Phosphate-affinity gel electrophoresis using a phos-tag molecule for phosphoproteome study

Current Proteomics

Volumn 6, Issue 2, 2009, Pages 104-121

  Kinoshita, Eiji ^a   Emiko, Kinoshita Kikuta ^a   Koike, Tohru ^a  

^a HIROSHIMA UNIVERSITY   (Japan)

Author keywords

Affinity electrophoresis; Phos tag; Phosphoproteo mics; Phosphorylated protein; Phosphorylation; Protein kinase; Protein phosphatase; Signal transduction

Indexed keywords

PHOS;

EID: 67650908878     PISSN: 15701646     EISSN: None     Source Type: Journal    
DOI: 10.2174/157016409788680965     Document Type: Article

References (114)

1. 2-specific regulation of the ferrous heme-based sensor kinase FixL from Sinorhizobium meliloti and its aberrant inactivation in the ferric form. Biochem. Biophys. Res. Commun. 304 :136-42.
2. Akita, S., Umezawa, N. and Higuchi, T. (2005). On-bead fluorescence assay for serine/threonine kinases. Org. Lett. 7 :5565-8.
3. Akita, S., Umezawa, N., Kato, N. and Higuchi, T. (2008). Array-based fluorescence assay for serine/threonine kinases using specific chemical reaction. Bioorg. Med. Chem. 16 :7788-94.
4. Aoki, S., Jikiba, A., Takeda, K. and Kimura, E. (2004). A zinc(II) complex- conjugated polymer for selective recognition and separation of phosphates. J. Phys. Org. Chem. 17 :489-97.
5. Ariga, K. and Anslyn, E.V. (1992). Manipulating the stoichiometry and strength of phosphodiester binding to a bisguanidine cleft in DMSO/water solutions. J. Org. Chem. 57 :417-9.
6. Barbieri, C.M. and Stock, A.M. (2008). Universally applicable methods for monitoring response regulator aspartate phosphorylation both in vitro and in vivo using Phos-tag-based reagents. Anal. Biochem. 376 :73-82.
7. Barrie, S.E., Eno-Amooquaye, E., Hardcastle, A., Platt, G., Richards, J., Bedford, D., Workman, P., Aherne, W., et al. (2003). High-throughput screening for the identification of small-molecule inhibitors of retino- blastoma protein phosphorylation in cells. Anal. Biochem. 320 :66-74.
8. Berger, M. and Schmidtchen, F.P. (1996). Electroneutral artificial hosts for oxoanions active in strong donor solvents. J. Am. Chem. Soc. 118 :8947-8.
9. Cohen, P. (2002). Protein kinase-the major drug targets of the twenty-first century? Nat. Rev. DrugDiscov. 1 :309-15.
10. Das, S., Wong, R., Rajapakse, N., Murphy, E. and Steenbergen, C. (2008). Glycogen synthase kinase 3 inhibition slows mitochondrial adenine nu- cleotide transport and regulates voltage-dependent anion Channel phos-phorylation. Circ. Res. 103 :983-91.
11. David, M., Daveran, M.L., Batut, J., Dedieu, A., Domergue, O., Ghai, J., Hertig, C., Boistard, P., et al. (1988). Cascade regulation of nif gene expression in Rhizobium meliloti. Cell 54 :671-83.
12. Devault, A., Gueydon, E. and Schwob, E. (2008). Interplay between S- cyclin-dependent kinase and Dbf4-dependent kinase in controlling DNA replication through phosphorylation of yeast Mcm4 N-terminal domain. Mol. Biol. Cell 19 :2267-77.
13. Fujioka, H., Koike, T., Yamada, N. and Kimura, E. (1996). A new bis(zinc(II)-cyclen) complex as a novel chelator for barbiturates and phosphates. Heterocycles 42 :775-87.
14. Gafken, P.R. and Lampe, P.D. (2006). Methodologies for characterizing phosphoproteins by mass spectrometry. Cell Commun. Adhes. 13 :249-62.
15. Gallon, C.E. (2008). Current techniques for the study of troponin I phos- phorylation in human heart. J. Muscle Res. Cell Motil. 29 :169-72.
