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Volumn 409, Issue 3, 2011, Pages 369-383

Structure of the dimeric autoinhibited conformation of DAPK2, a pro-apoptotic protein kinase

Author keywords

AMP PNP; bovine serum albumin; BSA; calmodulin; CaM; CaM dependent protein kinase; CaMK; DAPK; death associated protein kinase; denosine 5' (beta,gamma imido) triphosphate; EDTA; EMBL DESY; ESRF; ethylenediaminetetraacetic acid; European Molecular Biology Laboratory Deutsches Elektronen Synchrotron; European Synchrotron Radiation Facility; MLCK; myosin light chain kinase; PhK; phosphorylase kinase; SAXS; small angle X ray scattering; ZIPK; zipper interacting protein kinase

Indexed keywords

DEATH ASSOCIATED PROTEIN KINASE; DEATH ASSOCIATED PROTEIN KINASE 1; DEATH ASSOCIATED PROTEIN KINASE 2; UNCLASSIFIED DRUG;

EID: 79956134440     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.03.065     Document Type: Article
Times cited : (30)

References (56)
  • 1
    • 0037020686 scopus 로고    scopus 로고
    • The DAP-kinase family of proteins: Study of a novel group of calcium-regulated death-promoting kinases
    • DOI 10.1016/S1570-9639(02)00443-0, PII S1570963902004430
    • Shohat G., Shani G., Eisenstein M., and Kimchi A. The DAP-kinase family of proteins: study of a novel group of calcium-regulated death-promoting kinases Biochim. Biophys. Acta 1600 2002 45 50 (Pubitemid 38224397)
    • (2002) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1600 , Issue.1-2 , pp. 45-50
    • Shohat, G.1    Shani, G.2    Eisenstein, M.3    Kimchi, A.4
  • 2
    • 0031056002 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent, cytoskeletal-associated protein kinase, with cell death-inducing functions that depend on its catalytic activity
    • DOI 10.1093/emboj/16.5.998
    • 2+/calmodulin-dependent, cytoskeletal-associated protein kinase, with cell death-inducing functions that depend on its catalytic activity EMBO J. 16 1997 998 1008 (Pubitemid 27113179)
    • (1997) EMBO Journal , vol.16 , Issue.5 , pp. 998-1008
    • Cohen, O.1    Feinstein, E.2    Kimchi, A.3
  • 3
    • 0033960235 scopus 로고    scopus 로고
    • Death-associated protein kinase-related protein 1, a novel serine/threonine kinase involved in apoptosis
    • DOI 10.1128/MCB.20.3.1044-1054.2000
    • Inbal B., Shani G., Cohen O., Kissil J.L., and Kimchi A. Death-associated protein kinase-related protein 1, a novel serine/threonine kinase involved in apoptosis Mol. Cell. Biol. 20 2000 1044 1054 (Pubitemid 30044241)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.3 , pp. 1044-1054
    • Inbal, B.1    Shani, G.2    Cohen, O.3    Kissil, J.L.4    Kimchi, A.5
  • 4
    • 0033542380 scopus 로고    scopus 로고
    • Death-associated protein kinase 2 is a new calcium/calmodulin-dependent protein kinase that signals apoptosis through its catalytic activity
    • DOI 10.1038/sj.onc.1202701
    • Kawai T., Nomura F., Hoshino K., Copeland N.G., Gilbert D.J., Jenkins N.A., and Akira S. Death-associated protein kinase 2 is a new calcium/calmodulin-dependent protein kinase that signals apoptosis through its catalytic activity Oncogene 18 1999 3471 3480 (Pubitemid 29317342)
    • (1999) Oncogene , vol.18 , Issue.23 , pp. 3471-3480
    • Kawai, T.1    Nomura, F.2    Hoshino, K.3    Copeland, N.G.4    Gilbert, D.J.5    Jenkins, N.A.6    Akira, S.7
  • 5
    • 0035283099 scopus 로고    scopus 로고
    • Autophosphorylation restrains the apoptotic activity of DRP-1 kinase by controlling dimerization and calmodulin binding
    • DOI 10.1093/emboj/20.5.1099
    • Shani G., Henis-Korenblit S., Jona G., Gileadi O., Eisenstein M., and Ziv T. Autophosphorylation restrains the apoptotic activity of DRP-1 kinase by controlling dimerization and calmodulin binding EMBO J. 20 2001 1099 1113 (Pubitemid 32186800)
    • (2001) EMBO Journal , vol.20 , Issue.5 , pp. 1099-1113
