Chapter 7 Analysis of Tyrosine-Phosphorylated Proteins in Rat Brain Mitochondria

Methods in Enzymology

Volumn 457, Issue B, 2009, Pages 117-136

  Lewandrowski, Urs ^a   Tibaldi, Elena ^b   Cesaro, Luca ^b   Brunati, Anna M ^b   Toninello, Antonio ^b   Sickmann, Albert ^c   Salvi, Mauro ^b  

^a LEIBNIZ INSTITUT FÜR ANALYTISCHE WISSENSCHAFTEN ISAS E V   (Germany)

^b UNIVERSITY OF PADOVA   (Italy)

^c RUHR UNIVERSITY BOCHUM   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

MITOCHONDRIAL PROTEIN; PHOSPHOPROTEIN; PROTEIN KINASE FGR; PROTEIN KINASE LYN; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE; PROTEOME; UNCLASSIFIED DRUG; PHOSPHOPEPTIDE; TYROSINE;

BIOINFORMATICS; BRAIN MITOCHONDRION; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN ISOLATION; PROTEIN PHOSPHORYLATION; PROTEIN PURIFICATION; REVIEW; STRUCTURE ACTIVITY RELATION; ANIMAL; ARTICLE; BRAIN; CHEMICAL STRUCTURE; CHEMISTRY; ISOLATION AND PURIFICATION; METABOLISM; METHODOLOGY; MITOCHONDRION; PHOSPHORYLATION; RAT;

RATTUS;

ANIMALS; BRAIN; MASS SPECTROMETRY; MITOCHONDRIA; MITOCHONDRIAL PROTEINS; MODELS, MOLECULAR; PHOSPHOPEPTIDES; PHOSPHORYLATION; RATS; SRC-FAMILY KINASES; STRUCTURE-ACTIVITY RELATIONSHIP; TYROSINE;

EID: 65449134336     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(09)05007-1     Document Type: Review

References (28)