16. Ge, Y., Preston, R.J. and Owen, R.D. (2007). Toxicoproteomics and its application to human health risk assessment. Proteomics Clin. Appl. 1 :1613-24.
17. Gilles-Gonzalez, M.A., Ditta, G..S. and Helinski, D.R. (1991). A haemopro- tein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti. Nature 350 :170-2.
18. Girardet, J.M., Miclo, L., Florent, S., Molle, D. and Gaillard, J.L. (2006). Determination of the phosphorylation level and deamidation susceptibility of equine P-casein. Proteomics 6 :3707-17.
19. de Graauw, M., Hensbergen, P. and van de Water, B. (2006). Phospho- protemic analysis of cellular signaling. Electrophoresis 27 :2676-86.
20. Görg, A., Obermaier, C., Boguth, G., Harder, A., Scheibe, B., Wildgruber, R. and Weiss, W. (2000). The current state of two-dimensional electro- phoresis with immobilized pH gradients. Electrophoresis 21 :1037-53.
21. Grob, A., Roussel, P., Wright, J.E., McStay, B., Hernandez-Verdun, D. and Sirri, V. (2009). Involvement of SIRT7 in resumption of rDNA transcription at the exit from mitosis. J. Cell Sci. 122 :489-98.
22. Gui, Y., Zheng, X.L., Zheng, J. and Walsh, M.P. (2008). Inhibition of rat aortic smooth muscle contraction by 2-methoxyestradiol. Am. J. Physiol. Heart Circ. Physiol. 295 :H1935-42.
23. Hattori, S., Iida, N. and Kosako, H. (2008). Identification of protein kinase substrates by proteomic approaches. Expert Rev. Proteomics 5 :497-505.
24. Van Hekken, D.L. and Thompson M.P. (1992). Application of PhastSystem to the resolution of bovine milk proteins on urea-polyacrylamide gel electrophoresis. J. Dairy Sci. 75 :1204-10.
25. Hirano, K., Matsui, H., Tanaka, T., Matsuura, F., Satouchi, K. and Koike, T. (2004). Production of 1,2-didocosahexaenoyl phosphatidylcholine by bonito muscle lysophosphatidylcholine/transacylase. J. Biochem. 136 :477-83.
26. Hoving, S., Gerrits, B., Voshol, H., Muller, D., Roberts, R.C. and van Oos- trum, J. (2002). Preparative two-dimensional gel electrophoresis at alkaline pH using narrow range immobilized pH gradients. Proteomics 2 :127-34.
27. Hunter, T. (2000). Signaling-2000 and beyond. Cell 100 :113-27.
28. Hunter, T. (2002). Tyrosine phosphorylation in cell signaling and disease. Keio J. Med. 51 :61-71.
29. Igarashi, J., Murase, M., Iizuka, A., Pichierri, F., Martinkova, M. and Shi- mizu, T. (2008). Elucidation of the heme binding site of heme-regulated eukaryotic initiation factor 2α kinase and the role of the regulatory motif in heme sensing by spectroscopic and catalytic studies of mutant proteins. J. Biol. Chem. 283 :18782-91.
30. 2+ sensitization in murine experimental colitis. Mol. Pharmacol. 75 :1031-41.
31. Ihara, M., Yamasaki, N., Hagiwara, A., Tanigaki, A., Kitano, A., Hikawa, R., Tomimoto, H., Noda, M., et al. (2007). Sept4, a component of pre- synaptic scaffold and Lewy bodies, is required for the suppression of aα- synuclein neurotoxicity. Neuron 53 :519-33.
32. Inamori, K., Kyo, M., Matsukawa, K., Inoue, Y., Sonoda, T., Tatematsu, K., Tanizawa, K., Mori, T., et al. (2008). Optimal surface chemistry for peptide immobilization in on-chip phosphorylation analysis. Anal. Chem. 80 :643-50.
33. Inamori, K., Kyo, M., Nishiya, Y., Inoue, Y., Sonoda, T., Kinoshita, E., Koike, T. and Katayama, Y. (2005). Detection and quantification of on- chip phosphorylated peptides by surface plasmon resonance imaging techniques using a phosphate capture molecule. Anal. Chem. 77 :3979-85.
