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Volumn 46, Issue 10, 2007, Pages 2655-2673

Chemical genetics approach to identify peptide ligands that selectively stimulate DAPK-1 kinase activity

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL GENETICS; DAPK-1 KINASE; PEPTIDE LIGANDS;

EID: 33947208878     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061562j     Document Type: Article
Times cited : (13)

References (47)
  • 1
    • 33745726644 scopus 로고    scopus 로고
    • Chemical genetics
    • Walsh, D. P., and Chang, Y. T. (2006) Chemical genetics, Chem. Rev. 106, 2476-2530.
    • (2006) Chem. Rev , vol.106 , pp. 2476-2530
    • Walsh, D.P.1    Chang, Y.T.2
  • 2
    • 0028331587 scopus 로고
    • Farnesyltransferase inhibitors: Ras research yields a potential cancer therapeutic
    • Gibbs, J. B., Oliff, A., and Kohl, N. E. (1994) Farnesyltransferase inhibitors: Ras research yields a potential cancer therapeutic. Cell 77, 175-178.
    • (1994) Cell , vol.77 , pp. 175-178
    • Gibbs, J.B.1    Oliff, A.2    Kohl, N.E.3
  • 3
    • 0031025385 scopus 로고    scopus 로고
    • Cell-cycle arrest and inhibition of Cdk4 activity by small peptides based on the carboxy-terminal domain of p21WAF1
    • Ball, K. L., Lain, S., Fahraeus, R., Smythe, C., and Lane, D. P. (1997) Cell-cycle arrest and inhibition of Cdk4 activity by small peptides based on the carboxy-terminal domain of p21WAF1, Curr. Biol. 7, 71-80.
    • (1997) Curr. Biol , vol.7 , pp. 71-80
    • Ball, K.L.1    Lain, S.2    Fahraeus, R.3    Smythe, C.4    Lane, D.P.5
  • 4
    • 0029177397 scopus 로고    scopus 로고
    • Inhibition of pRb phosphorylation and cell-cycle progression by a 20-residue peptide derived from p16CDKN2/ 1NK4A
    • Fahraeus, R., Paramio, J. M., Ball, K. L., Lain, S., and Lane, D. P. (1996) Inhibition of pRb phosphorylation and cell-cycle progression by a 20-residue peptide derived from p16CDKN2/ 1NK4A. Curr. Biol. 6, 84-91.
    • (1996) Curr. Biol , vol.6 , pp. 84-91
    • Fahraeus, R.1    Paramio, J.M.2    Ball, K.L.3    Lain, S.4    Lane, D.P.5
  • 5
    • 0031282325 scopus 로고    scopus 로고
    • Design of a synthetic Mdm2-binding mini protein that activates the p53 response in vivo
    • Bottger, A., Bouger, V., Sparks, A., Liu, W. L., Howard, S. F., and Lane, D. P. (1997) Design of a synthetic Mdm2-binding mini protein that activates the p53 response in vivo. Curr. Biol. 7, 860-869.
    • (1997) Curr. Biol , vol.7 , pp. 860-869
    • Bottger, A.1    Bouger, V.2    Sparks, A.3    Liu, W.L.4    Howard, S.F.5    Lane, D.P.6
  • 7
    • 33745949757 scopus 로고    scopus 로고
    • Dual-site regulation of MDM2 E3-ubiquitin ligase activity
    • Wallace, M., Worrall, E., Pettersson, S., Hupp, T. R., and Ball, K. L. (2006) Dual-site regulation of MDM2 E3-ubiquitin ligase activity, Mol. Cell 23, 251-263.
    • (2006) Mol. Cell , vol.23 , pp. 251-263
    • Wallace, M.1    Worrall, E.2    Pettersson, S.3    Hupp, T.R.4    Ball, K.L.5
  • 8
    • 0037954572 scopus 로고    scopus 로고
    • Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions
    • Biondi, R. M., and Nebreda, A. R. (2003) Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions, Biochem. J. 372, 1-13.
