메뉴 건너뛰기




Volumn 22, Issue 6, 2013, Pages 1140-1156

GTPase activity regulates kinase activity and cellular phenotypes of parkinson's disease-associated LRRK2

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE; LEUCINE RICH REPEAT KINASE 2; MUTANT PROTEIN; PHOSPHOTRANSFERASE; PROTEIN KINASE;

EID: 84874541806     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/dds522     Document Type: Article
Times cited : (112)

References (38)
  • 4
    • 84861232484 scopus 로고    scopus 로고
    • Mechanisms of LRRK2-mediated neurodegeneration
    • Tsika, E. and Moore, D.J. (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.J.2
  • 5
    • 33750931271 scopus 로고    scopus 로고
    • The Parkinson disease gene LRRK2: evolutionary and structural insights
    • Marin, I. (2006) The Parkinson disease gene LRRK2: evolutionary and structural insights. Mol. Biol. Evol., 23, 2423-2433.
    • (2006) Mol. Biol. Evol. , vol.23 , pp. 2423-2433
    • Marin, I.1
  • 6
    • 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
  • 7
    • 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
  • 9
    • 34548621385 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 (LRRK2)/PARK8 possesses GTPase activity that is altered in familial Parkinson's disease R1441C/G mutants
    • Li, X., Tan, Y.C., Poulose, S., Olanow, C.W., Huang, X.Y. and Yue, Z. (2007) Leucine-rich repeat kinase 2 (LRRK2)/PARK8 possesses GTPase activity that is altered in familial Parkinson's disease R1441C/G mutants. J. Neurochem., 103, 238-247.
    • (2007) J. Neurochem. , vol.103 , pp. 238-247
    • Li, X.1    Tan, Y.C.2    Poulose, S.3    Olanow, C.W.4    Huang, X.Y.5    Yue, Z.6
  • 12
    • 84859187983 scopus 로고    scopus 로고
    • GTPase activity and neuronal toxicity of Parkinson's disease-associated LRRK2 is regulated by ArfGAP1
    • Stafa, K., Trancikova, A., Webber, P.J., Glauser, L., West, A.B. and Moore, D.J. (2012) GTPase activity and neuronal toxicity of Parkinson's disease-associated LRRK2 is regulated by ArfGAP1. PLoS Genet., 8, e1002526.
    • (2012) PLoS Genet. , vol.8
    • Stafa, K.1    Trancikova, A.2    Webber, P.J.3    Glauser, L.4    West, A.B.5    Moore, D.J.6
  • 14
    • 34447118788 scopus 로고    scopus 로고
    • LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activity
    • Jaleel, M., Nichols, R.J., Deak, M., Campbell, D.G., Gillardon, F., Knebel, A. and Alessi, D.R. (2007) LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activity. Biochem. J., 405, 307-317.
    • (2007) Biochem. J. , vol.405 , pp. 307-317
    • Jaleel, M.1    Nichols, R.J.2    Deak, M.3    Campbell, D.G.4    Gillardon, F.5    Knebel, A.6    Alessi, D.R.7
  • 18
    • 40349101849 scopus 로고    scopus 로고
    • Structure of the ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 reveals a dimeric GTPase
    • Deng, J., Lewis, P.A., Greggio, E., Sluch, E., Beilina, A. and Cookson, M.R. (2008) Structure of the ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 reveals a dimeric GTPase. Proc. Natl Acad. Sci. USA, 105, 1499-1504.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 1499-1504
    • Deng, J.1    Lewis, P.A.2    Greggio, E.3    Sluch, E.4    Beilina, A.5    Cookson, M.R.6
  • 19
    • 77954197844 scopus 로고    scopus 로고
    • Membrane localization of LRRK2 is associated with increased formation of the highly active LRRK2 dimer and changes in its phosphorylation
    • Berger, Z., Smith, K.A. and LaVoie, M.J. (2010) Membrane localization of LRRK2 is associated with increased formation of the highly active LRRK2 dimer and changes in its phosphorylation. Biochemistry, 49, 5511-5523.
    • (2010) Biochemistry , vol.49 , pp. 5511-5523
    • Berger, Z.1    Smith, K.A.2    LaVoie, M.J.3
  • 20
    • 47749114984 scopus 로고    scopus 로고
    • The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation
