메뉴 건너뛰기




Volumn 40, Issue 5, 2012, Pages 1052-1057

Biochemical and functional characterization of the ROC domain of DAPK establishes a new paradigm of GTP regulation in ROCO proteins

Author keywords

Autophagy; Autophosphorylation; Dapk (death associated protein kinase); Leucine rich repeat kinase 2 (lrrk2)

Indexed keywords

DEATH ASSOCIATED PROTEIN KINASE; GUANOSINE TRIPHOSPHATE; RAS PROTEIN; ROCO PROTEIN; UNCLASSIFIED DRUG;

EID: 84866649955     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20120155     Document Type: Review
Times cited : (15)

References (49)
  • 1
    • 51349153846 scopus 로고    scopus 로고
    • The Roco protein family: A functional perspective
    • Marin, I., van Egmond, W.N. and van Haastert, P.J. (2008) The Roco protein family: a functional perspective. FASEB J. 22, 3103-3110
    • (2008) FASEB J. , vol.22 , pp. 3103-3110
    • Marin, I.1    Van Egmond, W.N.2    Van Haastert, P.J.3
  • 2
    • 77951217470 scopus 로고    scopus 로고
    • Lethal weapons: DAP-kinase, autophagy and cell death
    • Bialik, S. and Kimchi, A. (2010) Lethal weapons: DAP-kinase, autophagy and cell death. Curr. Opin. Cell Biol. 22, 199-205
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 199-205
    • Bialik, S.1    Kimchi, A.2
  • 3
    • 32644448252 scopus 로고    scopus 로고
    • The tumor suppressor DAPK inhibits cell motility by blocking the integrin-mediated polarity pathway
    • Kuo, J., Wang, W., Yao, C., Wu, P. and Chen, R. (2006) The tumor suppressor DAPK inhibits cell motility by blocking the integrin-mediated polarity pathway. J. Cell Biol. 172, 619-631
    • (2006) J. Cell Biol. , vol.172 , pp. 619-631
    • Kuo, J.1    Wang, W.2    Yao, C.3    Wu, P.4    Chen, R.5
  • 4
    • 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
  • 5
    • 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
  • 6
    • 49149091747 scopus 로고    scopus 로고
    • The tumor suppressor death-associated protein kinase targets to TCR-stimulated NF-κB activation
    • Chuang, Y.T., Fang, L.W., Lin-Feng, M.H., Chen, R.H. and Lai, M.Z. (2008) The tumor suppressor death-associated protein kinase targets to TCR-stimulated NF-κB activation. J. Immunol. 180, 3238-3249
    • (2008) J. Immunol. , vol.180 , pp. 3238-3249
    • Chuang, Y.T.1    Fang, L.W.2    Lin-Feng, M.H.3    Chen, R.H.4    Lai, M.Z.5
  • 9
    • 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
  • 10
    • 61849102389 scopus 로고    scopus 로고
    • DAP-kinase-mediated phosphorylation on the BH3 domain of beclin 1 promotes dissociation of beclin 1 from Bcl-XL and induction of autophagy
    • Zalckvar, E., Berissi, H., Mizrachy, L., Idelchuk, Y., Koren, I., Eisenstein, M., Sabanay, H., Pinkas-Kramarski, R. and Kimchi, A. (2009) DAP-kinase-mediated phosphorylation on the BH3 domain of beclin 1 promotes dissociation of beclin 1 from Bcl-XL and induction of autophagy. EMBO Rep. 10, 285-292
    • (2009) EMBO Rep. , vol.10 , pp. 285-292
    • Zalckvar, E.1    Berissi, H.2    Mizrachy, L.3    Idelchuk, Y.4    Koren, I.5    Eisenstein, M.6    Sabanay, H.7    Pinkas-Kramarski, R.8    Kimchi, A.9
  • 11
    • 35548946698 scopus 로고    scopus 로고
    • DAP-kinase regulates JNK signaling by binding and activating protein kinase D under oxidative stress