    • (2003) Biochem. J , vol.372 , pp. 1-13
    • Biondi, R.M.1    Nebreda, A.R.2
  • 9
    • 0042854721 scopus 로고    scopus 로고
    • Allosteric effects mediate CHK2 phosphorylation of the p53 transactivation domain,
    • 4
    • Craig, A., Scott, M., Burch, L., Smith, G., Ball, K., and Hupp, T. (2003) Allosteric effects mediate CHK2 phosphorylation of the p53 transactivation domain, EMBO Rep. 4, 787-792.
    • (2003) EMBO Rep , pp. 787-792
    • Craig, A.1    Scott, M.2    Burch, L.3    Smith, G.4    Ball, K.5    Hupp, T.6
  • 10
    • 2942740790 scopus 로고    scopus 로고
    • DAP-kinase-mediated morphological changes are localization dependent and involve myosin-II phosphorylation
    • Bialik, S., Bresnick, A. R., and Kimchi, A. (2004) DAP-kinase-mediated morphological changes are localization dependent and involve myosin-II phosphorylation. Cell Death Differ. 11, 631-644.
    • (2004) Cell Death Differ , vol.11 , pp. 631-644
    • Bialik, S.1    Bresnick, A.R.2    Kimchi, A.3
  • 11
    • 0035914415 scopus 로고    scopus 로고
    • A protein kinase associated with apoptosis and tumor suppression: Structure, activity, and discovery of peptide substrates
    • Velentza, A. V., Schumacher, A. M., Weiss, C., Egli, M., and Watterson, D. M. (2001) A protein kinase associated with apoptosis and tumor suppression: structure, activity, and discovery of peptide substrates. J. Biol. Chem. 276, 38956-38965.
    • (2001) J. Biol. Chem , vol.276 , pp. 38956-38965
    • Velentza, A.V.1    Schumacher, A.M.2    Weiss, C.3    Egli, M.4    Watterson, D.M.5
  • 12
    • 0034810794 scopus 로고    scopus 로고
    • Crystal structures of the catalytic domain of human protein kinase associated with apoptosis and tumor suppression
    • Tereshko, V., Teplova, M., Brunzelle, J., Watterson, D. M., and Egli, M. (2001) Crystal structures of the catalytic domain of human protein kinase associated with apoptosis and tumor suppression. Nat. struct. Biol. 8, 899-907.
    • (2001) Nat. struct. Biol , vol.8 , pp. 899-907
    • Tereshko, V.1    Teplova, M.2    Brunzelle, J.3    Watterson, D.M.4    Egli, M.5
  • 13
    • 0035990917 scopus 로고    scopus 로고
    • Structure, activity, regulation, and inhibitor discovery for a protein kinase associated with apoptosis and neuronal death
    • Velentza, A. V., Schumacher, A. M., and Watterson, D. M. (2002) Structure, activity, regulation, and inhibitor discovery for a protein kinase associated with apoptosis and neuronal death. Pharmacol. Ther. 93, 217-224.
    • (2002) Pharmacol. Ther , vol.93 , pp. 217-224
    • Velentza, A.V.1    Schumacher, A.M.2    Watterson, D.M.3
  • 14
    • 0036156206 scopus 로고    scopus 로고
    • DAP kinase activity is critical for C(2)-ceramide-induced apoptosis in PC12 cells
    • Yamamoto, M., Hioki, T., Ishii, T., Nakajimu-Iijima, S., and Uchino, S. (2002) DAP kinase activity is critical for C(2)-ceramide-induced apoptosis in PC12 cells, Eur. J. Biochem. 269, 139-147.