34. Inoue, S., Kinoshita, T., Matsumoto, M., Nakayama, K., Doi, M. and Shi- mazaki, K. (2008). Blue light-induced autophosphorylation of phototro- pin is a primary step for signaling. Proc. Natl. Acad. Sci. USA 105 :5626-31.
35. Ishiai, M., Kitao, H., Smogorzewska, A., Tomida, J., Kinomura, A., Uchida, E., Saberi, A., Kinoshita, E., et al. (2008). FANCI phosphorylation functions as a molecular switch to turn on the Fanconi anemia pathway. Nat. Struct. Mol. Biol. 15 :1138-46.
36. Ishida, A., Kameshita, I., Sueyoshi, N., Taniguchi, T. and Shigeri, Y. (2007). Recent advances in technologies for analyzing protein kinases. J. Pharmacol. Sci. 103 :5-11.
37. Johnson, S.A. and Hunter, T. (2005). Kinomics: methods for deciphering the kinome. Nat. Methods 2 :17-25.
38. Jubian, V., Veronese, A., Dixon, R.P. and Hamilton, A.D. (1995). Acceleration of a phosphate diester transesterification reaction by bis(alkylguanidinium) receptors containing an appended general base. Angew. Chem. Int. Ed. Engl. 34 :1237-9.
39. Kaufmann, H., Bailey, J.E. and Fussenegger, M. (2001). Use of antibodies for detection of phosphorylated proteins separated by two-dimensional gel electrophoresis. Proteomics 1 :194-9.
40. Kawashima, T., Bao, Y.C., Minoshima, Y., Nomura, Y., Hatori, T., Hori, T., Fukagawa, T., Fukada, T., et al. (2009). A Rac GTPase-activating protein, MgcRacGAP, is a nuclear localizing signal-containing nuclear chaperone in the activation of STAT transcription factors. Mol. Cell Biol. 29 :1796-813.
41. Kersten, B., Agrawal, G.K., Iwahashi, H. and Rakwal, R. (2006). Plant phosphoproteomics: a long road ahead. Proteomics 6 :5517-28.
42. Kimura, E. and Koike, T. (1998). Dynamic anion recognition by macrocyc- lic polyamines in neutral pH aqueous solution: development from static anion complexes to an enolate complex. Chem. Commun. 1495-500.
43. II-1,4,7,10- tetraazacyclododecane) complex as a new receptor for phosphate dian- ions in aqueous solution. J. Am. Chem. Soc. 119 :3068-76.
44. Kinoshita, E., Ishikawa, K., Kinoshita-Kikuta, E., Ohtani, K., Shiro, M. and Koike, T. (2005a) An alkoxide-bridged dinuclear zinc(II) hexaazacryp- tate: a novel phosphate capture molecule in aqueous solution. Bull. Chem. Soc. Jpn. 78 :125-31.
45. Kinoshita, E., Kinoshita-Kikuta, E., Matsubara, M., Aoki, Y., Ohie, S., Mouri, Y. and Koike, T. (2009). Two-dimensional phosphate-affinity gel electrophoresis for the analysis of phosphoprotein isotypes. Electro- phoresis 30 :550-9.
46. Kinoshita, E., Kinoshita-Kikuta, E., Matsubara, M., Yamada, S., Nakamura, H., Shiro, Y., Aoki, Y., Okita, K., et al. (2008). Separation of phos- phoprotein isotypes having the same number of phosphate groups using phosphate-affinity SDS-PAGE. Proteomics 8 :2994-3003.
47. Kinoshita, E., Kinoshita-Kikuta, E., Takiyama, K. and Koike, T. (2006). Phosphate-binding tag, a new tool to visualize phosphorylated proteins. Mol. Cell. Proteomics 5 :749-57.
48. Kinoshita, E., Takahashi, M., Takeda, H., Shiro, M. and Koike, T. (2004). Recognition of phosphate monoester dianion by an alkoxide-bridged dinuclear zinc(II) complex. Dalton Trans. 1189-93.
49. Kinoshita, E., Yamada, A., Takeda, H., Kinoshita-Kikuta, E. and Koike, T. (2005b) Novel immobilized zinc(II) affinity chromatography for phos-phopeptides and phosphorylated proteins. J. Sep. Sci. 28 :155-62.
