메뉴 건너뛰기




Volumn 43, Issue , 2015, Pages 390-395

Alterations in late endocytic trafficking related to the pathobiology of LRRK2-linked Parkinson's disease

Author keywords

Autophagy; Endocytosis; Leucine rich repeat kinase 2 (LRRK2); Nicotinic acid adenine dinucleotide phosphate (NAADP); Parkinson's disease; Rab protein

Indexed keywords

CALCIUM; ION CHANNEL; LEUCINE RICH REPEAT KINASE 2; RAB PROTEIN; TWO PORE CHANNEL; UNCLASSIFIED DRUG; CALCIUM CHANNEL; LRRK2 PROTEIN, HUMAN; PROTEIN SERINE THREONINE KINASE; RNA BINDING PROTEIN;

EID: 84934967144     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20140301     Document Type: Review
Times cited : (27)

References (50)
  • 2
    • 70549084415 scopus 로고    scopus 로고
    • Genome-wide association study identifies common variants at four loci as genetic risk factors for Parkinson's disease
    • CrossRef PubMed
    • Satake, W., Nakabayashi, Y., Mizuta, I., Hirota, Y., Ito, C., Kubo, M., Kawaguchi, T., Tsunoda, T., Watanabe, M., Takeda, A. et al. (2009) Genome-wide association study identifies common variants at four loci as genetic risk factors for Parkinson's disease. Nat. Genet. 41, 1303-1307 CrossRef PubMed
    • (2009) Nat. Genet. , vol.41 , pp. 1303-1307
    • Satake, W.1    Nakabayashi, Y.2    Mizuta, I.3    Hirota, Y.4    Ito, C.5    Kubo, M.6    Kawaguchi, T.7    Tsunoda, T.8    Watanabe, M.9    Takeda, A.10
  • 4
    • 77953395313 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 mutations and Parkinson's disease: Three questions
    • pii:e00002 CrossRef
    • Greggio, E. and Cookson, M.R. (2009) Leucine-rich repeat kinase 2 mutations and Parkinson's disease: three questions. ASN Neuro. 1, pii:e00002, doi:10.1042/AN20090007 CrossRef
    • (2009) ASN Neuro , vol.1
    • Greggio, E.1    Cookson, M.R.2
  • 5
    • 84891776413 scopus 로고    scopus 로고
    • Mutant LRRK2 toxicity in neurons depends on LRRK2 levels and synuclein but not kinase activity or inclusion bodies
    • CrossRef PubMed
    • Skibinski, G., Nakamura, K., Cookson, M.R. and Finkbeiner, S. (2014) Mutant LRRK2 toxicity in neurons depends on LRRK2 levels and synuclein but not kinase activity or inclusion bodies. J. Neurosci. 34, 418-433 CrossRef PubMed
    • (2014) J. Neurosci. , vol.34 , pp. 418-433
    • Skibinski, G.1    Nakamura, K.2    Cookson, M.R.3    Finkbeiner, S.4
  • 9
    • 84874541806 scopus 로고    scopus 로고
    • GTPase activity regulates kinase activity and cellular phenotypes of Parkinson's disease-associated LRRK2
    • CrossRef PubMed
    • Biosa, A., Trancikova, A., Civiero, L., Glauser, L., Bubacco, L., Greggio, E. and Moore, D.J. (2013) GTPase activity regulates kinase activity and cellular phenotypes of Parkinson's disease-associated LRRK2. Hum. Mol. Genet. 22, 1140-1156 CrossRef PubMed
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 1140-1156
    • Biosa, A.1    Trancikova, A.2    Civiero, L.3    Glauser, L.4    Bubacco, L.5    Greggio, E.6    Moore, D.J.7
  • 13
    • 84898622052 scopus 로고    scopus 로고
    • Ribosomal protein s15 phosphorylation mediates LRRK2 neurodegeneration in Parkinson's disease
    • CrossRef PubMed
    • Martin, I., Kim, J.W., Lee, B.D., Kang, H.C., Xu, J.C., Jia, H., Stankowski, J., Kim, M.S., Zhong, J., Kumar, M. et al. (2014) Ribosomal protein s15 phosphorylation mediates LRRK2 neurodegeneration in Parkinson's disease. Cell 157, 472-485 CrossRef PubMed
    • (2014) Cell , vol.157 , pp. 472-485
