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Volumn 7, Issue 1, 2012, Pages 79-91

The juvenile Batten disease protein, CLN3, and its role in regulating anterograde and retrograde post-Golgi trafficking

Author keywords

autophagy; Batten disease; CLN3; endosome; Golgi; juvenile neuronal ceroid lipofuscinosis; lysosome; palmitoylation

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); MEMBRANE PROTEIN; MESSENGER RNA; PROTEIN CLN3; UNCLASSIFIED DRUG;

EID: 84856835788     PISSN: 17460875     EISSN: 17584302     Source Type: Journal    
DOI: 10.2217/clp.11.70     Document Type: Review
Times cited : (74)

References (90)
  • 1
    • 67649419305 scopus 로고    scopus 로고
    • Towards understanding the neuronal ceroid lipofuscinoses
    • Kohlschutter A, Schulz A. Towards understanding the neuronal ceroid lipofuscinoses. Brain Dev. 31(7), 499-502 (2009).
    • (2009) Brain Dev. , vol.31 , Issue.7 , pp. 499-502
    • Kohlschutter, A.1    Schulz, A.2
  • 2
    • 62949195147 scopus 로고    scopus 로고
    • Neuronal ceroid lipofuscinoses
    • Jalanko A, Braulke T. Neuronal ceroid lipofuscinoses. Biochim. Biophys. Acta 1793(4), 697-709 (2009).
    • (2009) Biochim. Biophys. Acta , vol.1793 , Issue.4 , pp. 697-709
    • Jalanko, A.1    Braulke, T.2
  • 4
    • 25844517550 scopus 로고    scopus 로고
    • Correlations between genotype, ultrastructural morphology and clinical phenotype in the neuronal ceroid lipofuscinoses
    • DOI 10.1007/s10048-005-0218-3
    • Mole S, Williams R, Goebel H. Correlations between genotype, ultrastructural morphology and clinical phenotype in the neuronal ceroid lipofuscinoses. Neurogenetics 6(3), 107-126 (2005). (Pubitemid 41396987)
    • (2005) Neurogenetics , vol.6 , Issue.3 , pp. 107-126
    • Mole, S.E.1    Williams, R.E.2    Goebel, H.H.3
  • 5
    • 71749101489 scopus 로고    scopus 로고
    • An autoantibody inhibitory to glutamic acid decarboxylase in the neurodegenerative disorder Batten disease
    • Chattopadhyay S, Ito M, Cooper J et al. An autoantibody inhibitory to glutamic acid decarboxylase in the neurodegenerative disorder Batten disease. Hum. Mol. Genet. 11(12), 1421-1431 (2002).
    • (2002) Hum. Mol. Genet. , vol.11 , Issue.12 , pp. 1421-1431
    • Chattopadhyay, S.1    Ito, M.2    Cooper, J.3
  • 6
    • 36549065253 scopus 로고    scopus 로고
    • Identification of α-fetoprotein as an autoantigen in juvenile Batten disease
    • DOI 10.1016/j.nbd.2007.08.007, PII S096999610700188X
    • Castaneda J, Pearce D. Identifcation of alpha-fetoprotein as an autoantigen in juvenile Batten disease. Neurobiol. Dis. 29(1), 92-102 (2008). (Pubitemid 350180486)
    • (2008) Neurobiology of Disease , vol.29 , Issue.1 , pp. 92-102
    • Castaneda, J.A.1    Pearce, D.A.2
  • 7
    • 79954623288 scopus 로고    scopus 로고
    • Cardiac involvement in juvenile neuronal ceroid lipofuscinosis (Batten disease)
    • Ostergaard J, Rasmussen T, Molgaard H. Cardiac involvement in juvenile neuronal ceroid lipofuscinosis (Batten disease). Neurology 76(14), 1245-1251 (2011).
    • (2011) Neurology , vol.76 , Issue.14 , pp. 1245-1251
    • Ostergaard, J.1    Rasmussen, T.2    Molgaard, H.3
  • 8
    • 0034926037 scopus 로고    scopus 로고
    • Cardiac pathology in neuronal ceroid lipofuscinoses - A clinicopathologic correlation in three patients
    • DOI 10.1053/ejpn.2001.0515
    • Hofman I, van der Wal A, Dingemans K, Becker A. Cardiac pathology in neuronal ceroid lipofuscinoses-a clinicopathologic correlation in three patients. Eur. J. Paediatr. Neurol. 5(Suppl. A), 213-217 (2001). (Pubitemid 32677142)
    • (2001) European Journal of Paediatric Neurology , vol.5 , Issue.SUPPL. A , pp. 213-217
    • Hofman, I.L.1    Van Der Wal, A.C.2    Dingemans, K.P.3    Becker, A.E.4
  • 9
    • 82855172223 scopus 로고    scopus 로고
    • Analysis of potential biomarkers and modifer genes affecting the clinical course of CLN3 disease
    • doi:10.2119/molmed.2010.00241 Epub ahead of print
    • Lebrun A, Moll-Khosrawi P, Pohl S et al. Analysis of potential biomarkers and modifer genes affecting the clinical course of CLN3 disease. Mol. Med. doi:10.2119/molmed.2010.00241 (2011) (Epub ahead of print).