    • (2002) Eur. J. Biochem , vol.269 , pp. 139-147
    • Yamamoto, M.1    Hioki, T.2    Ishii, T.3    Nakajimu-Iijima, S.4    Uchino, S.5
  • 15
    • 29644433255 scopus 로고    scopus 로고
    • Death-associated protein kinase is activated by dephosphorylation in response to cerebral ischemia
    • Shamloo, M., Soriano, L., Wieloch, T., Nikolich, K., Urfer, R., and Oksenberg, D. (2005) Death-associated protein kinase is activated by dephosphorylation in response to cerebral ischemia. J. Biol. Chem. 280, 42290-42299.
    • (2005) J. Biol. Chem , vol.280 , pp. 42290-42299
    • Shamloo, M.1    Soriano, L.2    Wieloch, T.3    Nikolich, K.4    Urfer, R.5    Oksenberg, D.6
  • 17
    • 0036460487 scopus 로고    scopus 로고
    • Immune-related mechanisms participating in resistance and susceptibility to glutamate toxicity
    • Schori, H., Yoles, E., Wheeler, L. A., Raveh, T., Kimchi, A., and Schwartz, M. (2002) Immune-related mechanisms participating in resistance and susceptibility to glutamate toxicity, Eur. J. Neurosci. 16, 557-564.
    • (2002) Eur. J. Neurosci , vol.16 , pp. 557-564
    • Schori, H.1    Yoles, E.2    Wheeler, L.A.3    Raveh, T.4    Kimchi, A.5    Schwartz, M.6
  • 18
    • 0037127269 scopus 로고    scopus 로고
    • Death-associated protein (DAP) kinase plays a central role in ceramide-induced apoptosis in cultured hippocampal neurons
    • Pelled, D., Raveh, T., Riebeling, C., Fridkin, M., Berissi, H., Futerman, A. H. and Kimchi, A. (2002) Death-associated protein (DAP) kinase plays a central role in ceramide-induced apoptosis in cultured hippocampal neurons, J. Biol. Chem. 277, 1957-1961.
    • (2002) J. Biol. Chem , vol.277 , pp. 1957-1961
    • Pelled, D.1    Raveh, T.2    Riebeling, C.3    Fridkin, M.4    Berissi, H.5    Futerman, A.H.6    Kimchi, A.7
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 21
    • 0037121923 scopus 로고    scopus 로고
    • PDK1-dependent activation of atypical PKC leads to degradation of the p21 tumour modifier protein
    • Scott, M. T., Ingram, A., and Ball, K. L. (2002) PDK1-dependent activation of atypical PKC leads to degradation of the p21 tumour modifier protein. EMBO J. 21, 6771-6780.
    • (2002) EMBO J , vol.21 , pp. 6771-6780
    • Scott, M.T.1    Ingram, A.2    Ball, K.L.3
  • 22
    • 1442277686 scopus 로고    scopus 로고
    • Phage-peptide display identifies the interferon-responsive, death-activated protein kinase family as a novel modifier of MDM2 and p21WAF1
    • Burch, L. R., Scott, M., Pohler, E., Meek, D., and Hupp, T. (2004) Phage-peptide display identifies the interferon-responsive, death-activated protein kinase family as a novel modifier of MDM2 and p21WAF1. J. Mol. Biol. 337, 115-128.
    • (2004) J. Mol. Biol , vol.337 , pp. 115-128
    • Burch, L.R.1    Scott, M.2    Pohler, E.3    Meek, D.4    Hupp, T.5
  • 23
    • 0346121431 scopus 로고    scopus 로고
    • Uncoordinated regulation of stress fibers and focal adhesions by DAP kinase
    • Kuo, J. C., Lin, J. R., Staddon, J. M., Hosoya, H., and Chen, R. H. (2003) Uncoordinated regulation of stress fibers and focal adhesions by DAP kinase, J. Cell Sci. 116, 4777-4790.
