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Volumn 1697, Issue 1-2, 2004, Pages 39-51

Biosensors of protein kinase action: From in vitro assays to living cells

Author keywords

Combinatorial library; Consensus sequence; ELISA; Enzyme linked immunosorbent assay; Fluorescence resonance energy transfer; FRET; HBTU; Protein kinase sensor; Protein kinase substrate; Signal transduction

Indexed keywords

PEPTIDE LIBRARY; PROTEIN KINASE C;

EID: 1542298996     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2003.11.012     Document Type: Conference Paper
Times cited : (43)

References (47)
  • 3
    • 0344809977 scopus 로고    scopus 로고
    • ATP-site directed inhibitors of cyclin-dependent kinases
    • Gray N., Detivaud L., Doerig C., Meijer L. ATP-site directed inhibitors of cyclin-dependent kinases. Curr. Med. Chem. 6:1999;859-875.
    • (1999) Curr. Med. Chem. , vol.6 , pp. 859-875
    • Gray, N.1    Detivaud, L.2    Doerig, C.3    Meijer, L.4
  • 4
    • 0035150402 scopus 로고    scopus 로고
    • Rho-Rho-kinase pathway in smooth muscle contraction and cytoskeletal reorganization of non-muscle cells
    • Fukata Y., Amano M., Kaibuchi K. Rho-Rho-kinase pathway in smooth muscle contraction and cytoskeletal reorganization of non-muscle cells. Trends Pharmacol. Sci. 22:2001;32-39.
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 32-39
    • Fukata, Y.1    Amano, M.2    Kaibuchi, K.3
  • 6
    • 0034142054 scopus 로고    scopus 로고
    • Postsynaptic protein phosphorylation and LTP
    • Soderling T.R., Derkach V.A. Postsynaptic protein phosphorylation and LTP. Trends Neurosci. 23:2000;75-80.
    • (2000) Trends Neurosci. , vol.23 , pp. 75-80
    • Soderling, T.R.1    Derkach, V.A.2
  • 7
    • 0030919210 scopus 로고    scopus 로고
    • Synergies and coincidence requirements between NO, cGMP, and Ca2+ in the induction of cerebellar long-term depression
    • Lev-Ram V., Jiang T., Wood J., Lawrence D.S., Tsien R.Y. Synergies and coincidence requirements between NO, cGMP, and Ca2+ in the induction of cerebellar long-term depression. Neuron. 18:1997;1025-1038.
    • (1997) Neuron , vol.18 , pp. 1025-1038
    • Lev-Ram, V.1    Jiang, T.2    Wood, J.3    Lawrence, D.S.4    Tsien, R.Y.5
  • 9
    • 0032482375 scopus 로고    scopus 로고
    • Imaging the spatial dynamics of calmodulin activation during mitosis
    • Torok K., Wilding M., Groigno L., Patel R., Whitaker M. Imaging the spatial dynamics of calmodulin activation during mitosis. Curr. Biol. 8:1998;692-699.
    • (1998) Curr. Biol. , vol.8 , pp. 692-699
    • Torok, K.1    Wilding, M.2    Groigno, L.3    Patel, R.4    Whitaker, M.5
  • 10
    • 0030581751 scopus 로고    scopus 로고
    • How do protein kinases recognize their substrates?
    • Pinna L.A., Ruzzene M. How do protein kinases recognize their substrates? Biochim. Biophys. Acta. 1314:1996;191-225.
    • (1996) Biochim. Biophys. Acta , vol.1314 , pp. 191-225
    • Pinna, L.A.1    Ruzzene, M.2
  • 12
    • 0028124583 scopus 로고
    • The active site substrate specificity of protein kinase C
    • Kwon Y.G., Mendelow M., Lawrence D.S. The active site substrate specificity of protein kinase C. J. Biol. Chem. 269:1994;4839-4844.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4839-4844
    • Kwon, Y.G.1    Mendelow, M.2    Lawrence, D.S.3
  • 13
    • 0030042940 scopus 로고    scopus 로고
    • Precision substrate targeting of protein kinases. the cGMP- and cAMP-dependent protein kinases
    • Wood J.S., Yan X., Mendelow M., Corbin J.D., Francis S.H., Lawrence D.S. Precision substrate targeting of protein kinases. The cGMP- and cAMP-dependent protein kinases. J. Biol. Chem. 271:1996;174-179.
    • (1996) J. Biol. Chem. , vol.271 , pp. 174-179
    • Wood, J.S.1    Yan, X.2    Mendelow, M.3    Corbin, J.D.4    Francis, S.H.5    Lawrence, D.S.6
  • 14
    • 0029912745 scopus 로고    scopus 로고
    • Distinguishing between a mitogenic and two closely related nonmitogenic protein kinases