    • (2011) Mol. Med
    • Lebrun, A.1    Moll-Khosrawi, P.2    Pohl, S.3
  • 10
    • 33344469599 scopus 로고    scopus 로고
    • You say lipofuscin, we say ceroid: Defining autofluorescent storage material
    • DOI 10.1016/j.neurobiolaging.2005.12.006, PII S0197458005004276, Protein Misfolding in Alzheimer's and Other Age-Related Neurodegenerative Diseases
    • Seehafer S, Pearce D. You say lipofuscin, we say ceroid: defning autofuorescent storage material. Neurobiol. Aging 27(4), 576-588 (2006). (Pubitemid 43290526)
    • (2006) Neurobiology of Aging , vol.27 , Issue.4 , pp. 576-588
    • Seehafer, S.S.1    Pearce, D.A.2
  • 11
    • 22544463623 scopus 로고    scopus 로고
    • A short guided tour through functional and structural features of saposin-like proteins
    • DOI 10.1042/BJ20050051
    • Bruhn H. A short guided tour through functional and structural features of saposin-like proteins. Biochem. J. 389(Pt 2), 249-257 (2005). (Pubitemid 41021127)
    • (2005) Biochemical Journal , vol.389 , Issue.2 , pp. 249-257
    • Bruhn, H.1
  • 12
    • 38449095568 scopus 로고    scopus 로고
    • The function of sphingolipids in the nervous system: Lessons learnt from mouse models of specifc sphingolipid activator protein defciencies
    • Matsuda J, Yoneshige A, Suzuki K. The function of sphingolipids in the nervous system: lessons learnt from mouse models of specifc sphingolipid activator protein defciencies. J. Neurochem. 103(Suppl. 1), 32-38 (2007).
    • (2007) J. Neurochem. , vol.103 , Issue.SUPPL. 1 , pp. 32-38
    • Matsuda, J.1    Yoneshige, A.2    Suzuki, K.3
  • 13
    • 0026539541 scopus 로고
    • Mitochondrial ATP synthase subunit c storage in the ceroid-lipofuscinoses (Batten disease)
    • Palmer D, Fearnley I, Walker J et al. Mitochondrial ATP synthase subunit c storage in the ceroid-lipofuscinoses (Batten disease). Am. J. Med. Genet. 42(4), 561-567 (1992).
    • (1992) Am. J. Med. Genet. , vol.42 , Issue.4 , pp. 561-567
    • Palmer, D.1    Fearnley, I.2    Walker, J.3
  • 14
    • 0029009246 scopus 로고
    • Batten disease and the ATP synthase subunit c turnover pathway: Raising antibodies to subunit c
    • Palmer D, Bayliss S, Westlake V. Batten disease and the ATP synthase subunit c turnover pathway: raising antibodies to subunit c. Am. J. Med. Genet. 57(2), 260-265 (1995).
    • (1995) Am. J. Med. Genet. , vol.57 , Issue.2 , pp. 260-265
    • Palmer, D.1    Bayliss, S.2    Westlake, V.3
  • 15
    • 1842830744 scopus 로고    scopus 로고
    • What are the requirements for lysosomal degradation of subunit c of mitochondrial ATPase?
    • Kominami E. What are the requirements for lysosomal degradation of subunit c of mitochondrial ATPase? IUBMB Life 54(2), 89-90 (2002).
    • (2002) IUBMB Life , vol.54 , Issue.2 , pp. 89-90
    • Kominami, E.1
  • 16
    • 34250781863 scopus 로고    scopus 로고
    • Genotype-phenotype analyses of classic neuronal ceroid lipofuscinosis (NCLs): Genetic predictions from clinical and pathological fndings
    • Ju W, Wronska A, Moroziewicz D et al. Genotype-phenotype analyses of classic neuronal ceroid lipofuscinosis (NCLs): genetic predictions from clinical and pathological fndings. Beijing Da Xue Xue Bao 38(1), 41-48 (2006).
    • (2006) Beijing da Xue Xue Bao , vol.38 , Issue.1 , pp. 41-48
    • Ju, W.1    Wronska, A.2    Moroziewicz, D.3
  • 17
    • 0028970313 scopus 로고
    • Sphingolipid activator proteins in the neuronal ceroid-lipofuscinoses: An immunological study
    • Tyynela J, Baumann M, Henseler M, Sandhoff K, Haltia M. Sphingolipid activator proteins in the neuronal ceroid-lipofuscinoses: an immunological study. Acta Neuropathol. 89(5), 391-398 (1995).