    • Eisenberg-Lerner, A. and Kimchi, A. (2007) DAP-kinase regulates JNK signaling by binding and activating protein kinase D under oxidative stress. Cell Death Differ. 14, 1908-1915
    • (2007) Cell Death Differ. , vol.14 , pp. 1908-1915
    • Eisenberg-Lerner, A.1    Kimchi, A.2
  • 13
    • 33746359639 scopus 로고    scopus 로고
    • The death-associated protein kinases: Structure, function and beyond
    • Bialik, S. and Kimchi, A. (2006) The death-associated protein kinases: structure, function and beyond. Annu. Rev. Biochem. 75, 189-210
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 189-210
    • Bialik, S.1    Kimchi, A.2
  • 15
  • 16
    • 0031056002 scopus 로고    scopus 로고
    • 2+ /calmodulin-dependent, cytoskeletal-associated protein kinase, with cell death-inducing functions that depend on its catalytic activity
    • 2+ /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
  • 17
    • 33846818834 scopus 로고    scopus 로고
    • GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease
    • Ito, G., Okai, T., Fujino, G., Takeda, K., Ichijo, H., Katada, T. and Iwatsubo, T. (2007) GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease. Biochemistry 46, 1380-1388
    • (2007) Biochemistry , vol.46 , pp. 1380-1388
    • Ito, G.1    Okai, T.2    Fujino, G.3    Takeda, K.4    Ichijo, H.5    Katada, T.6    Iwatsubo, T.7
  • 18
    • 34548604567 scopus 로고    scopus 로고
    • The Parkinson's disease-associated protein, leucine-rich repeat kinase 2 (LRRK2), is an authentic GTPase that stimulates kinase activity
    • Guo, L., Gandhi, P.N., Wang, W., Petersen, R.B., Wilson-Delfosse, A.L. and Chen, S.G. (2007) The Parkinson's disease-associated protein, leucine-rich repeat kinase 2 (LRRK2), is an authentic GTPase that stimulates kinase activity. Exp. Cell Res. 313, 3658-3670
    • (2007) Exp. Cell Res. , vol.313 , pp. 3658-3670
    • Guo, L.1    Gandhi, P.N.2    Wang, W.3    Petersen, R.B.4    Wilson-Delfosse, A.L.5    Chen, S.G.6
  • 19
    • 32244443107 scopus 로고    scopus 로고
    • LRRK1 protein kinase activity is stimulated upon binding of GTP to its Roc domain
    • Korr, D., Toschi, L., Donner, P., Pohlenz, H.D., Kreft, B. and Weiss, B. (2006) LRRK1 protein kinase activity is stimulated upon binding of GTP to its Roc domain. Cell. Signalling 18, 910-920
    • (2006) Cell. Signalling , vol.18 , pp. 910-920
    • Korr, D.1    Toschi, L.2    Donner, P.3    Pohlenz, H.D.4    Kreft, B.5    Weiss, B.6
  • 20
    • 4544374632 scopus 로고    scopus 로고
    • Death-associated protein kinase phosphorylates ZIP kinase, forming a unique kinase hierarchy to activate its cell death functions
    • Shani, G., Marash, L., Gozuacik, D., Bialik, S., Teitelbaum, L., Shohat, G. and Kimchi, A. (2004) Death-associated protein kinase phosphorylates ZIP kinase, forming a unique kinase hierarchy to activate its cell death functions. Mol. Cell. Biol. 24, 8611-8626
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8611-8626
    • Shani, G.1    Marash, L.2    Gozuacik, D.3    Bialik, S.4    Teitelbaum, L.5    Shohat, G.6    Kimchi, A.7
  • 22
    • 73649097539 scopus 로고    scopus 로고
    • Death-associated protein kinase (DAPK) and signal transduction: Additional roles beyond cell death