    • Shani, G.1    Henis-Korenblit, S.2    Jona, G.3    Gileadi, O.4    Eisenstein, M.5    Ziv, T.6    Admon, A.7    Kimchi, A.8
  • 6
    • 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., and Berrisi H. The pro-apoptotic function of death-associated protein kinase is controlled by a unique inhibitory autophosphorylation-based mechanism J. Biol. Chem. 276 2001 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
  • 7
    • 0037193474 scopus 로고    scopus 로고
    • DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death
    • DOI 10.1083/jcb.200109094
    • Inbal B., Bialik S., Sabanay I., Shani G., and Kimchi A. DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death J. Cell Biol. 157 2002 455 468 (Pubitemid 34839809)
    • (2002) Journal of Cell Biology , vol.157 , Issue.3 , pp. 455-468
    • Inbal, B.1    Bialik, S.2    Sabanay, I.3    Shani, G.4    Kimchi, A.5
  • 8
    • 50949103721 scopus 로고    scopus 로고
    • Attenuation of EPO-dependent erythroblast formation by death-associated protein kinase-2
    • Fang J., Menon M., Zhang D., Torbett B., Oxburgh L., and Tschan M. Attenuation of EPO-dependent erythroblast formation by death-associated protein kinase-2 Blood 112 2008 886 890
    • (2008) Blood , vol.112 , pp. 886-890
    • Fang, J.1    Menon, M.2    Zhang, D.3    Torbett, B.4    Oxburgh, L.5    Tschan, M.6
  • 12
    • 67651152680 scopus 로고    scopus 로고
    • Targeted restoration of down-regulated DAPK2 tumor suppressor activity induces apoptosis in Hodgkin lymphoma cells
    • Tur M.K., Neef I., Jost E., Galm O., Jager G., and Stocker M. Targeted restoration of down-regulated DAPK2 tumor suppressor activity induces apoptosis in Hodgkin lymphoma cells J. Immunother. 32 2009 431 441
    • (2009) J. Immunother. , vol.32 , pp. 431-441
    • Tur, M.K.1    Neef, I.2    Jost, E.3    Galm, O.4    Jager, G.5    Stocker, M.6
  • 13
    • 3042515471 scopus 로고    scopus 로고
    • DAP-kinase as a target for drug design in cancer and diseases associated with accelerated cell death
    • DOI 10.1016/j.semcancer.2004.04.008, PII S1044579X04000252
    • Bialik S., and Kimchi A. DAP-kinase as a target for drug design in cancer and diseases associated with accelerated cell death Semin. Cancer Biol. 14 2004 283 294 (Pubitemid 38824589)
    • (2004) Seminars in Cancer Biology , vol.14 , Issue.4 , pp. 283-294
    • Bialik, S.1    Kimchi, A.2
  • 16
    • 0035990917 scopus 로고    scopus 로고
    • Structure, activity, regulation, and inhibitor discovery for a protein kinase associated with apoptosis and neuronal death
    • DOI 10.1016/S0163-7258(02)00190-0, PII S0163725802001900
    • Velentza A.V., Schumacher A.M., and Watterson D.M. Structure, activity, regulation, and inhibitor discovery for a protein kinase associated with apoptosis and neuronal death Pharmacol. Ther. 93 2002 217 224 (Pubitemid 34615562)
    • (2002) Pharmacology and Therapeutics , vol.93 , Issue.2-3 , pp. 217-224
    • Velentza, A.V.1    Schumacher, A.M.2    Watterson D.Martin3
  • 17
    • 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. A protein kinase associated with apoptosis and tumor suppression: structure, activity, and discovery of peptide substrates J. Biol. Chem. 276 2001 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
  • 18
    • 77950037970 scopus 로고    scopus 로고
    • Structure-activity relationship of novel DAPK inhibitors identified by structure-based virtual screening
    • Okamoto M., Takayama K., Shimizu T., Muroya A., and Furuya T. Structure-activity relationship of novel DAPK inhibitors identified by structure-based virtual screening Bioorg. Med. Chem. 18 2010 2728 2734
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 2728-2734
    • Okamoto, M.1    Takayama, K.2    Shimizu, T.3    Muroya, A.4    Furuya, T.5
  • 19
    • 70949096942 scopus 로고    scopus 로고
    • Identification of death-associated protein kinases inhibitors using structure-based virtual screening