    • (1995) Acta Neuropathol. , vol.89 , Issue.5 , pp. 391-398
    • Tyynela, J.1    Baumann, M.2    Henseler, M.3    Sandhoff, K.4    Haltia, M.5
  • 18
    • 71949103162 scopus 로고    scopus 로고
    • Novel interactions of CLN5 support molecular networking between neuronal ceroid lipofuscinosis proteins
    • Lyly A, Von Schantz C, Heine C et al. Novel interactions of CLN5 support molecular networking between neuronal ceroid lipofuscinosis proteins. BMC Cell. Biol. 10, 83 (2009).
    • (2009) BMC Cell. Biol. , vol.10 , pp. 83
    • Lyly, A.1    Von Schantz, C.2    Heine, C.3
  • 21
    • 79951552729 scopus 로고    scopus 로고
    • Interactions of the proteins of neuronal ceroid lipofuscinosis: Clues to function
    • Getty A, Pearce D. Interactions of the proteins of neuronal ceroid lipofuscinosis: clues to function. Cell. Mol. Life Sci. 68(3), 453-474 (2011).
    • (2011) Cell. Mol. Life Sci. , vol.68 , Issue.3 , pp. 453-474
    • Getty, A.1    Pearce, D.2
  • 23
    • 0029147298 scopus 로고
    • Isolation of a novel gene underlying Batten disease, CLN3. The International Batten Disease Consortium
    • Isolation of a novel gene underlying Batten disease, CLN3. The International Batten Disease Consortium. Cell 82 (6), 949-957 (1995).
    • (1995) Cell , vol.82 , Issue.6 , pp. 949-957
  • 26
    • 0038069054 scopus 로고    scopus 로고
    • Control of glutamatergic neurotransmission in the rat spinal dorsal horn by the nucleoside transporter ENT1
    • DOI 10.1113/jphysiol.2002.038091
    • Ackley M, Governo R, Cass C, Young J, Baldwin S, King A. Control of glutamatergic neurotransmission in the rat spinal dorsal horn by the nucleoside transporter ENT1. J. Physiol. 548(Pt 2), 507-517 (2003). (Pubitemid 36527472)
    • (2003) Journal of Physiology , vol.548 , Issue.2 , pp. 507-517
    • Ackley, M.A.1    Governo, R.J.M.2    Cass, C.E.3    Young, J.D.4    Baldwin, S.A.5    King, A.E.6
  • 27
    • 0031888525 scopus 로고    scopus 로고
    • Major facilitator superfamily Microbiol
    • Pao S, Paulsen I, Saier M Jr. Major facilitator superfamily Microbiol. Mol. Biol. Rev. 62(1), 1-34 (1998).
    • (1998) Mol. Biol. Rev. , vol.62 , Issue.1 , pp. 1-34
    • Pao, S.1    Paulsen, I.2    Saier Jr., M.3
  • 28
    • 40849086134 scopus 로고    scopus 로고
    • The transmembrane topology of Batten disease protein CLN3 determined by consensus computational prediction constrained by experimental data
    • Nugent T, Mole S, Jones D. The transmembrane topology of Batten disease protein CLN3 determined by consensus computational prediction constrained by experimental data. FEBS Lett. 582(7), 1019-1024 (2008).
    • (2008) FEBS Lett. , vol.582 , Issue.7 , pp. 1019-1024
    • Nugent, T.1    Mole, S.2    Jones, D.3
  • 29
    • 33947245588 scopus 로고    scopus 로고
    • C-terminal prenylation of the CLN3 membrane glycoprotein is required for efficient endosomal sorting to lysosomes
    • DOI 10.1111/j.1600-0854.2007.00537.x
    • Storch S, Pohl S, Quitsch A, Falley K, Braulke T C-terminal prenylation of the CLN3 membrane glycoprotein is required for effcient endosomal sorting to lysosomes. Traffic 8(4), 431-444 (2007). (Pubitemid 46421624)
    • (2007) Traffic , vol.8 , Issue.4 , pp. 431-444
    • Storch, S.1    Pohl, S.2    Quitsch, A.3    Falley, K.4    Braulke, T.5
  • 31
    • 33845293272 scopus 로고    scopus 로고
    • CLN3P, the Batten's disease protein, is a novel palmitoyl-protein Δ-9 desaturase
    • DOI 10.1002/ana.20975
    • Narayan S, Rakheja D, Tan L, Pastor J, Bennett M. CLN3P, the Batten's disease protein, is a novel palmitoyl-protein Delta-9 desaturase. Ann. Neurol. 60(5), 570-577 (2006). (Pubitemid 44871799)