    • Greggio, E., Zambrano, I., Kaganovich, A., Beilina, A., Taymans, J.-M., Daniëls, V., Lewis, P., Jain, S., Ding, J., Syed, A. et al. (2008) The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation. J. Biol. Chem., 283, 16906-16914.
    • (2008) J. Biol. Chem. , vol.283 , pp. 16906-16914
    • Greggio, E.1    Zambrano, I.2    Kaganovich, A.3    Beilina, A.4    Taymans, J.-M.5    Daniëls, V.6    Lewis, P.7    Jain, S.8    Ding, J.9    Syed, A.10
  • 21
    • 73649120624 scopus 로고    scopus 로고
    • Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization
    • Sen, S., Webber, P.J. and West, A.B. (2009) Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization. J. Biol. Chem., 284, 36346-36356.
    • (2009) J. Biol. Chem. , vol.284 , pp. 36346-36356
    • Sen, S.1    Webber, P.J.2    West, A.B.3
  • 22
    • 84864743687 scopus 로고    scopus 로고
    • The G2385R variant of leucine-rich repeat kinase 2 associated with Parkinson's disease is a partial loss-of-function mutation
    • Rudenko, I.N., Kaganovich, A., Hauser, D.N., Beylina, A., Chia, R., Ding, J., Maric, D., Jaffe, H. and Cookson, M.R. (2012) The G2385R variant of leucine-rich repeat kinase 2 associated with Parkinson's disease is a partial loss-of-function mutation. Biochem. J., 446, 99-111.
    • (2012) Biochem. J. , vol.446 , pp. 99-111
    • Rudenko, I.N.1    Kaganovich, A.2    Hauser, D.N.3    Beylina, A.4    Chia, R.5    Ding, J.6    Maric, D.7    Jaffe, H.8    Cookson, M.R.9
  • 23
    • 33751256567 scopus 로고    scopus 로고
    • The familial parkinsonism gene LRRK2 regulates neurite process morphology
    • MacLeod, D., Dowman, J., Hammond, R., Leete, T., Inoue, K. and Abeliovich, A. (2006) The familial parkinsonism gene LRRK2 regulates neurite process morphology. Neuron, 52, 587-593.
    • (2006) Neuron , vol.52 , pp. 587-593
    • MacLeod, D.1    Dowman, J.2    Hammond, R.3    Leete, T.4    Inoue, K.5    Abeliovich, A.6
  • 24
    • 70449377127 scopus 로고    scopus 로고
    • Phosphorylation of Ezrin/Radixin/Moesin proteins by LRRK2 promotes the rearrangement of actin cytoskeleton in neuronal morphogenesis
    • Parisiadou, L., Xie, C., Cho, H.J., Lin, X., Gu, X.-L., Long, C.-X., Lobbestael, E., Baekelandt, V., Taymans, J.-M., Sun, L. et al. (2009) Phosphorylation of Ezrin/Radixin/Moesin proteins by LRRK2 promotes the rearrangement of actin cytoskeleton in neuronal morphogenesis. J. Neurosci., 29, 13971-13980.
    • (2009) J. Neurosci. , vol.29 , pp. 13971-13980
    • Parisiadou, L.1    Xie, C.2    Cho, H.J.3    Lin, X.4    Gu, X.-L.5    Long, C.-X.6    Lobbestael, E.7    Baekelandt, V.8    Taymans, J.-M.9    Sun, L.10
  • 25
    • 80054977424 scopus 로고    scopus 로고
    • Chemoproteomics-based design of potent LRRK2-selective lead compounds that attenuate Parkinson's disease-related toxicity in human neurons
    • Ramsden, N., Perrin, J., Ren, Z., Lee, B.D., Zinn, N., Dawson, V.L., Tam, D., Bova, M., Lang, M., Drewes, G. et al. (2011) Chemoproteomics-based design of potent LRRK2-selective lead compounds that attenuate Parkinson's disease-related toxicity in human neurons. ACS Chem. Biol., 6, 1021-1028.
    • (2011) ACS Chem. Biol. , vol.6 , pp. 1021-1028
    • Ramsden, N.1    Perrin, J.2    Ren, Z.3    Lee, B.D.4    Zinn, N.5    Dawson, V.L.6    Tam, D.7    Bova, M.8    Lang, M.9    Drewes, G.10
  • 26
    • 77950631558 scopus 로고    scopus 로고
    • Phosphopeptide analysis reveals two discrete clusters of phosphorylation in the N-terminus and the Roc domain of the Parkinson-disease associated protein kinase LRRK2
    • Gloeckner, C.J., Boldt, K., von Zweydorf, F., Helm, S., Wiesent, L., Sarioglu, H. and Ueffing, M. (2010) Phosphopeptide analysis reveals two discrete clusters of phosphorylation in the N-terminus and the Roc domain of the Parkinson-disease associated protein kinase LRRK2. J. Proteome Res., 9, 1738-1745.
