorylated forms of raf-activating 14-3-3 beta and zeta. In vivo stoichiometric phosphorylation in brain at a Ser-Pro-Glu-Lys MOTIF. J Biol Chem 1995, 270:5706-5709.
30. Fu H., Subramanian R.R., Masters S.C. 14-3-3 proteins: structure, function, and regulation. Annu Rev Pharmacol Toxicol 2000, 40:617-647.
31. Morrison D.K. The 14-3-3 proteins: integrators of diverse signaling cues that impact cell fate and cancer development. Trends Cell Biol 2009, 19:16-23.
32. Meller N., Liu Y.C., Collins T.L., Bonnefoy-Berard N., Baier G., Isakov N., et al. Direct interaction between protein kinase C theta (PKC theta) and 14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition of PKC theta translocation and function. Mol Cell Biol 1996, 16:5782-5791.
33. Acs P., Szallasi Z., Kazanietz M.G., Blumberg P.M. Differential activation of PKC isozymes by 14-3-3 zeta protein. Biochem Biophys Res Commun 1995, 216:103-109.
34. Roberts R.L., Mosch H.U., Fink G.R. 14-3-3 proteins are essential for RAS/MAPK cascade signaling during pseudohyphal development in S. cerevisiae. Cell 1997, 89:1055-1065.
35. Xing H., Zhang S., Weinheimer C., Kovacs A., Muslin A.J. 14-3-3 proteins block apoptosis and differentially regulate MAPK cascades. EMBO J 2000, 19:349-358.
36. Dong S., Kang S., Gu T.L., Kardar S., Fu H., Lonial S., et al. 14-3-3 integrates prosurvival signals mediated by the AKT and MAPK pathways in ZNF198-FGFR1-transformed hematopoietic cells. Blood 2007, 110:360-369.
37. Kovacina K.S., Park G.Y., Bae S.S., Guzzetta A.W., Schaefer E., Birnbaum M.J., et al. Identification of a proline-rich Akt substrate as a 14-3-3 binding partner. J Biol Chem 2003, 278:10189-10194.
38. Aslan J.E., You H., Williamson D.M., Endig J., Youker R.T., Thomas L., et al. Akt and 14-3-3 control a PACS-2 homeostatic switch that integrates membrane traffic with TRAIL-induced apoptosis. Mol Cell 2009, 34:497-509.
39. Larance M., Rowland A.F., Hoehn K.L., Humphreys D.T., Preiss T., Guilhaus M., et al. Global phosphoproteomics identifies a major role for AKT and 14-3-3 in regulating EDC3. Mol Cell Proteomics 2010, 9:682-694.
40. Neal C.L., Yu D. 14-3-3zeta as a prognostic marker and therapeutic target for cancer. Expert Opin Ther Targets 2010, 14:1343-1354.
41. Newton A.C. Protein kinase C: structure, function, and regulation. J Biol Chem 1995, 270:28495-28498.
42. Rosse C., Linch M., Kermorgant S., Cameron A.J., Boeckeler K., Parker P.J. PKC and the control of localized signal dynamics. Nat Rev Mol Cell Biol 2010, 11:103-112.
43. Podar K., Raab M.S., Zhang J., McMillin D., Breitkreutz I., Tai Y.T., et al. Targeting PKC in multiple myeloma: in vitro and in vivo effects of the novel, orally available small-molecule inhibitor enzastaurin (LY317615.HCl). Blood 2007, 109:1669-1677.
44. Qiang Y.W., Walsh K., Yao L., Kedei N., Blumberg P.M., Rubin J.S., et al. Wnts induce migration and invasion of myeloma plasma cells. Blood 2005, 106:1786-1793.
45. Podar K., Tai Y.T., Lin B.K., Narsimhan R.P., Sattler M., Kijima T., et al. Vascular endothelial growth factor-induced migration of multiple myeloma cells is associated with beta 1 integrin- and phosphatidylinositol 3-kinase-dependent PKC alpha activation. J Biol Chem 2002, 277:7875-7881.
46. Raab M.S., Breitkreutz I., Tonon G., Zhang J., Hayden P.J., Nguyen T., et al. Targeting PKC: a novel role for beta-catenin in ER stress and apoptotic signaling. Blood 2009, 113:1513-1521.
47. Aziz M.H., Manoharan H.T., Church D.R., Dreckschmidt N.E., Zhong W., Oberley T.D., et al. Protein kinase Cepsilon interacts with signal transducers and activators of transcription 3 (Stat3), phosphorylates Stat3Ser727, and regulates its constitutive activation in prostate cancer. Cancer Res 2007, 67:8828-8838.
48. Millward T.A., Zolnierowicz S., Hemmings B.A. Regulation of protein kinase cascades by protein phosphatase 2A. Trends Biochem Sci 1999, 24:186-191.
49. Janssens V., Goris J. Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Biochem J 2001, 353:417-439.
50. Kang H.S., Choi I. Protein phosphatase 2A modulates the proliferation of human multiple myeloma cells via regulation of the production of reactive oxygen intermediates and anti-apoptotic factors. Cell Immunol 2001, 213:34-44.
51. Woetmann A., Nielsen M., Christensen S.T., Brockdorff J., Kaltoft K., Engel A.M., et al. Inhibition of protein phosphatase 2A induces serine/threonine phosphorylation, subcellular redistribution, and functional inhibition of STAT3. Proc Natl Acad Sci U S A 1999, 96:10620-10625.