    • (2006) Annals of Neurology , vol.60 , Issue.5 , pp. 570-577
    • Narayan, S.B.1    Rakheja, D.2    Tan, L.3    Pastor, J.V.4    Bennett, M.J.5
  • 32
    • 36849084546 scopus 로고    scopus 로고
    • Intermediate levels of neuronal palmitoyl-protein Δ-9 desaturase in heterozygotes for murine Batten disease
    • DOI 10.1016/j.ymgme.2007.09.005, PII S1096719207004052
    • Narayan S, Tan L, Bennett M. Intermediate levels of neuronal palmitoyl-protein D-9 desaturase in heterozygotes for murine Batten disease. Mol. Genet. Metab. 93(1), 89-91 (2008). (Pubitemid 350236008)
    • (2008) Molecular Genetics and Metabolism , vol.93 , Issue.1 , pp. 89-91
    • Narayan, S.B.1    Tan, L.2    Bennett, M.J.3
  • 33
    • 0035990987 scopus 로고    scopus 로고
    • Neuronal ceroid lipofuscinoses caused by defects in soluble lysosomal enzymes (CLN1 and CLN2)
    • DOI 10.2174/1566524023362294
    • Hofmann S, Atashband A, Cho S, Das A, Gupta P, Lu Jy. Neuronal ceroid lipofuscinoses caused by defects in soluble lysosomal enzymes (CLN1 and CLN2). Curr. Mol. Med. 2(5), 423-437 (2002). (Pubitemid 34760025)
    • (2002) Current Molecular Medicine , vol.2 , Issue.5 , pp. 423-437
    • Hofmann, S.L.1    Atashband, A.2    Cho, S.K.3    Das, A.K.4    Gupta, P.5    Lu, J.-Y.6
  • 34
    • 80051672679 scopus 로고    scopus 로고
    • Mutations in DNAJC5, encoding cysteine-string protein alpha, cause autosomal-dominant adult-onset neuronal ceroid lipofuscinosis
    • Noskova L, Stranecky V, Hartmannova H et al. Mutations in DNAJC5, encoding cysteine-string protein alpha, cause autosomal-dominant adult-onset neuronal ceroid lipofuscinosis. Am. J. Hum. Genet. 89(2), 241-252 (2011).
    • (2011) Am. J. Hum. Genet. , vol.89 , Issue.2 , pp. 241-252
    • Noskova, L.1    Stranecky, V.2    Hartmannova, H.3
  • 36
    • 30544437316 scopus 로고    scopus 로고
    • Btn1, the Schizosaccharomyces pombe homologue of the human Batten disease gene CLN3, regulates vacuole homeostasis
    • DOI 10.1242/jcs.02656
    • Gachet Y, Codlin S, Hyams J, Mole S. btn1, the Schizosaccharomyces pombe homologue of the human Batten disease gene CLN3, regulates vacuole homeostasis. J. Cell. Sci. 118(Pt 23), 5525-5536 (2005). (Pubitemid 43079293)
    • (2005) Journal of Cell Science , vol.118 , Issue.23 , pp. 5525-5536
    • Gachet, Y.1    Codlin, S.2    Hyams, J.S.3    Mole, S.E.4
  • 37
    • 45849094467 scopus 로고    scopus 로고
    • Analysis of NCL proteins from an evolutionary standpoint
    • DOI 10.2174/138920208784139573
    • Muzaffar N, Pearce D. Analysis of NCL Proteins from an evolutionary standpoint. Curr. Genom. 9(2), 115-136 (2008). (Pubitemid 351888529)
    • (2008) Current Genomics , vol.9 , Issue.2 , pp. 115-136
    • Muzaffar, N.E.1    Pearce, D.A.2
  • 38
    • 67650924287 scopus 로고    scopus 로고
    • Protracted course of juvenile ceroid lipofuscinosis associated with a novel CLN3 mutation (p.Y199X)
    • Sarpong A, Schottmann G, Ruther K et al. Protracted course of juvenile ceroid lipofuscinosis associated with a novel CLN3 mutation (p.Y199X). Clin. Genet. 76(1), 38-45 (2009).
    • (2009) Clin. Genet. , vol.76 , Issue.1 , pp. 38-45
    • Sarpong, A.1    Schottmann, G.2    Ruther, K.3
  • 39
    • 58149218092 scopus 로고    scopus 로고
    • A 30-year follow-up of a neuronal ceroid lipofuscinosis patient with mutations in CLN3 and protracted disease course
    • Aberg L, Lauronen L, Hamalainen J, Mole S, Autti T. A 30-year follow-up of a neuronal ceroid lipofuscinosis patient with mutations in CLN3 and protracted disease course. Pediatr. Neurol. 40(2), 134-137 (2009).