    • (2003) J. Cell Sci , vol.116 , pp. 4777-4790
    • Kuo, J.C.1    Lin, J.R.2    Staddon, J.M.3    Hosoya, H.4    Chen, R.H.5
  • 24
    • 0035800862 scopus 로고    scopus 로고
    • Zipper-interacting protein kinase induces Ca(2+)-free smooth muscle contraction via myosin light chain phosphorylation
    • Niiro, N., and Ikebe, M. (2001) Zipper-interacting protein kinase induces Ca(2+)-free smooth muscle contraction via myosin light chain phosphorylation, J. Biol. Chem. 276, 29567-29574.
    • (2001) J. Biol. Chem , vol.276 , pp. 29567-29574
    • Niiro, N.1    Ikebe, M.2
  • 26
    • 0035092598 scopus 로고    scopus 로고
    • Inhibition of p53-dependent transcription by BOX-I phospho-peptide mimetics that bind to p300,
    • 2
    • Dornan, D., and Hupp, T. R. (2001) Inhibition of p53-dependent transcription by BOX-I phospho-peptide mimetics that bind to p300, EMBO Rep. 2, 139-144.
    • (2001) EMBO Rep , pp. 139-144
    • Dornan, D.1    Hupp, T.R.2
  • 27
    • 0031056002 scopus 로고    scopus 로고
    • DAP-kinase is a Ca2+/calmodulin-dependent, cytoskeletal-associated protein kinase, with cell death-inducing functions that depend on its catalytic activity
    • Cohen, O., Feinstein, E., and Kimchi, A. (1997) DAP-kinase is a Ca2+/calmodulin-dependent, cytoskeletal-associated protein kinase, with cell death-inducing functions that depend on its catalytic activity. EMBO J. 16, 998-1008.
    • (1997) EMBO J , vol.16 , pp. 998-1008
    • Cohen, O.1    Feinstein, E.2    Kimchi, A.3
  • 28
    • 0035861546 scopus 로고    scopus 로고
    • The pro-apoptotic function of death-associated protein kinase is controlled by a unique inhibitory autophosphorylation-based mechanism
    • Shohat, G., Spivak-Kroizman, T., Cohen, O., Bialik, S., Shani, G., Berrisi, H., Eisenstein, M., and Kimchi, A. (2001) The pro-apoptotic function of death-associated protein kinase is controlled by a unique inhibitory autophosphorylation-based mechanism. J. Biol. Chem. 276, 47460-47467.
    • (2001) J. Biol. Chem , vol.276 , pp. 47460-47467
    • Shohat, G.1    Spivak-Kroizman, T.2    Cohen, O.3    Bialik, S.4    Shani, G.5    Berrisi, H.6    Eisenstein, M.7    Kimchi, A.8
  • 30
    • 0034647433 scopus 로고    scopus 로고
    • The C-terminal regulatory domain of p53 contains a functional docking site for cyclin A
    • Luciani, M. G., Hutchins, J. R., Zheleva, D., and Hupp, T. R. (2000) The C-terminal regulatory domain of p53 contains a functional docking site for cyclin A, J. Mol. Biol. 300, 503-518.
    • (2000) J. Mol. Biol , vol.300 , pp. 503-518
    • Luciani, M.G.1    Hutchins, J.R.2    Zheleva, D.3    Hupp, T.R.4
  • 31
    • 0035150402 scopus 로고    scopus 로고
    • Rho-Rho-kinase pathway in smooth muscle contraction and cytoskeletal reorganization of non-muscle cells
    • Fukata, Y., Amano, M., and Kaibuchi, K. (2001) Rho-Rho-kinase pathway in smooth muscle contraction and cytoskeletal reorganization of non-muscle cells. Trends Pharmacol. Sci. 22, 32-39.