50. Kinoshita-Kikuta, E., Kinoshita, E. and Koike, T. (2009). Phos-tag beads as an immunoblotting enhancer for selective detection of phosphoproteins in cell lysates. Anal. Biochem. 389 :83-5.
51. Kinoshita-Kikuta, E., Aoki, Y., Kinoshita, E. and Koike T. (2007). Label-free kinase profiling using phosphate affinity polyacrylamide gel elec- trophoresis. Mol. Cell. Proteomics 6 :356-66.
52. Kinoshita-Kikuta, E., Kinoshita, E., Yamada, A., Endo, M. and Koike, T. (2006). Enrichment of phosphorylated proteins from cell lysate using a novel phosphate-affinity chromatography at physiological pH. Pro-teomics 6 :5088-95.
53. Koike, T. and Kimura, E. (1991). Roles of zinc(II) ion in phosphatases. A model study with zinc(II)-macrocyclic polyamine complexes. J. Am. Chem. Soc. 113 :8935-41.
54. Koike, T., Inoue, M., Kimura, E. and Shiro, M. (1996). Novel properties of cooperative dinuclear zinc(II) ions: the selective recognition of phos- phomonoesters and their P-O ester bond cleavage by a new dinuclear zinc(II) cryptate. J. Am. Chem. Soc. 118 :3091-9.
55. Kubo-Murai, M., Hazeki, K., Sukenobu, N., Yoshikawa, K., Nigorikawa, K., Inoue, K., Yamamoto, T., Matsumoto, M., et al. (2007). Protein kinase C8 binds TIRAP/Mal to participate in TLR signaling. Mol. Immunol. 44 :2257-64.
56. Kubota, T., Matsuoka, M., Chang, T.H., Tailor, P., Sasaki, T., Tashiro, M., Kato, A. and Ozato, K. (2008). Virus infection triggers SUMOylation of IRF3 and IRF7, leading to the negative regulation of type I interferon gene expression. J. Biol. Chem. 283 :25660-70.
57. Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 :680-5.
58. Lee, B.S., Jayathilaka, G.D., Huang, J.S., Decresce, D., Borgia, J.A., Zhou, X. and Gupta, S. (2008a) Modification of the immobilized metal affinity electrophoresis using sodium dodecyl sulfate polyacrylamide gel electrophoresis. Electrophoresis 29 :3160-3.
59. Lee, B.S., Lasanthi, G.D., Jayathilaka, G.D., Huang, J.S. and Gupta, S. (2008b) Immobilized metal affinity electrophoresis: a novel method of capturing phosphoproteins by electrophoresis. J. Biomol. Tech. 19 :106-8.
60. Lee, G., Thangavel, R., Sharma, V.M., Litersky, J.M., Bhaskar, K., Fang, S.M., Do, L.H., Andreadis, A., et al. (2004). Phosphorylation of tau by Fyn: implications for Alzheimer's disease. J. Neurosci. 24 :2304-12.
61. Lee, J., Ahn, H.C., Shin, D. and Ahn, D.R. (2008c) Label-free and real-time monitoring of phosphatase reactions using a phosphate-specific and fluorescent probe. Bull. Korean Chem. Soc. 29 :943-7.
62. Lee, V.M., Goedert, M. and Trojanowski, J.Q. (2001). Neurodegenerative tauopathies. Annu. Rev. Neurosci. 24 :1121-59.
63. Maeder, C.I., Hink, M.A., Kinkhabwala, A., Mayr, R., Bastiaens, P.I.H. and Knop, M. (2007). Spatial regulation of Fus3 MAP kinase activity through a reaction-diffusion mechanism in yeast pheromone signalling. Nat. Cell Biol. 9 :1319-26.
64. Magrans, J.O., Ortiz, A.R., Molins, M.A., Lebouille, P.H.P., Sanchez- Quesada, J., Porados, P., Pons, M., Gago, F., et al. (1996). A designed non-peptidic receptor that mimics the phosphocholine binding site of the McPC603 antibody. Angew. Chem. Int. Ed. Engl. 35 :1712-5.
65. Mann, M., Ong, S.E., Granborg, M., Steen, H., Jensen, O.N. and Pandey, A. (2002). Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome. Trends Biotechnol. 20 :261-8.