    • (2009) Pediatr. Neurol. , vol.40 , Issue.2 , pp. 134-137
    • Aberg, L.1    Lauronen, L.2    Hamalainen, J.3    Mole, S.4    Autti, T.5
  • 45
    • 0032807059 scopus 로고    scopus 로고
    • Analysis of intracellular distribution and trafficking of the CLN3 protein in fusion with the green fluorescent protein in vitro
    • DOI 10.1006/mgme.1999.2837
    • Kida E, Kaczmarski W, Golabek A, Kaczmarski A, Michalewski M, Wisniewski K. Analysis of intracellular distribution and traffcking of the CLN3 protein in fusion with the green fuorescent protein in vitro. Mol. Genet. Metab. 66(4), 265-271 (1999). (Pubitemid 29390185)
    • (1999) Molecular Genetics and Metabolism , vol.66 , Issue.4 , pp. 265-271
    • Kida, E.1    Kaczmarski, W.2    Golabek, A.A.3    Kaczmarski, A.4    Michalewski, M.5    Wisniewski, K.E.6
  • 46
    • 1542313968 scopus 로고    scopus 로고
    • Two motifs target batten disease protein CLN3 to lysosomes in transfected nonneuronal and neuronal cells
    • DOI 10.1091/mbc.E03-02-0120
    • Kyttala A, Ihrke G, Vesa J, Schell M, Luzio J. Two motifs target Batten disease protein CLN3 to lysosomes in transfected nonneuronal and neuronal cells. Mol. Biol. Cell 15, 1313-1323 (2004). (Pubitemid 38316237)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.3 , pp. 1313-1323
    • Kyttala, A.1    Ihrke, G.2    Vesa, J.3    Schell, M.J.4    Luzio, J.P.5
  • 47
    • 11144231239 scopus 로고    scopus 로고
    • A dileucine motif and a cluster of acidic amino acids in the second cytoplasmic domain of the batten disease-related CLN3 protein are required for efficient lysosomal targeting
    • DOI 10.1074/jbc.M410930200
    • Storch S, Pohl S, Braulke T. A dileucine motif and a cluster of acidic amino acids in the second cytoplasmic domain of the batten disease-related CLN3 protein are required for effcient lysosomal targeting. J. Biol. Chem. 279(51), 53625-53634 (2004). (Pubitemid 40051870)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.51 , pp. 53625-53634
    • Storch, S.1    Pohl, S.2    Braulke, T.3
  • 48
    • 15444378335 scopus 로고    scopus 로고
    • AP-1 and AP-3 facilitate lysosomal targeting of Batten disease protein CLN3 via its dileucine motif
    • DOI 10.1074/jbc.M411862200
    • Kyttala A, Yliannala K, Schu P, Jalanko A, Luzio J. AP-1 and AP-3 facilitate lysosomal targeting of Batten disease protein CLN3 via its dileucine motif. J. Biol. Chem. 280(11), 10277-10283 (2005). (Pubitemid 40395883)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.11 , pp. 10277-10283
    • Kyttala, A.1    Yliannala, K.2    Schu, P.3    Jalanko, A.4    Luzio, J.P.5
  • 49
    • 0032812173 scopus 로고    scopus 로고
    • Splicing variants in sheep CLN3, the gene underlying juvenile neuronal ceroid lipofuscinosis
    • DOI 10.1006/mgme.1999.2848
    • Oswald M, Palmer D, Damak S. Splicing variants in sheep CLN3, the gene underlying juvenile neuronal ceroid lipofuscinosis. Mol. Genet. Metab. 67(2), 169-175 (1999). (Pubitemid 29393245)
    • (1999) Molecular Genetics and Metabolism , vol.67 , Issue.2 , pp. 169-175
    • Oswald, M.J.1    Palmer, D.N.2    Damak, S.3
  • 54
    • 12944291307 scopus 로고    scopus 로고
    • Membrane traffcking and mitochondrial abnormalities precede subunit c deposition in a cerebellar cell model of juvenile neuronal ceroid lipofuscinosis
    • Fossale E, Wolf P, Espinola J et al. Membrane traffcking and mitochondrial abnormalities precede subunit c deposition in a cerebellar cell model of juvenile neuronal ceroid lipofuscinosis. BMC Neurosci. 5, 57 (2004).
    • (2004) BMC Neurosci. , vol.5 , pp. 57
    • Fossale, E.1    Wolf, P.2    Espinola, J.3
  • 55
    • 79951993462 scopus 로고    scopus 로고
    • Distinct early molecular responses to mutations causing vLINCL and JNCL presage ATP synthase subunit c accumulation in cerebellar cells
    • Cao Y, Staropoli J, Biswas S et al. Distinct early molecular responses to mutations causing vLINCL and JNCL presage ATP synthase subunit c accumulation in cerebellar cells. PLoS One 6(2), E17118 (2011).