    • (2001) Trends Pharmacol. Sci , vol.22 , pp. 32-39
    • Fukata, Y.1    Amano, M.2    Kaibuchi, K.3
  • 33
    • 0037157872 scopus 로고    scopus 로고
    • Cytoplasmic p21(Cip1/WAF1) regulates neurite remodeling by inhibiting Rho-kinase activity
    • Tanaka, H., Yamashita, T., Asada, M., Mizutani, S., Yoshikawa, H., and Tohyama, M. (2002) Cytoplasmic p21(Cip1/WAF1) regulates neurite remodeling by inhibiting Rho-kinase activity, J. Cell Biol. 158, 321-329.
    • (2002) J. Cell Biol , vol.158 , pp. 321-329
    • Tanaka, H.1    Yamashita, T.2    Asada, M.3    Mizutani, S.4    Yoshikawa, H.5    Tohyama, M.6
  • 34
    • 1942466518 scopus 로고    scopus 로고
    • p27Kip1 modulates cell migration through the regulation of RhoA activation
    • Besson, A., Gurian-West, M., Schmidt, A., Hall, A., and Roberts, J. M. (2004) p27Kip1 modulates cell migration through the regulation of RhoA activation. Genes Dev. 18, 862-876.
    • (2004) Genes Dev , vol.18 , pp. 862-876
    • Besson, A.1    Gurian-West, M.2    Schmidt, A.3    Hall, A.4    Roberts, J.M.5
  • 35
    • 0032931786 scopus 로고    scopus 로고
    • ZIP kinase identified as a novel myosin regulatory light chain kinase in HeLa cells
    • Murata-Hori, M., Suizu, F., Iwasaki, T., Kikuchi, A., and Hosoya, H. (1999) ZIP kinase identified as a novel myosin regulatory light chain kinase in HeLa cells, FEBS Lett. 451, 81-84.
    • (1999) FEBS Lett , vol.451 , pp. 81-84
    • Murata-Hori, M.1    Suizu, F.2    Iwasaki, T.3    Kikuchi, A.4    Hosoya, H.5
  • 36
    • 32644448252 scopus 로고    scopus 로고
    • The tumor suppressor DAPK inhibits cell motility by blocking the integrin-mediated polarity pathway
    • Kuo, J. C., Wang, W. J., Yao, C. C., Wu, P. R., and Chen, R. H. (2006) The tumor suppressor DAPK inhibits cell motility by blocking the integrin-mediated polarity pathway, J. Cell Biol. 172, 619-31.
    • (2006) J. Cell Biol , vol.172 , pp. 619-631
    • Kuo, J.C.1    Wang, W.J.2    Yao, C.C.3    Wu, P.R.4    Chen, R.H.5
  • 37
    • 2142828492 scopus 로고    scopus 로고
    • ZIP kinase is responsible for the phosphorylation of myosin II and necessary for cell motility in mammalian fibroblasts
    • Komatsu, S., and Ikebe, M. (2004) ZIP kinase is responsible for the phosphorylation of myosin II and necessary for cell motility in mammalian fibroblasts, J. Cell Biol. 165, 243-254.
    • (2004) J. Cell Biol , vol.165 , pp. 243-254
    • Komatsu, S.1    Ikebe, M.2
  • 38
    • 0037078325 scopus 로고    scopus 로고
    • DAP-kinase induces apoptosis by suppressing integrin activity and disrupting matrix survival signals
    • Wang, W. J., Kuo, J. C., Yao, C. C., and Chen, R. H. (2002) DAP-kinase induces apoptosis by suppressing integrin activity and disrupting matrix survival signals, J. Cell Biol. 159, 169-179.