66. Manning, G., Whyte, D.B., Martinez, R., Hunter, T. and Sudarsanam, S. (2002). The protein kinase complement of the human genome. Science 298 :1912-34.
67. Masaoka, T., Nishi, M., Ryo, A., Endo, Y. and Sawasaki, T. (2008). The wheat germ cell-free based screening of protein substrates of cal-cium/calmodulin-dependent protein kinase II delta. FEBS Lett. 582 :1795-801.
68. Matos, J., Lipp, J.J., Bogdanova, A., Guillot, S., Okaz, E., Junqueira, M., Shevchenko, A. and Zachariae W. (2008). Dbf4-dependent CDC7 kinase links DNA replication to the segregation of homologous chromosomes in meiosis I. Cell 135 :662-78.
69. Matsui, I., Hamano, T., Mikami, S., Fujii, N., Takabatake, Y., Nagasawa, Y., Kawada, N., Ito, T., et al. (2009). Fully phosphorylated fetuin-A forms a mineral complex in the serum of rats with adenine-induced renal failure. Kidney Int. 75 :915-28.
70. Miyata, Y. and Nishida, E. (2007). Analysis of the CK2-dependent phos- phorylation of serine 13 in Cdc37 using a phospho-specific antibody and phospho-affinity gel electrophoresis. FEBS J. 274 :5690-703.
71. Miyatake, H., Mukai, M., Park, S.Y., Adachi, S., Tamura, K., Nakamura, H., Nakamura, K., Tsuchiya, T., et al. (2000). Sensory mechanism of oxygen sensor FixL from Rhizobium meliloti: crystallographic, mutagenesis and resonance Raman spectroscopic studies. J. Mol. Biol. 301 :415-31.
72. Molina, H., Horn, D.M., Tang, N., Mathivanan, S. and Pandey, A. (2007). Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc. Natl. Acad. Sci. USA 104 :2199-204.
73. Molloy, M.P. and Andrews, P.C. (2001). Phosphopeptide derivatization signatures to identify serine and threonine phosphorylated peptides by mass spectrometry. Anal. Chem. 73 :5387-94.
74. Mori, T., Inamori, K., Inoue, Y., Han, X., Yamanouchi, G., Niidome, T. and Katayama, Y. (2008). Evaluation of protein kinase activities of cell lysates using peptide microarrays based on surface plasmon resonance imaging. Anal. Biochem. 375 :223-31.
75. Mukai, N., Nakanishi, T., Shimizu, A., Takubo, T. and Ikeda, T. (2008). Identification of phosphotyrosyl proteins in vitreous humours of patients with vitreoretinal diseases by sodium dodecyl sulphate- polyacrylamide gel electrophoresis/Western blotting/matrix-assisted laser desorption time-of-flight mass spectrometry. Ann. Clin. Biochem. 45 :307-12.
76. Nakamura, H., Kumita, H., Imai, K., Iizuka, T. and Shiro, Y. (2004). ADP reduces the oxygen-binding affinity of a sensory histidine kinase, FixL: the possibility of an enhanced reciprocating kinase reaction. Proc. Natl. Acad. Sci. USA 101 :2742-6.
77. Nakamura, H., Saito, K., Ito, E., Tamura, K., Tsuchiya, T., Nishigaki, K., Shiro, Y. and Iizuka, T. (1998). Identification of the hydrophobic amino acid residues required for heme assembly in the rhizobial oxygen sensor protein FixL. Biochem. Biophys. Res. Commun. 247 :427-31.
78. Nakanishi, T., Ando, E., Furuta, M., Kinoshita, E., Kinoshita-Kikuta, E., Koike, T., Tsunasawa, S. and Nishimura, O. (2007). Identification on membrane and characterization of phosphoproteins using an alkoxide- bridged dinuclear metal complex as a phosphate-binding tag molecule. J. Biomol. Tech. 18 :278-86.
79. Nalivaeva, N.N. and Turner, A.J. (2001). Post-translational modifications of proteins: acetylcholinesterase as a model system. Proteomics 1 :735-47.