    • (2011) PLoS One , vol.6 , Issue.2
    • Cao, Y.1    Staropoli, J.2    Biswas, S.3
  • 56
    • 54449095178 scopus 로고    scopus 로고
    • Transcript and in silico analysis of CLN3 in juvenile neuronal ceroid lipofuscinosis and associated mouse models
    • Chan C, Mitchison H, Pearce D. Transcript and in silico analysis of CLN3 in juvenile neuronal ceroid lipofuscinosis and associated mouse models. Hum. Mol. Genet. 17(21), 3332-3339 (2008).
    • (2008) Hum. Mol. Genet. , vol.17 , Issue.21 , pp. 3332-3339
    • Chan, C.1    Mitchison, H.2    Pearce, D.3
  • 57
    • 37849028611 scopus 로고    scopus 로고
    • A function retained by the common mutant CLN3 protein is responsible for the late onset of juvenile neuronal ceroid lipofuscinosis
    • Kitzmuller C, Haines R, Codlin S, Cutler D, Mole S. A function retained by the common mutant CLN3 protein is responsible for the late onset of juvenile neuronal ceroid lipofuscinosis. Hum. Mol. Genet. 17(2), 303-312 (2008).
    • (2008) Hum. Mol. Genet. , vol.17 , Issue.2 , pp. 303-312
    • Kitzmuller, C.1    Haines, R.2    Codlin, S.3    Cutler, D.4    Mole, S.5
  • 58
    • 0030786568 scopus 로고    scopus 로고
    • Farnesylation of Batten disease CLN3 protein
    • Pullarkat R, Morris G. Farnesylation of Batten disease CLN3 protein. Neuropediatrics 28(1), 42-44 (1997). (Pubitemid 27283157)
    • (1997) Neuropediatrics , vol.28 , Issue.1 , pp. 42-44
    • Pullarkat, R.K.1    Morris, G.N.2
  • 59
    • 4344583947 scopus 로고    scopus 로고
    • A galactosylceramide binding domain is involved in trafficking of CLN3 from Golgi to rafts via recycling endosomes
    • Persaud-Sawin D, Mcnamara J, Vandongen R, Boustany R. A galactosylceramide binding domain is involved in traffcking of CLN3 from Golgi to rafts via recycling endosomes. Pediatr. Res. 56(3), 449-463 (2004). (Pubitemid 39128832)
    • (2004) Pediatric Research , vol.56 , Issue.3 , pp. 449-463
    • Persaud-Sawin, D.-A.1    McNamara II, J.O.2    Rylova, S.3    Vandongen, A.4    Boustany, R.-M.N.5
  • 65
    • 53349099845 scopus 로고    scopus 로고
    • Btn1 affects cytokinesis and cell-wall deposition by independent mechanisms, one of which is linked to dysregulation of vacuole pH
    • Codlin S, Haines R, Burden J, Mole S. Btn1 affects cytokinesis and cell-wall deposition by independent mechanisms, one of which is linked to dysregulation of vacuole pH. J. Cell. Sci. 121(Pt 17), 2860-2870 (2008).
    • (2008) J. Cell. Sci. , vol.121 , Issue.PART 17 , pp. 2860-2870
    • Codlin, S.1    Haines, R.2    Burden, J.3    Mole, S.4
  • 66
    • 0034772310 scopus 로고    scopus 로고
    • CLN3 protein is targeted to neuronal synapses but excluded from synaptic vesicles: New clues to Batten disease
    • Luiro K, Kopra O, Lehtovirta M, Jalanko A. CLN3 protein is targeted to neuronal synapses but excluded from synaptic vesicles: new clues to Batten disease. Hum. Mol. Genet. 10(19), 2123-2131 (2001). (Pubitemid 32998824)
    • (2001) Human Molecular Genetics , vol.10 , Issue.19 , pp. 2123-2131
    • Luiro, K.1    Kopra, O.2    Lehtovirta, M.3    Jalanko, A.4
  • 67
    • 33744788400 scopus 로고    scopus 로고
    • Selectively increased sensitivity of cerebellar granule cells to AMPA receptor-mediated excitotoxicity in a mouse model of Batten disease
    • DOI 10.1016/j.nbd.2005.12.018, PII S0969996105003645
    • Kovacs A, Weimer J, Pearce D. Selectively increased sensitivity of cerebellar granule cells to AMPA receptor-mediated excitotoxicity in a mouse model of Batten disease. Neurobiol. Dis. 22(3), 575-585 (2006). (Pubitemid 43832129)
    • (2006) Neurobiology of Disease , vol.22 , Issue.3 , pp. 575-585
    • Kovacs, A.D.1    Weimer, J.M.2    Pearce, D.A.3
  • 69
    • 79953689889 scopus 로고    scopus 로고
    • Altered sensitivity of cerebellar granule cells to glutamate receptor overactivation in the Cln3(Deltaex7/8)-knock-in mouse model of juvenile neuronal ceroid lipofuscinosis
    • Finn R, Kovacs A, Pearce D. Altered sensitivity of cerebellar granule cells to glutamate receptor overactivation in the Cln3(Deltaex7/8)-knock-in mouse model of juvenile neuronal ceroid lipofuscinosis. Neurochem. Int. 58(6), 648-655 (2011).