    • Okamoto M., Takayama K., Shimizu T., Ishida K., Takahashi O., and Furuya T. Identification of death-associated protein kinases inhibitors using structure-based virtual screening J. Med. Chem. 52 2009 7323 7327
    • (2009) J. Med. Chem. , vol.52 , pp. 7323-7327
    • Okamoto, M.1    Takayama, K.2    Shimizu, T.3    Ishida, K.4    Takahashi, O.5    Furuya, T.6
  • 21
    • 0034810794 scopus 로고    scopus 로고
    • Crystal structures of the catalytic domain of human protein kinase associated with apoptosis and tumor suppression
    • DOI 10.1038/nsb1001-899
    • Tereshko V., Teplova M., Brunzelle J., Watterson D.M., and Egli M. Crystal structures of the catalytic domain of human protein kinase associated with apoptosis and tumor suppression Nat. Struct. Biol. 8 2001 899 907 (Pubitemid 32923612)
    • (2001) Nature Structural Biology , vol.8 , Issue.10 , pp. 899-907
    • Tereshko, V.1    Teplova, M.2    Brunzelle, J.3    Watterson, D.M.4    Egli, M.5
  • 22
    • 77951648455 scopus 로고    scopus 로고
    • Molecular basis of the death-associated protein kinase-calcium/calmodulin regulator complex
    • de Diego I., Kuper J., Bakalova N., Kursula P., and Wilmanns M. Molecular basis of the death-associated protein kinase-calcium/calmodulin regulator complex Sci. Signal. 3 2010 ra6
    • (2010) Sci. Signal. , vol.3 , pp. 6
    • De Diego, I.1    Kuper, J.2    Bakalova, N.3    Kursula, P.4    Wilmanns, M.5
  • 23
    • 0029871290 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of calcium/calmodulin-dependent protein kinase I
    • DOI 10.1016/S0092-8674(00)81066-1
    • Goldberg J., Nairn A.C., and Kuriyan J. Structural basis for the autoinhibition of calcium/calmodulin-dependent protein kinase I Cell 84 1996 875 887 (Pubitemid 26106857)
    • (1996) Cell , vol.84 , Issue.6 , pp. 875-887
    • Goldberg, J.1    Nairn, A.C.2    Kuriyan, J.3
  • 24
    • 28344445756 scopus 로고    scopus 로고
    • Structure of the autoinhibited kinase domain of CaMKII and SAXS analysis of the holoenzyme
    • DOI 10.1016/j.cell.2005.10.029, PII S0092867405011736
    • Rosenberg O.S., Deindl S., Sung R.J., Nairn A.C., and Kuriyan J. Structure of the autoinhibited kinase domain of CaMKII and SAXS analysis of the holoenzyme Cell 123 2005 849 860 (Pubitemid 41721031)
    • (2005) Cell , vol.123 , Issue.5 , pp. 849-860
    • Rosenberg, O.S.1    Deindl, S.2    Sung, R.-J.3    Nairn, A.C.4    Kuriyan, J.5
  • 27
  • 28
    • 0028287635 scopus 로고
    • Insights into autoregulation from the crystal structure of twitchin kinase
    • DOI 10.1038/369581a0
    • Hu S.H., Parker M.W., Lei J.Y., Wilce M.C., Benian G.M., and Kemp B.E. Insights into autoregulation from the crystal structure of twitchin kinase Nature 369 1994 581 584 (Pubitemid 24192530)
    • (1994) Nature , vol.369 , Issue.6481 , pp. 581-584
    • Hu, S.-H.1    Parker, M.W.2    Lei, J.Y.3    Wilce, M.C.J.4    Benian, G.M.5    Kemp, B.E.6
  • 29
    • 0034697165 scopus 로고    scopus 로고
    • 2+/calmodulin binding and activation of myosin light chain kinase
    • DOI 10.1016/S0014-5793(00)01434-4, PII S0014579300014344
    • 2+/calmodulin binding and activation of myosin light chain kinase FEBS Lett. 472 2000 148 152 (Pubitemid 30224604)
    • (2000) FEBS Letters , vol.472 , Issue.1 , pp. 148-152
    • Padre, R.C.1    Stull, J.T.2
  • 30
    • 0028050528 scopus 로고
    • Mutational analysis of secondary structure in the autoinhibitory and autophosphorylation domains of calmodulin kinase II
    • Mukherji S., Brickey D.A., and Soderling T.R. Mutational analysis of secondary structure in the autoinhibitory and autophosphorylation domains of calmodulin kinase II J. Biol. Chem. 269 1994 20733 20738 (Pubitemid 24260488)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.32 , pp. 20733-20738
    • Mukherji, S.1    Brickey, D.A.2    Soderling, T.R.3
  • 31
    • 0029010470 scopus 로고