    • Yan X., Lawrence D.S., Corbin J.D., Francis S.H. Distinguishing between a mitogenic and two closely related nonmitogenic protein kinases. J. Am. Chem. Soc. 118:1996;11684-11685.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11684-11685
    • Yan, X.1    Lawrence, D.S.2    Corbin, J.D.3    Francis, S.H.4
  • 15
    • 0030061201 scopus 로고    scopus 로고
    • Distinguishing between closely related protein kinases: A variation on the bisubstrate inhibitor theme
    • Yan X., Lawrence D.S., Corbin J.D., Francis S.H. Distinguishing between closely related protein kinases: a variation on the bisubstrate inhibitor theme. J. Am. Chem. Soc. 118:1996;6321-6322.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6321-6322
    • Yan, X.1    Lawrence, D.S.2    Corbin, J.D.3    Francis, S.H.4
  • 16
    • 0032008085 scopus 로고    scopus 로고
    • Engineering Src family protein kinases with unnatural nucleotide specificity
    • Liu Y., Shah K., Yang F., Witucki L., Shokat K.M. Engineering Src family protein kinases with unnatural nucleotide specificity. Chem. Biol. 5:1998;91-101.
    • (1998) Chem. Biol. , vol.5 , pp. 91-101
    • Liu, Y.1    Shah, K.2    Yang, F.3    Witucki, L.4    Shokat, K.M.5
  • 18
    • 0030828409 scopus 로고    scopus 로고
    • Imaging of cAMP-dependent protein kinase activity in living neural cells using a novel fluorescent substrate
    • Higashi H., Sato K., Ohtake A., Omori A., Yoshida S., Kudo Y. Imaging of cAMP-dependent protein kinase activity in living neural cells using a novel fluorescent substrate. FEBS Lett. 414:1997;55-60.
    • (1997) FEBS Lett. , vol.414 , pp. 55-60
    • Higashi, H.1    Sato, K.2    Ohtake, A.3    Omori, A.4    Yoshida, S.5    Kudo, Y.6
  • 19
    • 0025733796 scopus 로고
    • A continuous fluorescence assay for protein kinase C
    • McIlroy B.K., Walters J.D., Johnson J.D. A continuous fluorescence assay for protein kinase C. Anal. Biochem. 195:1991;148-152.
    • (1991) Anal. Biochem. , vol.195 , pp. 148-152
    • McIlroy, B.K.1    Walters, J.D.2    Johnson, J.D.3
  • 20
    • 24444442471 scopus 로고    scopus 로고
    • Fluorescence-based sensing of protein kinase a activity using the dual fluorescent-labeled peptide
    • Ohuchi Y., Katayama Y., Maeda M. Fluorescence-based sensing of protein kinase A activity using the dual fluorescent-labeled peptide. Anal. Sci. 17(Supplement):2001;i1465-i1467.
    • (2001) Anal. Sci. , vol.17 , Issue.SUPPLEMENT , pp. 1465-i1467
    • Ohuchi, Y.1    Katayama, Y.2    Maeda, M.3
  • 21
    • 0009252811 scopus 로고
    • Fluorometric assay for adenosine 3′,5′-cyclic monophosphate-dependent protein kinase and phosphoprotein phosphatase activities
    • Wright D.E., Noiman E.S., Chock P.B., Chau V. Fluorometric assay for adenosine 3′,5′-cyclic monophosphate-dependent protein kinase and phosphoprotein phosphatase activities. Proc. Natl. Acad. Sci. U. S. A. 78:1981;6048-6050.
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78 , pp. 6048-6050
    • Wright, D.E.1    Noiman, E.S.2    Chock, P.B.3    Chau, V.4
  • 22
    • 0035903217 scopus 로고    scopus 로고
    • A pair of fluorescent resonace energy transfer-based probes for tyrosine phosphorylation of the CrkII adaptor protein in vivo
    • Kurokawa K., Mochizuki N., Ohba Y., Mizuno H., Miyawaki A., Matsuda M. A pair of fluorescent resonace energy transfer-based probes for tyrosine phosphorylation of the CrkII adaptor protein in vivo. J. Biol. Chem. 276:2001;31305-31310.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31305-31310
    • Kurokawa, K.1    Mochizuki, N.2    Ohba, Y.3    Mizuno, H.4    Miyawaki, A.5    Matsuda, M.6
  • 24
    • 0036196296 scopus 로고    scopus 로고
    • Fluorescent indicators for imaging protein phosphorylation in single living cells
    • Sato M., Ozawa T., Inukai K., Asano T., Umezawa Y. Fluorescent indicators for imaging protein phosphorylation in single living cells. Nat. Biotechnol. 20:2002;287-294.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 287-294