1. Aleshin E.A., Kirby C., Liu X., Bourenkov G.P., Bartunik H.D., Fromm H.J., and Honzatko R.B. Crystal structure of mutant monomeric hexokinase I reveal multiple ADP binding sites and conformational changes relevant to allosteric regulation. J. Mol. Biol. 296 (2000) 1001-1015
2. Beausoleil S.A., Jedrychowski M., Scwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., and Gygi S.P. Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc. Natl. Acad. Sci. USA 101 (2004) 12130-12135
3. Bodenmiller B., Mueller L.N., Mueller M., Domon B., and Aebersold R. Reproducible isolation of distinct, overlapping segments of the phosphoproteome. Nat. Methods 4 (2007) 231-237
4. Cohen P., and Knebel A. KESTREL: A powerful method for identifying the physiological substrates of protein kinases. Biochem. J. 393 (2006) 1-6
5. Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., and White F.M. Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae. Nat. Biotechnol. 20 (2002) 301-305
6. Geer L.Y., Markey S.P., Kowalak J.A., Wagner L., Xu M., Maynard D.M., Yang X., Shi W., and Bryant S.H. Open mass spectrometry search algorithm. J. Proteome Res. 3 (2004) 958-964
7. Hunter T. The Croonian lecture 1997. The phosphorylation of proteins on tyrosine: Its role in cell growth and disease. Philos. Trans. R. Soc. Lond. B Biol. Sci. 353 (1998) 583-605
8. Itoh S., Lemay S., Osawa M., Che W., Duan Y., Tompkins A., Brookes P.S., Sheu S.S., and Abe J. Mitochondrial Dok-4 recruits Src kinase and regulates NF-kappaB activation in endothelial cells. J. Biol. Chem. 280 (2005) 26383-26396
9. Knebel A., Morrice N., and Cohen P. A novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta. EMBO J. 20 (2001) 4360-4369
10. Larsen M.R., Jensen S.S., Jakobsen L.A., and Heegaard N.H. Exploring the sialiome using titanium dioxide chromatography and mass spectrometry. Mol. Cell. Proteomics 6 (2007) 1778-1787
11. Larsen M.R., Thingholm T.E., Jensen O.N., Roepstorff P., and Jorgensen T.J. Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol. Cell. Proteomics 4 (2005) 873-886
12. Lee L., Salomon A.R., Ficarro S., Mathes I., Lottspeich F., Grossman L.I., and Huttemann M. cAMP-dependent tyrosine phosphorylation of subunit I inhibits cytochrome c oxidase activity. J. Biol. Chem. 280 (2005) 6094-6100
13. Lewandrowski U., Sickmann A., Cesaro L., Brunati A.M., Toninello A., and Salvi M. Identification of new tyrosine phosphorylated proteins in rat brain mitochondria. FEBS Lett. 582 (2008) 1104-1110
14. Livigni A., Scorziello A., Agnese S., Adornetto A., Carlucci A., Garbi C., Castaldo L., Annunziato L., Avvedimento E.V., and Feliciello A. Mitochondrial AKAP121 links cAMP and src signaling to oxidative metabolism. Mol. Biol. Cell. 17 (2006) 263-271
15. Miyazaki T., Neff L., Tanaka S., Horne W.C., and Baron R. Regulation of cytochrome c oxidase activity by c-Src in osteoclasts. J. Cell. Biol. 160 (2003) 709-718
16. Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., and Mann M. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127 (2006) 635-648
17. Pagliarini D.J., and Dixon J.E. Mitochondrial modulation: Reversible phosphorylation takes center stage?. Trends Biochem. Sci. 31 (2006) 26-34
18. Pagliarini D.J., Wiley S.E., Kimple M.E., Dixon J.R., Kelly P., Worby C.A., Casey P.J., and Dixon J.E. Involvement of a mitochondrial phosphatase in the regulation of ATP production and insulin secretion in pancreatic beta cells. Mol. Cell 19 (2005) 197-207
19. Pebay-Peyroula E., Dahout-Gonzalez C., Kah R., Trezeguet V., Lauquin G.J.M., and Brandolin G. Structure of mitochondrial ADP/ATP carrier in complex with carboxyactractyloside. Nature 426 (2003) 39-44
20. Perkins D.N., Pappin D.J., Creasy D.M., and Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20 (1999) 3551-3567
21. Pinkse M.W., Uitto P.M., Hilhorst M.J., Ooms B., and Heck A.J. Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns. Anal. Chem. 76 (2004) 3935-3943
22. Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.M., Polakiewicz R.D., and Comb M.J. Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat. Biotechnol. 23 (2005) 94-101
23. Salvi M., Brunati A.M., La Rocca N., Bordin L., Clari G., and Toninello A. Characterization and location of Src-dependent Tyrosine phosphorylation in rat brain mitochondria. Biochim. Biophys. Acta 1589 (2002) 181-195
24. Salvi M., Brunati A.M., and Toninello A. Tyrosine phosphorylation in mitochondria: A new frontier in mitochondrial signaling. Free Radic. Biol. Med. 38 (2005) 1267-1277
25. Salvi M., Morrice N., Brunati A.M., and Toninello A. Identification of the flavoprotein of succinate dehydrogenase and aconitase as in vitro mitochondrial substrates of Fgr tyrosine kinase. FEBS Lett. 581 (2007) 5579-5585
26. Salvi M., Stringaro A., Brunati A.M., Agostinelli E., Arancia G., Clari G., and Toninello A. Tyrosine phosphatase activity in mitochondria: Presence of Shp-2 phosphatase in mitochondria. Cell. Mol. Life Sci. 61 (2004) 2393-2404
27. Schindler J., Lewandrowski U., Sickmann A., and Friauf E. Aqueous polymer two-phase systems for the proteomic analysis of plasma membranes from minute brain samples. J. Proteome Res. 7 (2008) 432-442
28. Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schutz C., Walter U., Gambaryan S., and Sickmann A. Phosphoproteome of resting human platelets. J. Proteome Res. 7 (2008) 526-534