    • Pseudosubstrate sequence may not be critical for autoinhibition of smooth muscle myosin light chain kinase
    • Tanaka M., Ikebe R., Matsuura M., and Ikebe M. Pseudosubstrate sequence may not be critical for autoinhibition of smooth muscle myosin light chain kinase EMBO J. 14 1995 2839 2846
    • (1995) EMBO J. , vol.14 , pp. 2839-2846
    • Tanaka, M.1    Ikebe, R.2    Matsuura, M.3    Ikebe, M.4
  • 32
    • 0027057114 scopus 로고
    • Identification of basic residues involved in activation and calmodulin binding of rabbit smooth muscle myosin light chain kinase
    • Fitzsimons D.P., Herring B.P., Stull J.T., and Gallagher P.J. Identification of basic residues involved in activation and calmodulin binding of rabbit smooth muscle myosin light chain kinase J. Biol. Chem. 267 1992 23903 23909 (Pubitemid 23088202)
    • (1992) Journal of Biological Chemistry , vol.267 , Issue.33 , pp. 23903-23909
    • Fitzsimons, D.P.1    Herring, B.P.2    Stull, J.T.3    Gallagher, P.J.4
  • 33
    • 0030812650 scopus 로고    scopus 로고
    • The crystal structure of a phosphorylase kinase peptide substrate complex: Kinase substrate recognition
    • Lowe E.D., Noble M.E., Skamnaki V.T., Oikonomakos N.G., Owen D.J., and Johnson L.N. The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition EMBO J. 16 1997 6646 6658 (Pubitemid 27503477)
    • (1997) EMBO Journal , vol.16 , Issue.22 , pp. 6646-6658
    • Lowe, E.D.1    Noble, M.E.M.2    Skamnaki, V.T.3    Oikonomakos, N.G.4    Owen, D.J.5    Johnson, L.N.6
  • 35
    • 4544374632 scopus 로고    scopus 로고
    • Death-associated protein kinase phosphorylates ZIP kinase, forming a unique kinase hierarchy to activate its cell death functions
    • DOI 10.1128/MCB.24.19.8611-8626.2004
    • Shani G., Marash L., Gozuacik D., Bialik S., Teitelbaum L., Shohat G., and Kimchi A. Death-associated protein kinase phosphorylates ZIP kinase, forming a unique kinase hierarchy to activate its cell death functions Mol. Cell. Biol. 24 2004 8611 8626 (Pubitemid 39245081)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.19 , pp. 8611-8626
    • Shani, G.1    Marash, L.2    Gozuacik, D.3    Bialik, S.4    Teitelbaum, L.5    Shohat, G.6    Kimchi, A.7
  • 36
    • 78649798970 scopus 로고    scopus 로고
    • Homodimerization of the death-associated protein kinase catalytic domain: Development of a new small molecule fluorescent reporter
    • Zimmermann M., Atmanene C., Xu Q., Fouillen L., Van Dorsselaer A., and Bonnet D. Homodimerization of the death-associated protein kinase catalytic domain: development of a new small molecule fluorescent reporter PLoS One 5 2010 e14120
    • (2010) PLoS One , vol.5 , pp. 14120
    • Zimmermann, M.1    Atmanene, C.2    Xu, Q.3    Fouillen, L.4    Van Dorsselaer, A.5    Bonnet, D.6
  • 37
    • 1042275583 scopus 로고    scopus 로고
    • A Dissection of Specific and Non-specific Protein-Protein Interfaces
    • DOI 10.1016/j.jmb.2003.12.073
    • Bahadur R.P., Chakrabarti P., Rodier F., and Janin J. A dissection of specific and non-specific protein-protein interfaces J. Mol. Biol. 336 2004 943 955 (Pubitemid 38201541)
    • (2004) Journal of Molecular Biology , vol.336 , Issue.4 , pp. 943-955
    • Bahadur, R.P.1    Chakrabarti, P.2    Rodier, F.3    Janin, J.4
  • 38
    • 77949415443 scopus 로고    scopus 로고
    • Epigallocatechin-3-gallate induces cell death in acute myeloid leukaemia cells and supports all-trans retinoic acid-induced neutrophil differentiation via death-associated protein kinase 2
    • Britschgi A., Simon H.U., Tobler A., Fey M.F., and Tschan M.P. Epigallocatechin-3-gallate induces cell death in acute myeloid leukaemia cells and supports all-trans retinoic acid-induced neutrophil differentiation via death-associated protein kinase 2 Br. J. Haematol. 149 2010 55 64
    • (2010) Br. J. Haematol. , vol.149 , pp. 55-64