    • Martin, I.1    Kim, J.W.2    Lee, B.D.3    Kang, H.C.4    Xu, J.C.5    Jia, H.6    Stankowski, J.7    Kim, M.S.8    Zhong, J.9    Kumar, M.10
  • 18
    • 84863241584 scopus 로고    scopus 로고
    • Roles of the Drosophila LRRK2 homolog in Rab7-dependent lysosomal positioning
    • CrossRef PubMed
    • Dodson, M.W., Zhang, T., Jiang, C., Chen, S. and Guo, M. (2012) Roles of the Drosophila LRRK2 homolog in Rab7-dependent lysosomal positioning. Hum. Mol. Genet. 21, 1350-1363 CrossRef PubMed
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 1350-1363
    • Dodson, M.W.1    Zhang, T.2    Jiang, C.3    Chen, S.4    Guo, M.5
  • 19
    • 84919674911 scopus 로고    scopus 로고
    • Novel ethyl methanesulfonate (EMS)-induced null alleles of the Drosophila homolog of LRRK2 reveal a crucial role in endolysosomal functions and autophagy in vivo
    • CrossRef PubMed
    • Dodson, M.W., Leung, L.K., Lone, M., Lizzio, M.A. and Guo, M. (2014) Novel ethyl methanesulfonate (EMS)-induced null alleles of the Drosophila homolog of LRRK2 reveal a crucial role in endolysosomal functions and autophagy in vivo. Dis. Model. Mech. 7, 1351-1363 CrossRef PubMed
    • (2014) Dis. Model. Mech. , vol.7 , pp. 1351-1363
    • Dodson, M.W.1    Leung, L.K.2    Lone, M.3    Lizzio, M.A.4    Guo, M.5
  • 21
    • 84883420073 scopus 로고    scopus 로고
    • Dysfunction of the autophagy/lysosomal degradation pathway is a shared feature of the genetic synucleinopathies
    • CrossRef PubMed
    • Manzoni, C. and Lewis, P.A. (2013) Dysfunction of the autophagy/lysosomal degradation pathway is a shared feature of the genetic synucleinopathies. FASEB J 27, 3424-3429 CrossRef PubMed
    • (2013) FASEB J , vol.27 , pp. 3424-3429
    • Manzoni, C.1    Lewis, P.A.2
  • 22
    • 84887956934 scopus 로고    scopus 로고
    • Genetics of Parkinson's disease-state of the art, 2013
    • CrossRef PubMed
    • Bonifati, V. (2014) Genetics of Parkinson's disease-state of the art, 2013. Parkinsonism Relat. Disord. 20 (Suppl. 1), S23-S28, doi:10.1016/S1353-8020(13)70009-9 CrossRef PubMed
    • (2014) Parkinsonism Relat. Disord. , vol.20 , pp. S23-S28
    • Bonifati, V.1
  • 23
    • 33847388051 scopus 로고    scopus 로고
    • Calcium: A fundamental regulator of intracellular membrane fusion?
    • CrossRef PubMed
    • Hay, J.C. (2007) Calcium: a fundamental regulator of intracellular membrane fusion? EMBO Rep. 8, 236-240 CrossRef PubMed
    • (2007) EMBO Rep. , vol.8 , pp. 236-240
    • Hay, J.C.1
  • 26
    • 84876214388 scopus 로고    scopus 로고
    • Calcium, bioenergetics, and neuronal vulnerability in Parkinson's disease
    • CrossRef PubMed
    • Surmeier, D.J. and Schumacker, P.T. (2013) Calcium, bioenergetics, and neuronal vulnerability in Parkinson's disease. J. Biol. Chem. 288, 10736-10741 CrossRef PubMed
    • (2013) J. Biol. Chem. , vol.288 , pp. 10736-10741
    • Surmeier, D.J.1    Schumacker, P.T.2
  • 27
    • 84872691988 scopus 로고    scopus 로고
    • Mutant LRRK2 elicits calcium imbalance and depletion of dendritic mitochondria in neurons
    • CrossRef PubMed
    • Cherra, 3rd, S.J., Steer, E., Gusdon, A.M., Kiselyov, K. and Chu, C.T. (2013) Mutant LRRK2 elicits calcium imbalance and depletion of dendritic mitochondria in neurons. Am. J. Pathol. 182, 474-484 CrossRef PubMed
    • (2013) Am. J. Pathol. , vol.182 , pp. 474-484
    • Cherra, S.J.1    Steer, E.2    Gusdon, A.M.3    Kiselyov, K.4    Chu, C.T.5
  • 28
    • 80052233389 scopus 로고    scopus 로고
    • Endosome maturation
    • CrossRef PubMed