    • (2011) Neurochem. Int. , vol.58 , Issue.6 , pp. 648-655
    • Finn, R.1    Kovacs, A.2    Pearce, D.3
  • 72
    • 1942516415 scopus 로고    scopus 로고
    • CLN3P, the Batten disease protein, localizes to membrane lipid rafts (detergent-resistant membranes)
    • DOI 10.1016/j.bbrc.2004.03.146, PII S0006291X04006552
    • Rakheja D, Narayan S, Pastor J, Bennett M. CLN3P, the Batten disease protein, localizes to membrane lipid rafts (detergent-resistant membranes). Biochem. Biophys. Res. Commun. 317(4), 988-991 (2004). (Pubitemid 38496407)
    • (2004) Biochemical and Biophysical Research Communications , vol.317 , Issue.4 , pp. 988-991
    • Rakheja, D.1    Narayan, S.B.2    Pastor, J.V.3    Bennett, M.J.4
  • 74
    • 0036712747 scopus 로고    scopus 로고
    • Motifs within the CLN3 protein: Modulation of cell growth rates and apoptosis
    • Persaud-Sawin D-A, Vandongen A, Boustany R-M. Motifs within the CLN3 protein: modulation of cell growth rates and apoptosis. Hum. Mol. Genet. 11(18), 2129-2142 (2002). (Pubitemid 34994001)
    • (2002) Human Molecular Genetics , vol.11 , Issue.18 , pp. 2129-2142
    • Persaud-Sawin, D.N.W.1    Vandongen, A.2    Boustany, R.-M.N.3
  • 75
    • 16444366586 scopus 로고    scopus 로고
    • CLN3, the protein associated with batten disease: Structure, function and localization
    • DOI 10.1002/jnr.20367
    • Phillips S, Benedict J, Weimer J, Pearce D. CLN3, the protein associated with Batten disease: structure, function and localization. J. Neurosci. Res. 79, 573-583 (2005). (Pubitemid 40476436)
    • (2005) Journal of Neuroscience Research , vol.79 , Issue.5 , pp. 573-583
    • Phillips, S.N.1    Benedict, J.W.2    Weimer, J.M.3    Pearce, D.A.4
  • 77
    • 78650912761 scopus 로고    scopus 로고
    • PH-dependent localization of Btn1p in the yeast model for Batten disease
    • Wolfe DM, Padilla-Lopez S, Vitiello SP, Pearce DA. pH-dependent localization of Btn1p in the yeast model for Batten disease. Dis. Model. Mech. 4(1), 120-125 (2011).
    • (2011) Dis. Model. Mech. , vol.4 , Issue.1 , pp. 120-125
    • Wolfe, D.M.1    Padilla-Lopez, S.2    Vitiello, S.P.3    Pearce, D.A.4
  • 78
    • 80155138564 scopus 로고    scopus 로고
    • The yeast Batten disease ortholog, Btn1, controls endosome-Golgi retrograde transport via SNARE assembly
    • Kama R, Kanneganti V, Ungermann C, Gerst J. The yeast Batten disease ortholog, Btn1, controls endosome-Golgi retrograde transport via SNARE assembly. J. Cell Biol. 195(2), 203-215 (2011).
    • (2011) J. Cell Biol. , vol.195 , Issue.2 , pp. 203-215
    • Kama, R.1    Kanneganti, V.2    Ungermann, C.3    Gerst, J.4
  • 79
    • 33744530432 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae lacking Btn1p modulate vacuolar ATPase activity to regulate pH imbalance in the vacuole
    • DOI 10.1074/jbc.M510625200
    • Padilla-Lopez S, Pearce D. Saccharomyces cerevisiae lacking Btn1p modulate vacuolar ATPase activity in order to regulate pH imbalance in the vacuole. J. Biol. Chem. 281(15), 10273-10280 (2006). (Pubitemid 43864565)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.15 , pp. 10273-10280
    • Padilla-Lopez, S.1    Pearce, D.A.2
  • 80
    • 66849138215 scopus 로고    scopus 로고
    • S. pombe btn1, the orthologue of the Batten disease gene CLN3, is required for vacuole protein sorting of Cpy1p and Golgi exit of Vps10p
    • Codlin S, Mole SE. S. pombe btn1, the orthologue of the Batten disease gene CLN3, is required for vacuole protein sorting of Cpy1p and Golgi exit of Vps10p. J. Cell. Sci. 122(Pt 8), 1163-1173 (2009).