    • (2002) J. Cell Biol , vol.159 , pp. 169-179
    • Wang, W.J.1    Kuo, J.C.2    Yao, C.C.3    Chen, R.H.4
  • 39
    • 0034941567 scopus 로고    scopus 로고
    • Akt-dependent phosphorylation of p21-(Cip1) regulates PCNA binding and proliferation of endothelial cells
    • Rossig, L., Jadidi, A. S., Urbich, C., Badorff, C., Zeiher, A. M., and Dimmeler, S. (2001) Akt-dependent phosphorylation of p21-(Cip1) regulates PCNA binding and proliferation of endothelial cells, Mol. Cell. Biol. 21, 5644-5657.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 5644-5657
    • Rossig, L.1    Jadidi, A.S.2    Urbich, C.3    Badorff, C.4    Zeiher, A.M.5    Dimmeler, S.6
  • 40
    • 0035857044 scopus 로고    scopus 로고
    • HeLa ZIP kinase induces diphosphorylation of myosin II regulatory light chain and reorganization of actin filaments in nonmuscle cells
    • Murata-Hori, M., Fukuta, Y., Ueda, K., Iwasaki, T., and Hosoya, H. (2001) HeLa ZIP kinase induces diphosphorylation of myosin II regulatory light chain and reorganization of actin filaments in nonmuscle cells, Oncogene 20, 8175-8183.
    • (2001) Oncogene , vol.20 , pp. 8175-8183
    • Murata-Hori, M.1    Fukuta, Y.2    Ueda, K.3    Iwasaki, T.4    Hosoya, H.5
  • 41
    • 15744392181 scopus 로고    scopus 로고
    • Regulation of zipper-interacting protein kinase activity in vitro and in vivo by multisite phosphorylation
    • Graves, P. R., Winkfield, K. M., and Haystead, T. A. (2005) Regulation of zipper-interacting protein kinase activity in vitro and in vivo by multisite phosphorylation, J. Biol. Chem. 280, 9363-9374.
    • (2005) J. Biol. Chem , vol.280 , pp. 9363-9374
    • Graves, P.R.1    Winkfield, K.M.2    Haystead, T.A.3
  • 42
    • 4944255743 scopus 로고    scopus 로고
    • Post-translational modification of p53 in tumorigenesis
    • Bode, A. M., and Dong, Z. (2004) Post-translational modification of p53 in tumorigenesis, Nat. Rev. Cancer 4, 793-805.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 793-805
    • Bode, A.M.1    Dong, Z.2
  • 43
    • 0033429271 scopus 로고    scopus 로고
    • Dumaz, N., Milne, D. M., and Meek, D. W. (1999) Protein kinase CK1 is a p53-threonine 18 kinase which requires prior phosphorylation of serine 15, FEBS Lett. 463, 312-316.
    • Dumaz, N., Milne, D. M., and Meek, D. W. (1999) Protein kinase CK1 is a p53-threonine 18 kinase which requires prior phosphorylation of serine 15, FEBS Lett. 463, 312-316.
  • 44
    • 0038752083 scopus 로고    scopus 로고
    • Chk2 activates E2F-1 in response to DNA damage
    • Stevens, C., Smith, L., and La Thangue, N. B. (2003) Chk2 activates E2F-1 in response to DNA damage, Nat. Cell Biol. 5, 401-409.
    • (2003) Nat. Cell Biol , vol.5 , pp. 401-409
    • Stevens, C.1    Smith, L.2    La Thangue, N.B.3
  • 45
    • 0034738420 scopus 로고    scopus 로고
    • p21(WAF1/Cip1): More than a break to the cell cycle?
    • Dotto, G. P. (2000) p21(WAF1/Cip1): more than a break to the cell cycle? Biochim. Biophys. Acta 1471, M43-M56.
    • (2000) Biochim. Biophys. Acta , vol.1471
    • Dotto, G.P.1
  • 46
    • 0029662315 scopus 로고    scopus 로고
    • Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: Conformational disorder mediates binding diversity
    • Kriwacki, R. W., Hengst, L., Tennant, L., Reed, S. I., and Wright, P. E. (1996) Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity, Proc. Natl. Acad. Sci. U.S.A. 93, 11504-11509.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 11504-11509
    • Kriwacki, R.W.1    Hengst, L.2    Tennant, L.3    Reed, S.I.4    Wright, P.E.5


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