    • Huotari, J. and Helenius, A. (2011) Endosome maturation. EMBO J. 30, 3481-3500 CrossRef PubMed
    • (2011) EMBO J. , vol.30 , pp. 3481-3500
    • Huotari, J.1    Helenius, A.2
  • 30
    • 70349991886 scopus 로고    scopus 로고
    • LRRK2 regulates autophagic activity and localizes to specific microdomains in a novel human genomic reporter cellular model
    • CrossRef PubMed
    • Alegre-Abarrategui, J., Christian, H., Lufino, M.M., Mutihac, R., Venda, L.L., Ansorge, O. and Wade-Martins, R. (2009) LRRK2 regulates autophagic activity and localizes to specific microdomains in a novel human genomic reporter cellular model. Hum. Mol. Genet. 18, 4022-4034 CrossRef PubMed
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 4022-4034
    • Alegre-Abarrategui, J.1    Christian, H.2    Lufino, M.M.3    Mutihac, R.4    Venda, L.L.5    Ansorge, O.6    Wade-Martins, R.7
  • 31
    • 84902163498 scopus 로고    scopus 로고
    • Membrane recruitment of endogenous LRRK2 precedes its potent regulation of autophagy
    • CrossRef PubMed
    • Schapansky, J., Nardozzi, J.D., Felizia, F. and LaVoie, M.J. (2014) Membrane recruitment of endogenous LRRK2 precedes its potent regulation of autophagy. Hum. Mol. Genet. 23, 4201-4214 CrossRef PubMed
    • (2014) Hum. Mol. Genet. , vol.23 , pp. 4201-4214
    • Schapansky, J.1    Nardozzi, J.D.2    Felizia, F.3    LaVoie, M.J.4
  • 32
    • 84924913990 scopus 로고    scopus 로고
    • LRRK2 localizes to endosomes and interacts with clathrin-light chains to limit Rac1 activation
    • CrossRef
    • Schreij, A.M., Chaineau, M., Ruan, W., Lin, S., Barker, P.A., Fon, E.A. and McPherson, P.S. (2015) LRRK2 localizes to endosomes and interacts with clathrin-light chains to limit Rac1 activation. EMBO Rep. 16, 79-86 CrossRef
    • (2015) EMBO Rep. , vol.16 , pp. 79-86
    • Schreij, A.M.1    Chaineau, M.2    Ruan, W.3    Lin, S.4    Barker, P.A.5    Fon, E.A.6    McPherson, P.S.7
  • 34
    • 79955544006 scopus 로고    scopus 로고
    • Rac1 protein rescues neurite retraction caused by G2019S leucine-rich repeat kinase 2 (LRRK2)
    • CrossRef PubMed
    • Chan, D., Citro, A., Cordy, J.M., Shen, G.C. and Wolozin, B. (2011) Rac1 protein rescues neurite retraction caused by G2019S leucine-rich repeat kinase 2 (LRRK2). J. Biol. Chem. 286, 16140-16149 CrossRef PubMed
    • (2011) J. Biol. Chem. , vol.286 , pp. 16140-16149
    • Chan, D.1    Citro, A.2    Cordy, J.M.3    Shen, G.C.4    Wolozin, B.5
  • 37
    • 84907814142 scopus 로고    scopus 로고
    • TPC1 has two variant isoforms, and their removal has different effects on endo-lysosomal functions compared to loss of TPC2
    • CrossRef PubMed
    • Ruas, M., Chuang, K.T., Davis, L.C., Al-Douri, A., Tynan, P.W., Tunn, R., Teboul, L., Galione, A. and Parrington, J. (2014) TPC1 has two variant isoforms, and their removal has different effects on endo-lysosomal functions compared to loss of TPC2. Mol. Cell Biol. 34, 3981-3992 CrossRef PubMed
    • (2014) Mol. Cell Biol. , vol.34 , pp. 3981-3992
    • Ruas, M.1    Chuang, K.T.2    Davis, L.C.3    Al-Douri, A.4    Tynan, P.W.5    Tunn, R.6    Teboul, L.7    Galione, A.8    Parrington, J.9
  • 41
    • 20444476585 scopus 로고    scopus 로고
    • Ion regulation of homotypic vacuole fusion in Saccharomyces cerevisiae
    • CrossRef PubMed
    • Starai, V.J., Thorngren, N., Fratti, R.A. and Wickner, W. (2005) Ion regulation of homotypic vacuole fusion in Saccharomyces cerevisiae. J. Biol. Chem. 280, 16754-16762 CrossRef PubMed
    • (2005) J. Biol. Chem. , vol.280 , pp. 16754-16762