80. Oda, Y., Nagasu, T. and Chait, B.T. (2001). Enrichment analysis of phos- phorylated proteins as a tool for probing the phosphoproteome. Nat. Biotechnol. 19 :379-82.
81. O'Farrell, P.H. (1975). High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250 :4007-21.
82. O'Farrell, P.Z., Goodman, H.M. and O'Farrell, P.H. (1977). High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell 12 :1133-42.
83. Oh, H. and Irvine, K.D. (2008). In vivo regulation of Yorkie phosphoryla- tion and localization. Development 135 :1081-8.
84. Ojida, A., Mito-oka, Y., Inoue, M. and Hamachi, I. (2002). First artificial receptors and chemosensors toward phosphorylated peptide in aqueous solution. J. Am. Chem. Soc. 124 :6256-8.
85. Olive, D.M. (2004). Quantitative methods for the analysis of protein phos- phorylation in drug development. Expert Rev. Proteomics 1 :327-41.
86. Oyama, S., Yamakawa, H., Sasagawa, N., Hosoi, Y., Futai, E. and Ishiura, S. (2009). Dysbindin-1, a schizophrenia-related protein, functionally interacts with the DNA- dependent protein kinase complex in an isoform- dependent manner. PLoS One 4 :e4199.
87. Peterson, R.F. (1963). High resolution of milk proteins obtained by gel electrophoresis. J. Dairy Sci. 46 :1136-9.
88. Prudent, M., Rossier, J.S., Lion, N. and Girault, H.H. (2008). Microfabri- cated dual sprayer for on-line mass tagging of phosphopeptides. Anal. Chem. 80 :2531-8.
89. Puddu, F., Granata, M., Di Nola, L., Balestrini, A., Piergiovanni, G., Lazza- ro, F., Giannattasio, M., Plevani, P., et al. (2008). Phosphorylation of the budding yeast 9-1-1 complex is required for Dpb11 function in the full activation of the UV-induced DNA damage checkpoint. Mol. Cell. Biol. 28 :4782-93.
90. Saito, K., Ito, E., Hosono, K., Nakamura, K., Imai, K., Iizuka, T., Shiro, Y. and Nakamura, H. (2003). The uncoupling of oxygen sensing, phos- phorylation signalling and transcriptional activation in oxygen sensor FixL and FixJ mutants. Mol. Microbiol. 48 :373-83.
91. Sakai, R., Fukuzawa, M., Nakano, R., Tatsuki, S. and Ishikawa, Y. (2009). Alternative suppression of transcription from two desaturase genes is the key for species-specific sex pheromone biosynthesis in two Ostrinia moths. Insect Biochem. Mol. Biol. 39 :62-7.
92. Schmidt, S.R., Schweikart, F. and Andersson, M.E. (2007). Current methods for phosphoprotein isolation and enrichment. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 849 :154-62.
93. Sessler, J.L., Davis, J.M., Kral, V., Kimbrough, T. and Lynch, V. (2003). Water soluble sapphyrins: potential fluorescent phosphate anion sensors. Org. Biomol. Chem. 1 :4113-23.
94. Shigaki, S., Yamaji, T., Han, X., Yamanouchi, G., Sonoda, T., Okitsu, O., Mori, T., Niidome, T., et al. (2007). A peptide micoarray for the detection of protein kinase activity in cell lysate. Anal. Sci. 23 :271-5.
95. Shults, M.D., Kozlov, I.A., Nelson, N., Kermani, B.G., Melnyk, P.C., Shevchenko, V., Srinivasan, A., Musmacker, J., et al. (2007). A multiplexed protein kinase assay. Chembiochem 8 :933-42.
96. Sopko, R. and Andrews, B.J. (2008). Linking the kinome and phosphory- lome-a comprehensive review of approaches to find kinase targets. Mol. Biosyst. 4 :920-33.
97. Steinberg, T.H., Agnew, B.J., Gee, K.R., Leung, W.Y., Goodman, T., Schulenberg, B., Hendrickson, J., Beechem, J.M., et al. (2003). Global quantitative phosphoprotein analysis using multiplexed proteomics technology. Proteomics 3:1128-44.
98. Sumara, G., Formentini, I., Collins, S., Sumara, I., Windak, R., Boden- miller, B., Ramracheya, R., Caille, D., et al. (2009). Regulation of PKD by the MAPK p388 in insulin secretion and glucose homeostasis. Cell 136 :235-48.