    • Britschgi, A.1    Simon, H.U.2    Tobler, A.3    Fey, M.F.4    Tschan, M.P.5
  • 40
    • 67849117178 scopus 로고    scopus 로고
    • Accurate solution structures of proteins from X-ray data and a minimal set of NMR data: Calmodulin-peptide complexes as examples
    • Bertini I., Kursula P., Luchinat C., Parigi G., Vahokoski J., Wilmanns M., and Yuan J. Accurate solution structures of proteins from X-ray data and a minimal set of NMR data: calmodulin-peptide complexes as examples J. Am. Chem. Soc. 131 2009 5134 5144
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 5134-5144
    • Bertini, I.1    Kursula, P.2    Luchinat, C.3    Parigi, G.4    Vahokoski, J.5    Wilmanns, M.6    Yuan, J.7
  • 42
    • 77956415702 scopus 로고    scopus 로고
    • Structural and functional characterization of human peripheral nervous system myelin protein P2
    • Majava V., Polverini E., Mazzini A., Nanekar R., Knoll W., and Peters J. Structural and functional characterization of human peripheral nervous system myelin protein P2 PLoS One 5 2010 e10300
    • (2010) PLoS One , vol.5 , pp. 10300
    • Majava, V.1    Polverini, E.2    Mazzini, A.3    Nanekar, R.4    Knoll, W.5    Peters, J.6
  • 43
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier F.W. Protein production by auto-induction in high density shaking cultures Protein Expression Purif. 41 2005 207 234
    • (2005) Protein Expression Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 44
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants J. Appl. Crystallogr. 26 1993 795 800
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 45
    • 3442881027 scopus 로고    scopus 로고
    • XDSi: A graphical interface for the data processing program XDS
    • Kursula P. XDSi: a graphical interface for the data processing program XDS J. Appl. Crystallogr. 37 2004 347 348
    • (2004) J. Appl. Crystallogr. , vol.37 , pp. 347-348
    • Kursula, P.1
  • 51
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • DOI 10.1107/S0021889892001663
    • Svergun D.I. Determination of the regularization parameter in indirect-transform methods using perceptual criteria J. Appl. Crystallogr. 25 1992 495 503 (Pubitemid 23564996)
    • (1992) Journal of Applied Crystallography , vol.25 , Issue.PART 4 , pp. 495-503
    • Svergun, D.I.1
  • 52
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun D.I. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing Biophys. J. 76 1999 2879 2886 (Pubitemid 29269438)
    • (1999) Biophysical Journal , vol.76 , Issue.6 , pp. 2879-2886
    • Svergun, D.I.1
  • 53
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering
    • Franke D., and Svergun D.I. DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering J. Appl. Crystallogr. 42 2009 342 346
    • (2009) J. Appl. Crystallogr. , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 54
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from x-ray solution scattering
    • Svergun D.I., Petoukhov M.V., and Koch M.H. Determination of domain structure of proteins from X-ray solution scattering Biophys. J. 80 2001 2946 2953 (Pubitemid 32521666)
    • (2001) Biophysical Journal , vol.80 , Issue.6 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.J.3
  • 55
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • DOI 10.1107/S0021889800014126
    • Kozin M., and Svergun D.I. Automated matching of high- and low-resolution structural models J. Appl. Crystallogr. 34 2000 33 41 (Pubitemid 32151714)
    • (2001) Journal of Applied Crystallography , vol.34 , Issue.1 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 56
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small angle scattering
    • Volkov V.V., and Svergun D.I. Uniqueness of ab initio shape determination in small angle scattering J. Appl. Crystallogr. 36 2003 860 864
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2


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