    • Sato, M.1    Ozawa, T.2    Inukai, K.3    Asano, T.4    Umezawa, Y.5
  • 25
    • 0035909994 scopus 로고    scopus 로고
    • Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells
    • Ting A.Y., Kain K.H., Klemke R.L., Tsien R.Y. Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells. Proc. Natl. Acad. Sci. U. S. A. 98:2001;15003-15008.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 15003-15008
    • Ting, A.Y.1    Kain, K.H.2    Klemke, R.L.3    Tsien, R.Y.4
  • 26
    • 0037780971 scopus 로고    scopus 로고
    • A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C
    • Violin J.D., Zhang J., Tsien R.Y., Newton A.C. A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C. J. Cell Biol. 161:2003.
    • (2003) J. Cell Biol. , vol.161
    • Violin, J.D.1    Zhang, J.2    Tsien, R.Y.3    Newton, A.C.4
  • 27
    • 0034254797 scopus 로고    scopus 로고
    • The specificity of the protein kinase C alpha, betaII and gamma isoforms as assessed by an unnatural alcohol-appended peptide library
    • Yan X., Curley K., Lawrence D.S. The specificity of the protein kinase C alpha, betaII and gamma isoforms as assessed by an unnatural alcohol-appended peptide library. Biochem. J. 349:2000;709-715.
    • (2000) Biochem. J. , vol.349 , pp. 709-715
    • Yan, X.1    Curley, K.2    Lawrence, D.S.3
  • 28
    • 0037123172 scopus 로고    scopus 로고
    • Design and synthesis of a fluorescent reporter of protein kinase activity
    • Chen C.-A., Yeh R.H., Lawrence D.S. Design and synthesis of a fluorescent reporter of protein kinase activity. J. Am. Chem. Soc. 124:2002;3840-3841.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 3840-3841
    • Chen, C.-A.1    Yeh, R.H.2    Lawrence, D.S.3
  • 29
    • 0024488636 scopus 로고
    • Fluorescent probes of cell signaling
    • Tsien R.Y. Fluorescent probes of cell signaling. Annu. Rev. Neurosci. 12:1989;227-253.
    • (1989) Annu. Rev. Neurosci. , vol.12 , pp. 227-253
    • Tsien, R.Y.1
  • 30
    • 0024336003 scopus 로고
    • Fluorescent indicators for cytosolic calcium based on rhodamine and fluorescein chromophores
    • Minta A., Kao J.P., Tsien R.Y. Fluorescent indicators for cytosolic calcium based on rhodamine and fluorescein chromophores. J. Biol. Chem. 264:1989;8171-8178.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8171-8178
    • Minta, A.1    Kao, J.P.2    Tsien, R.Y.3
  • 31
  • 32
    • 0024601583 scopus 로고
    • A fluorescent indicator for measuring cytosolic free magnesium
    • Raju B., Murphy E., Levy L.A., Hall R.D., London R.E. A fluorescent indicator for measuring cytosolic free magnesium. Am. J. Physiol. 256:1989;C540-C548.
    • (1989) Am. J. Physiol. , vol.256 , pp. 540-C548
    • Raju, B.1    Murphy, E.2    Levy, L.A.3    Hall, R.D.4    London, R.E.5
  • 35
    • 0035840116 scopus 로고    scopus 로고
    • Synthesis of achiral and chiral peptide nucleic acid (PNA) monomers using Mitsunobu reaction
    • Falkiewicz B., Kolodziejczyk A.S., Liberek B., Wisniewski K. Synthesis of achiral and chiral peptide nucleic acid (PNA) monomers using Mitsunobu reaction. Tetrahedron. 57:2001;7909-7917.
    • (2001) Tetrahedron , vol.57 , pp. 7909-7917
    • Falkiewicz, B.1    Kolodziejczyk, A.S.2    Liberek, B.3    Wisniewski, K.4
  • 36
    • 0001520063 scopus 로고    scopus 로고
    • SH2-directed ligands of the Lck tyrosine kinase
    • Lee T.R., Lawrence D.S. SH2-directed ligands of the Lck tyrosine kinase. J. Med. Chem. 43:2000;1173-1179.
    • (2000) J. Med. Chem. , vol.43 , pp. 1173-1179
    • Lee, T.R.1    Lawrence, D.S.2
  • 37
    • 0035853839 scopus 로고    scopus 로고
    • From consensus sequence peptide to high affinity ligand, a "library scan" strategy
    • Yeh R.H., Lee T.R., Lawrence D.S. From consensus sequence peptide to high affinity ligand, a "library scan" strategy. J. Biol. Chem. 276:2001;12235-12240.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12235-12240
    • Yeh, R.H.1    Lee, T.R.2    Lawrence, D.S.3
  • 38
    • 0024336003 scopus 로고