    • (2010) J. Proteome Res. , vol.9 , pp. 1738-1745
    • Gloeckner, C.J.1    Boldt, K.2    von Zweydorf, F.3    Helm, S.4    Wiesent, L.5    Sarioglu, H.6    Ueffing, M.7
  • 28
    • 72749105819 scopus 로고    scopus 로고
    • Identification of the autophosphorylation sites of LRRK2
    • Kamikawaji, S., Ito, G. and Iwatsubo, T. (2009) Identification of the autophosphorylation sites of LRRK2. Biochemistry, 48, 10963-10975.
    • (2009) Biochemistry , vol.48 , pp. 10963-10975
    • Kamikawaji, S.1    Ito, G.2    Iwatsubo, T.3
  • 29
    • 84860389765 scopus 로고    scopus 로고
    • Autophosphorylation in the leucine-rich repeat kinase 2 (LRRK2) GTPase domain modifies kinase and GTP-binding activities
    • Webber, P.J., Smith, A.D., Sen, S., Renfrow, M.B., Mobley, J.A. and West, A.B. (2011) Autophosphorylation in the leucine-rich repeat kinase 2 (LRRK2) GTPase domain modifies kinase and GTP-binding activities. J. Mol. Biol., 412, 94-110.
    • (2011) J. Mol. Biol. , vol.412 , pp. 94-110
    • Webber, P.J.1    Smith, A.D.2    Sen, S.3    Renfrow, M.B.4    Mobley, J.A.5    West, A.B.6
  • 30
    • 79959393264 scopus 로고    scopus 로고
    • Structure-function relationships of the G domain, a canonical switch motif
    • Wittinghofer, A. and Vetter, I.R. (2011) Structure-function relationships of the G domain, a canonical switch motif. Annu. Rev. Biochem., 80, 943-971.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 943-971
    • Wittinghofer, A.1    Vetter, I.R.2
  • 32
    • 84858050446 scopus 로고    scopus 로고
    • ArfGAP1 is a GTPase activating protein for LRRK2: reciprocal regulation of ArfGAP1 by LRRK2
    • Xiong, Y., Yuan, C., Chen, R., Dawson, T.M. and Dawson, V.L. (2012) ArfGAP1 is a GTPase activating protein for LRRK2: reciprocal regulation of ArfGAP1 by LRRK2. J. Neurosci., 32, 3877-3886.
    • (2012) J. Neurosci. , vol.32 , pp. 3877-3886
    • Xiong, Y.1    Yuan, C.2    Chen, R.3    Dawson, T.M.4    Dawson, V.L.5
  • 33
    • 84855952177 scopus 로고    scopus 로고
    • Re-examination of the dimerization state of leucine-rich repeat kinase 2: predominance of the monomeric form
    • Ito, G. and Iwatsubo, T. (2012) Re-examination of the dimerization state of leucine-rich repeat kinase 2: predominance of the monomeric form. Biochem. J., 441, 987-994.
    • (2012) Biochem. J. , vol.441 , pp. 987-994
    • Ito, G.1    Iwatsubo, T.2
  • 34
    • 39549117093 scopus 로고    scopus 로고
    • Role of autophagy in G2019S-LRRK2-associated neurite shortening in differentiated SH-SY5Y cells
    • Plowey, E.D., Cherra, S.J., Liu, Y.-J. and Chu, C.T. (2008) Role of autophagy in G2019S-LRRK2-associated neurite shortening in differentiated SH-SY5Y cells. J. Neurochem., 105, 1048-1056.
    • (2008) J. Neurochem. , vol.105 , pp. 1048-1056
    • Plowey, E.D.1    Cherra, S.J.2    Liu, Y.-J.3    Chu, C.T.4
  • 36
    • 78751522558 scopus 로고    scopus 로고
    • A rat model of progressive nigral neurodegeneration induced by the Parkinson's disease-associated G2019S mutation in LRRK2
    • Dusonchet, J., Kochubey, O., Stafa, K., Young, S.M. Jr, Zufferey, R., Moore, D.J., Schneider, B.L. and Aebischer, P. (2011) A rat model of progressive nigral neurodegeneration induced by the Parkinson's disease-associated G2019S mutation in LRRK2. J. Neurosci., 31, 907-912.
    • (2011) J. Neurosci. , vol.31 , pp. 907-912
    • Dusonchet, J.1    Kochubey, O.2    Stafa, K.3    Young, S.M.J.4    Zufferey, R.5    Moore, D.J.6    Schneider, B.L.7    Aebischer, P.8
  • 37
    • 77953395313 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 mutations and Parkinson's disease: three questions
    • Greggio, E. and Cookson, M.R. (2009) Leucine-rich repeat kinase 2 mutations and Parkinson's disease: three questions. ASN Neuro, 1, e00002.
    • (2009) ASN Neuro , vol.1
    • Greggio, E.1    Cookson, M.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.