    • Lin, Y., Hupp, T.R. and Stevens, C. (2010) Death-associated protein kinase (DAPK) and signal transduction: additional roles beyond cell death. FEBS J. 277, 48-57
    • (2010) FEBS J. , vol.277 , pp. 48-57
    • Lin, Y.1    Hupp, T.R.2    Stevens, C.3
  • 23
    • 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
  • 26
    • 77951615510 scopus 로고    scopus 로고
    • Protein phosphatase 2A (PP2A) holoenzymes regulate death-associated protein kinase (DAPK) in ceramide-induced anoikis
    • Widau, R.C., Jin, Y., Dixon, S.A., Wadzinski, B.E. and Gallagher, P.J. (2010) Protein phosphatase 2A (PP2A) holoenzymes regulate death-associated protein kinase (DAPK) in ceramide-induced anoikis. J. Biol. Chem. 285, 13827-13838
    • (2010) J. Biol. Chem. , vol.285 , pp. 13827-13838
    • Widau, R.C.1    Jin, Y.2    Dixon, S.A.3    Wadzinski, B.E.4    Gallagher, P.J.5
  • 27
    • 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. (2010) Molecular basis of the death-associated protein kinase-calcium/calmodulin regulator complex. Sci. Signaling 3, ra6
    • (2010) Sci. Signaling , vol.3
    • De Diego, I.1    Kuper, J.2    Bakalova, N.3    Kursula, P.4    Wilmanns, M.5
  • 29
    • 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
  • 30
    • 79956134440 scopus 로고    scopus 로고
    • Structure of the dimeric autoinhibited conformation of DAPK2, a pro-apoptotic protein kinase
    • Patel, A.K., Yadav, R.P., Majava, V., Kursula, I. and Kursula, P. (2011) Structure of the dimeric autoinhibited conformation of DAPK2, a pro-apoptotic protein kinase. J. Mol. Biol. 409, 369-383
    • (2011) J. Mol. Biol. , vol.409 , pp. 369-383
    • Patel, A.K.1    Yadav, R.P.2    Majava, V.3    Kursula, I.4    Kursula, P.5
  • 32
    • 70349929185 scopus 로고    scopus 로고
    • Homo- And heterodimerization of ROCO kinases: LRRK2 kinase inhibition by the LRRK2 ROCO fragment
    • Klein, C.L., Rovelli, G., Springer, W., Schall, C., Gasser, T. and Kahle, P.J. (2009) Homo- and heterodimerization of ROCO kinases: LRRK2 kinase inhibition by the LRRK2 ROCO fragment. J. Neurochem. 111, 703-715
    • (2009) J. Neurochem. , vol.111 , pp. 703-715
    • Klein, C.L.1    Rovelli, G.2    Springer, W.3    Schall, C.4    Gasser, T.5    Kahle, P.J.6
  • 33
    • 81555205691 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 (LRRK2) cellular biology: A review of recent advances in identifying physiological substrates and cellular functions
    • Drolet, R.E., Sanders, J.M. and Kern, J.T. (2011) Leucine-rich repeat kinase 2 (LRRK2) cellular biology: a review of recent advances in identifying physiological substrates and cellular functions. J. Neurogenet. 25, 140-151
    • (2011) J. Neurogenet. , vol.25 , pp. 140-151
    • Drolet, R.E.1    Sanders, J.M.2    Kern, J.T.3
  • 34
    • 0037829648 scopus 로고    scopus 로고
    • 2+-dependent phosphorylation of syntaxin-1A by the death-associated protein (DAP) kinase regulates its interaction with Munc18
    • 2+-dependent phosphorylation of syntaxin-1A by the death-associated protein (DAP) kinase regulates its interaction with Munc18. J. Biol. Chem. 278, 26265-26274
    • (2003) J. Biol. Chem. , vol.278 , pp. 26265-26274
    • Tian, J.H.1    Das, S.2    Sheng, Z.H.3
  • 40
    • 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
  • 41
    • 79957636562 scopus 로고    scopus 로고