    • Fluorescent indicators for cytosolic calcium based on rhodamine and fluorescein chromophores
    • Minta A., Kao J.P., Tsien R.Y. Fluorescent indicators for cytosolic calcium based on rhodamine and fluorescein chromophores. J. Biol. Chem. 264:1989;8171-8178.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8171-8178
    • Minta, A.1    Kao, J.P.2    Tsien, R.Y.3
  • 40
    • 0032925541 scopus 로고    scopus 로고
    • Sequential PKC- and Cdc2-mediated phosphorylation events elicit zebrafish nuclear envelope disassembly
    • Collas P. Sequential PKC- and Cdc2-mediated phosphorylation events elicit zebrafish nuclear envelope disassembly. J. Cell. Sci. 112:1999;977-987.
    • (1999) J. Cell. Sci. , vol.112 , pp. 977-987
    • Collas, P.1
  • 41
    • 0032812633 scopus 로고    scopus 로고
    • Protein kinase C-theta is specifically activated in murine erythroleukaemia cells during mitosis
    • Passalacqua M., Patrone M., Sparatore B., Pedrazzi M., Melloni E., Pontremoli S. Protein kinase C-theta is specifically activated in murine erythroleukaemia cells during mitosis. FEBS Lett. 453:1999;249-253.
    • (1999) FEBS Lett. , vol.453 , pp. 249-253
    • Passalacqua, M.1    Patrone, M.2    Sparatore, B.3    Pedrazzi, M.4    Melloni, E.5    Pontremoli, S.6
  • 42
    • 0029871758 scopus 로고    scopus 로고
    • Mitosis-specific phosphorylation of vimentin by protein kinase C coupled with reorganization of intracellular membranes
    • Takai Y., Ogawara M., Tomono Y., Moritoh C., Imajoh-Ohmi S., Tsutsumi O., Taketani Y., Inagaki M. Mitosis-specific phosphorylation of vimentin by protein kinase C coupled with reorganization of intracellular membranes. J. Cell Biol. 133:1996;141-149.
    • (1996) J. Cell Biol. , vol.133 , pp. 141-149
    • Takai, Y.1    Ogawara, M.2    Tomono, Y.3    Moritoh, C.4    Imajoh-Ohmi, S.5    Tsutsumi, O.6    Taketani, Y.7    Inagaki, M.8
  • 43
    • 0035184911 scopus 로고    scopus 로고
    • Protein kinase C mediates phosphorylation of the regulatory light chain of myosin-II during mitosis
    • Varlamova O., Spektor A., Bresnick A.R. Protein kinase C mediates phosphorylation of the regulatory light chain of myosin-II during mitosis. J. Muscle Res. Cell Motil. 22:2001;243-250.
    • (2001) J. Muscle Res. Cell Motil. , vol.22 , pp. 243-250
    • Varlamova, O.1    Spektor, A.2    Bresnick, A.R.3
  • 44
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies S.P., Reddy H., Caivano M., Cohen P. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. 351:2000;95-105.
    • (2000) Biochem. J. , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 45
    • 12044256353 scopus 로고
    • The cAMP-dependent protein kinase discriminates between prochiral hydroxyl groups
    • Kwon Y.G., Srinivasan J., Mendelow M., Pluskey S., Lawrence D.S. The cAMP-dependent protein kinase discriminates between prochiral hydroxyl groups. J. Am. Chem. Soc. 115:1993;7527-7528.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 7527-7528
    • Kwon, Y.G.1    Srinivasan, J.2    Mendelow, M.3    Pluskey, S.4    Lawrence, D.S.5
  • 46
    • 0028344567 scopus 로고
    • Phenol kinase activity of the serine/threonine-specific cAMP-dependent protein kinase: Steric and electronic effects
    • Lee T.R., Niu J., Lawrence D.S. Phenol kinase activity of the serine/threonine-specific cAMP-dependent protein kinase: steric and electronic effects. Biochemistry. 33:1994;4245-4250.
    • (1994) Biochemistry , vol.33 , pp. 4245-4250
    • Lee, T.R.1    Niu, J.2    Lawrence, D.S.3
  • 47
    • 0000652747 scopus 로고
    • Molecular basis for the substrate specificity of a serine/threonine- specific protein kinase
    • Lee T.R., Mendelow M., Srinivasan J., Kwon Y.G., Lawrence D.S. Molecular basis for the substrate specificity of a serine/threonine-specific protein kinase. J. Am. Chem. Soc. 115:1994;9888-9891.
    • (1994) J. Am. Chem. Soc. , vol.115 , pp. 9888-9891
    • Lee, T.R.1    Mendelow, M.2    Srinivasan, J.3    Kwon, Y.G.4    Lawrence, D.S.5


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