99. Takeda, H., Kawasaki, A., Takahashi, M., Yamada, A. and Koike, T. (2003). Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry of phosphorylated compounds using a novel phosphate capture molecule. Rapid Commun. Mass Spectrom. 17 :2075-81.
100. Takeya, K., Loutzenhiser, K., Shiraishi, M., Loutzenhiser, R. and Walsh, M.P. (2008). A highly sensitive technique to measure myosin regulatory light chain phosphorylation: the first quantification in renal arterioles. Am. J. Physiol. Renal. Physiol. 294 :F1487-92.
101. Takiyama, K., Kinoshita, E., Kinoshita-Kikuta, E., Fujioka, Y., Kubo, Y. and Koike, T. (2009). A Phos-tag-based fluorescence resonance energy transfer system for the analysis of the dephosphorylation of phos- phopeptides. Anal. Biochem. 388 :235-41.
102. Tanaka, A., Nakamura, H., Shiro, Y. and Fujii, H. (2006). Roles of the heme distal residues of FixL in O2 sensing: a single convergent structure of the heme moiety is relevant to the downregulation of kinase activity. Biochemistry 45 :2515-23.
103. Tanaka, T., Tsutsui, H., Hirano, K., Koike, T., Tokumura, A. and Satouchi, K. (2004). Quantitative analysis of lysophosphatidic acid by time-of- flight mass spectrometry using a phosphate-capture molecule. J. Lipid Res. 45 :2145-50.
104. Tanuma, N., Nomura, M., Ikeda, M., Kasugai, I., Tsubaki, Y., Takagaki, K., Kawamura, T., Yamashita, Y., et al. (2009). Protein phosphatase Dusp26 associates with KIF3 motor and promotes N-cadherinmediated cell-cell adhesion. Oncogene 28 :752-61.
105. Tatematsu, K., Yoshimoto, N., Okajima, T., Tanizawa, K. and Kuroda, S. (2008). Identification of ubiquitin ligase activity of RBCK1 and its inhibition by splice variant RBCK2 and protein kinase Cβ. J. Biol. Chem. 283 :11575-85.
106. Thompson, M.P. (1970). Phenotyping milk proteins: a review. J. Dairy Sci. 53 :1341-8.
107. Uhrig, R.G., O'Leary, B., Spang, H.E., MacDonald, J.A., She, Y.M. and Plaxton, W.C. (2008). Coimmunopurification of phosphorylated bacterial- and plant-type phosphoenolpyruvate carboxylases with the plas- tidial pyruvate dehydrogenase complex from developing castor oil seeds. Plant Physiol. 146 :1346-57.
108. Vallee, B.L. (1986). A synopsis of zinc biology and pathology. In Zinc enzymes (eds. I. Bertini, C. Luchinat, W. Maret and M. Zeppezauer), Brikhäuser, Boston, pp 1-15.
109. Waddleton, D., Ramachandran, C. and Wang, Q. (2002). Development of a time-resolved fluorescent assay for measuring tyrosine-phosphorylated proteins in cells. Anal. Biochem. 309 :150-7.
110. West, A.H. and Stock, A.M. (2001). Histidine kinases and response regulator proteins in two-component signaling systems, Trends Biochem. Sci. 26 :369-76.
111. Yamada, S., Nakamura, H., Kinoshita, E., Kinoshita-Kikuta, E., Kioke, T. and Shiro, Y. (2007). Separation of a phosphorylated histidine protein using phosphate affinity polyacrylamide gel electrophoresis. Anal. Biochem. 360 :160-2.
112. Yang, W., Steen, H. and Freeman, M.R. (2008). Proteomic approaches to the analysis of multiprotein signaling complexes. Proteomics 8 :832-51.
113. Ydenberg, C.A. and Rose, M.D. (2009). Antagonistic regulation of Fus2p nuclear localization by pheromone signaling and the cell cycle. J. Cell Biol. 184 :409-22.
114. Zhou, H., Watts, J.D. and Aebersold, R. (2001). A systematic approach to the analysis of protein phosphorylation. Nat. Biotechnol. 19 :375-8.