    • (2009) J. Cell. Sci. , vol.122 , Issue.PART 8 , pp. 1163-1173
    • Codlin, S.1    Mole, S.E.2
  • 81
    • 53849117085 scopus 로고    scopus 로고
    • Loss of the Batten disease gene CLN3 prevents exit from the TGN of the mannose 6-phosphate receptor
    • Metcalf D, Calvi A, Seaman M, Mitchison H, Cutler D. Loss of the Batten disease gene CLN3 prevents exit from the TGN of the mannose 6-phosphate receptor. Traffic 9(11), 1905-1914 (2008).
    • (2008) Traffic , vol.9 , Issue.11 , pp. 1905-1914
    • Metcalf, D.1    Calvi, A.2    Seaman, M.3    Mitchison, H.4    Cutler, D.5
  • 82
    • 0032905252 scopus 로고    scopus 로고
    • Action of BTN1, the yeast orthologue of the gene mutated in Batten disease
    • DOI 10.1038/8861
    • Pearce D, Ferea T, Nosel S, Das B, Sherman F. Action of BTN1, the yeast orthologue of the gene mutated in Batten disease. Nat. Genet. 22(1), 55-58 (1999). (Pubitemid 29214804)
    • (1999) Nature Genetics , vol.22 , Issue.1 , pp. 55-58
    • Pearce, D.A.1    Ferea, T.2    Nosel, S.A.3    Das, B.4    Sherman, F.5
  • 83
    • 0037436836 scopus 로고    scopus 로고
    • The yeast model for Batten disease: A role for Btn2p in the trafficking of the Golgi-associated vesicular targeting protein, Yif1p
    • DOI 10.1016/S0006-291X(03)00209-2
    • Chattopadhyay S, Roberts P, Pearce D. The yeast model for Batten disease: a role for Btn2p in the traffcking of the Golgi-associated vesicular targeting protein, Yif1p. Biochem. Biophys. Res. Commun. 302(3), 534-538 (2003). (Pubitemid 36279563)
    • (2003) Biochemical and Biophysical Research Communications , vol.302 , Issue.3 , pp. 534-538
    • Chattopadhyay, S.1    Roberts, P.M.2    Pearce, D.A.3
  • 84
    • 33846130921 scopus 로고    scopus 로고
    • Btn2, a Hook1 ortholog and potential Batten disease-related protein, mediates late endosome-Golgi protein sorting in yeast
    • DOI 10.1128/MCB.00699-06
    • Kama R, Robinson M, Gerst J. Btn2, a Hook1 ortholog and potential Batten disease-related protein, mediates late endosome-Golgi protein sorting in yeast. Mol. Cell. Biol. 27(2), 605-621 (2007). (Pubitemid 46080128)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.2 , pp. 605-621
    • Kama, R.1    Robinson, M.2    Gerst, J.E.3
  • 85
    • 79960798816 scopus 로고    scopus 로고
    • SNARE proteins are required for macroautophagy
    • Nair U, Jotwani A, Geng J et al. SNARE proteins are required for macroautophagy. Cell 146(2), 290-302 (2011).
    • (2011) Cell , vol.146 , Issue.2 , pp. 290-302
    • Nair, U.1    Jotwani, A.2    Geng, J.3
  • 86
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • Behrends C, Sowa M, Gygi S, Harper J. Network organization of the human autophagy system. Nature 466(7302), 68-76 (2010).
    • (2010) Nature , vol.466 , Issue.7302 , pp. 68-76
    • Behrends, C.1    Sowa, M.2    Gygi, S.3    Harper, J.4
  • 87
    • 74949090299 scopus 로고    scopus 로고
    • An overview of the molecular mechanism of autophagy
    • Yang Z, Klionsky D. An overview of the molecular mechanism of autophagy. Curr. Top. Microbiol. Immunol. 335, 1-32 (2009).
    • (2009) Curr. Top. Microbiol. Immunol. , vol.335 , pp. 1-32
    • Yang, Z.1    Klionsky, D.2
  • 89
    • 49749148054 scopus 로고    scopus 로고
    • Depalmitoylation of Ykt6 prevents its entry into the multivesicular body pathway
    • Meiringer CT, Auffarth K, Hou H, Ungermann C. Depalmitoylation of Ykt6 prevents its entry into the multivesicular body pathway Traffic 9(9), 1510-1521 (2008).
    • (2008) Traffic , vol.9 , Issue.9 , pp. 1510-1521
    • Meiringer, C.T.1    Auffarth, K.2    Hou, H.3    Ungermann, C.4
  • 90
    • 0034666116 scopus 로고    scopus 로고
    • Cathepsin D defciency induces lysosomal storage with ceroid lipofuscin in mouse CNS neurons
    • Koike M, Nakanishi H, Saftig P et al. Cathepsin D defciency induces lysosomal storage with ceroid lipofuscin in mouse CNS neurons. J. Neurosci. 20(18), 6898-6906 (2000).
    • (2000) J. Neurosci. , vol.20 , Issue.18 , pp. 6898-6906
    • Koike, M.1    Nakanishi, H.2    Saftig, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.