    • On the road to leucine-rich repeat kinase 2 signalling: Evidence from cellular and in vivo studies
    • Daniels, V., Baekelandt, V. and Taymans, J.M. (2011) On the road to leucine-rich repeat kinase 2 signalling: evidence from cellular and in vivo studies. Neurosignals 19, 1-15
    • (2011) Neurosignals , vol.19 , pp. 1-15
    • Daniels, V.1    Baekelandt, V.2    Taymans, J.M.3
  • 42
    • 84861232484 scopus 로고    scopus 로고
    • Mechanisms of LRRK2-mediated neurodegeneration
    • Tsika, E. and Moore, D. (2012) Mechanisms of LRRK2-mediated neurodegeneration. Curr. Neurol. Neurosci. Rep. 12, 251-260
    • (2012) Curr. Neurol. Neurosci. Rep. , vol.12 , pp. 251-260
    • Tsika, E.1    Moore, D.2
  • 43
    • 36248956949 scopus 로고    scopus 로고
    • DAP kinase mediates the phosphorylation of tropomyosin-1 downstream of the ERK pathway, which regulates the formation of stress fibers in response to oxidative stress
    • Houle, F., Poirier, A., Dumaresq, J. and Huot, J. (2007) DAP kinase mediates the phosphorylation of tropomyosin-1 downstream of the ERK pathway, which regulates the formation of stress fibers in response to oxidative stress. J. Cell Sci. 120, 3666-3677
    • (2007) J. Cell Sci. , vol.120 , pp. 3666-3677
    • Houle, F.1    Poirier, A.2    Dumaresq, J.3    Huot, J.4
  • 46
    • 78650389179 scopus 로고    scopus 로고
    • LRRK2 kinase regulates synaptic morphology through distinct substrates at the presynaptic and postsynaptic compartments of the Drosophila neuromuscular junction
    • Lee, S., Liu, H.-P., Lin, W.-Y., Guo, H. and Lu, B. (2010) LRRK2 kinase regulates synaptic morphology through distinct substrates at the presynaptic and postsynaptic compartments of the Drosophila neuromuscular junction. J. Neurosci. 30, 16959-16969
    • (2010) J. Neurosci. , vol.30 , pp. 16959-16969
    • Lee, S.1    Liu, H.-P.2    Lin, W.-Y.3    Guo, H.4    Lu, B.5
  • 47
    • 43949145220 scopus 로고    scopus 로고
    • DAPK-1 binding to a linear peptide motif in MAP1B stimulates autophagy and membrane blebbing
    • Harrison, B., Kraus, M., Burch, L., Stevens, C., Craig, A., Gordon-Weeks, P. and Hupp, T.R. (2008) DAPK-1 binding to a linear peptide motif in MAP1B stimulates autophagy and membrane blebbing. J. Biol. Chem. 283, 9999-10014
    • (2008) J. Biol. Chem. , vol.283 , pp. 9999-10014
    • Harrison, B.1    Kraus, M.2    Burch, L.3    Stevens, C.4    Craig, A.5    Gordon-Weeks, P.6    Hupp, T.R.7
  • 48
    • 0037193474 scopus 로고    scopus 로고
    • DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death
    • Inbal, B., Bialik, S., Sabanay, I., Shani, G. and Kimchi, A. (2002) DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death. J. Cell Biol. 157, 455-468
    • (2002) J. Cell Biol. , vol.157 , pp. 455-468
    • Inbal, B.1    Bialik, S.2    Sabanay, I.3    Shani, G.4    Kimchi, A.5
  • 49
    • 84859573948 scopus 로고    scopus 로고
    • PKD is a kinase of Vps34 that mediates ROS-induced autophagy downstream of DAPk
    • Eisenberg-Lerner, A. and Kimchi, A. (2011) PKD is a kinase of Vps34 that mediates ROS-induced autophagy downstream of DAPk. Cell Death Differ. 19, 788-797
    • (2011) Cell Death Differ. , vol.19 , pp. 788-797
    • Eisenberg-Lerner, A.1    Kimchi, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.