    • Starai, V.J.1    Thorngren, N.2    Fratti, R.A.3    Wickner, W.4
  • 42
    • 0034729167 scopus 로고    scopus 로고
    • The role of intraorganellar Ca2 + in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles
    • CrossRef PubMed
    • Pryor, P.R., Mullock, B.M., Bright, N.A., Gray, S.R. and Luzio, J.P. (2000) The role of intraorganellar Ca2 + in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles. J. Cell Biol. 149, 1053-1062 CrossRef PubMed
    • (2000) J. Cell Biol. , vol.149 , pp. 1053-1062
    • Pryor, P.R.1    Mullock, B.M.2    Bright, N.A.3    Gray, S.R.4    Luzio, J.P.5
  • 43
    • 0037144587 scopus 로고    scopus 로고
    • Selective effects of calcium chelators on anterograde and retrograde protein transport in the cell
    • Chen, J.L., Ahluwalia, J.P. and Stamnes, M. (2002) Selective effects of calcium chelators on anterograde and retrograde protein transport in the cell. J. Biol. Chem. 277, 3682-35687
    • (2002) J. Biol. Chem. , vol.277 , pp. 3682-35687
    • Chen, J.L.1    Ahluwalia, J.P.2    Stamnes, M.3
  • 45
  • 46
    • 84859833144 scopus 로고    scopus 로고
    • The interaction properties of the human Rab GTPase family-comparative analysis reveals determinants of molecular binding selectivity
    • CrossRef PubMed
    • Stein, M., Pilli, M., Bernauer, S., Habermann, B.H., Zerial, M. and Wade, R.C. (2012) The interaction properties of the human Rab GTPase family-comparative analysis reveals determinants of molecular binding selectivity. PLoS One 7, e34870, doi:10.1371/journal.pone.0034870 CrossRef PubMed
    • (2012) PLoS One , vol.7
    • Stein, M.1    Pilli, M.2    Bernauer, S.3    Habermann, B.H.4    Zerial, M.5    Wade, R.C.6
  • 48
    • 84900388122 scopus 로고    scopus 로고
    • A role of Rab29 in the integrity of the trans-Golgi network and retrograde trafficking of mannose-6-phosphate receptor
    • CrossRef PubMed
    • Wang, S., Ma, Z., Xu, X., Wang, Z., Sun, L., Zhou, Y., Lin, X., Hong, W. and Wang, T. (2014) A role of Rab29 in the integrity of the trans-Golgi network and retrograde trafficking of mannose-6-phosphate receptor. PLoS One 9, e96242, doi:10.1371/journal.pone.0096242 CrossRef PubMed
    • (2014) PLoS One , vol.9
    • Wang, S.1    Ma, Z.2    Xu, X.3    Wang, Z.4    Sun, L.5    Zhou, Y.6    Lin, X.7    Hong, W.8    Wang, T.9
  • 49
    • 33750367865 scopus 로고    scopus 로고
    • Rab38 and Rab32 control post-Golgi trafficking of melanogenic enzymes
    • CrossRef PubMed
    • Wasmeier, C., Romao, M., Plowright, L., Bennett, D.C., Raposo, G. and Seabra, M.C. (2006) Rab38 and Rab32 control post-Golgi trafficking of melanogenic enzymes. J. Cell Biol. 175, 271-281 CrossRef PubMed
    • (2006) J. Cell Biol. , vol.175 , pp. 271-281
    • Wasmeier, C.1    Romao, M.2    Plowright, L.3    Bennett, D.C.4    Raposo, G.5    Seabra, M.C.6
  • 50
    • 84891345615 scopus 로고    scopus 로고
    • Calcium-dependent regulation of Rab activation and vesicle fusion by an intracellular P2X ion channel
    • CrossRef PubMed
    • Parkinson, K., Baines, A.E., Keller, T., Gruenheit, N., Bragg, L., North, R.A. and Thompson, C.R.L. (2014) Calcium-dependent regulation of Rab activation and vesicle fusion by an intracellular P2X ion channel. Nat. Cell Biol. 16, 87-98 CrossRef PubMed
    • (2014) Nat. Cell Biol. , vol.16 , pp. 87-98
    • Parkinson, K.1    Baines, A.E.2    Keller, T.3    Gruenheit, N.4    Bragg, L.5    North, R.A.6    Thompson, C.R.L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.