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Volumn 25, Issue 5, 2016, Pages 936-950

Genetic interaction of hnRNPA2B1 and DNAJB6 in a Drosophila model of multisystem proteinopathy

Author keywords

[No Author keywords available]

Indexed keywords

RNA BINDING PROTEIN; CHAPERONE; DNA BINDING PROTEIN; DNAJB6 PROTEIN, HUMAN; DROSOPHILA PROTEIN; HEAT SHOCK PROTEIN 40; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN GROUP A B; HNRNP A2; HRB98DE PROTEIN, DROSOPHILA; NERVE PROTEIN; PROTEIN BINDING; ROX8 PROTEIN, DROSOPHILA; TBPH PROTEIN, DROSOPHILA;

EID: 84962854690     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddv627     Document Type: Article
Times cited : (24)

References (43)
  • 1
    • 41149151436 scopus 로고    scopus 로고
    • Inherited myopathies and muscular dystrophies
    • Cardamone, M., Darras, B.T. and Ryan, M.M. (2008) Inherited myopathies and muscular dystrophies. Semin. Neurol., 28, 250-259.
    • (2008) Semin. Neurol , vol.28 , pp. 250-259
    • Cardamone, M.1    Darras, B.T.2    Ryan, M.M.3
  • 2
    • 84940029424 scopus 로고    scopus 로고
    • Multisystem proteinopathy: intersecting genetics in muscle, bone, and brain degeneration
    • Taylor, J.P. (2015) Multisystem proteinopathy: intersecting genetics in muscle, bone, and brain degeneration. Neurology, 85, 658-660.
    • (2015) Neurology , vol.85 , pp. 658-660
    • Taylor, J.P.1
  • 6
    • 84862151933 scopus 로고    scopus 로고
    • The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease
    • King, O.D., Gitler, A.D. and Shorter, J. (2012) The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease. Brain Res., 1462, 61-80.
    • (2012) Brain Res , vol.1462 , pp. 61-80
    • King, O.D.1    Gitler, A.D.2    Shorter, J.3
  • 7
    • 84944907005 scopus 로고    scopus 로고
    • Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization
    • Molliex, A., Temirov, J., Lee, J., Coughlin, M., Kanagaraj, A.P., Kim, H.J., Mittag, T. and Taylor, J.P. (2015) Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization. Cell, 163, 123-133.
    • (2015) Cell , vol.163 , pp. 123-133
    • Molliex, A.1    Temirov, J.2    Lee, J.3    Coughlin, M.4    Kanagaraj, A.P.5    Kim, H.J.6    Mittag, T.7    Taylor, J.P.8
  • 9
    • 84944884978 scopus 로고    scopus 로고
    • Formation and maturation of phase-separated liquid droplets by RNA-binding proteins
    • Lin, Y., Protter, D.S., Rosen, M.K. and Parker, R. (2015) Formation and maturation of phase-separated liquid droplets by RNA-binding proteins. Mol. Cell, 60, 208-219.
    • (2015) Mol. Cell , vol.60 , pp. 208-219
    • Lin, Y.1    Protter, D.S.2    Rosen, M.K.3    Parker, R.4
  • 10
    • 84879349589 scopus 로고    scopus 로고
    • Eukaryotic stress granules are cleared by autophagy and Cdc48/VCP function
    • Buchan, J.R., Kolaitis, R.M., Taylor, J.P. and Parker, R. (2013) Eukaryotic stress granules are cleared by autophagy and Cdc48/VCP function. Cell, 153, 1461-1474.
    • (2013) Cell , vol.153 , pp. 1461-1474
    • Buchan, J.R.1    Kolaitis, R.M.2    Taylor, J.P.3    Parker, R.4
  • 11
    • 0031469912 scopus 로고    scopus 로고
    • Hsp70 and Hsp40 chaperone activities in the cytoplasm and the nucleus of mammalian cells
    • Michels, A.A., Kanon, B., Konings, A.W., Ohtsuka, K., Bensaude, O. and Kampinga, H.H. (1997) Hsp70 and Hsp40 chaperone activities in the cytoplasm and the nucleus of mammalian cells. J. Biol. Chem., 272, 33283-33289.
    • (1997) J. Biol. Chem , vol.272 , pp. 33283-33289
    • Michels, A.A.1    Kanon, B.2    Konings, A.W.3    Ohtsuka, K.4    Bensaude, O.5    Kampinga, H.H.6
  • 13
    • 84883312999 scopus 로고    scopus 로고
    • ATP-driven molecular chaperone machines
    • Clare, D.K. and Saibil, H.R. (2013) ATP-driven molecular chaperone machines. Biopolymers, 99, 846-859.
    • (2013) Biopolymers , vol.99 , pp. 846-859
    • Clare, D.K.1    Saibil, H.R.2
  • 14
    • 0032568541 scopus 로고    scopus 로고
    • Role of the Jdomain in the cooperation of Hsp40 with Hsp70
    • Greene, M.K., Maskos, K. and Landry, S.J. (1998) Role of the Jdomain in the cooperation of Hsp40 with Hsp70. Proc. Natl Acad. Sci. USA, 95, 6108-6113.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6108-6113
    • Greene, M.K.1    Maskos, K.2    Landry, S.J.3
  • 15
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • Cummings, C.J., Mancini, M.A., Antalffy, B., DeFranco, D.B., Orr, H.T. and Zoghbi, H.Y. (1998) Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nat. Genet., 19, 148-154.
    • (1998) Nat. Genet , vol.19 , pp. 148-154
    • Cummings, C.J.1    Mancini, M.A.2    Antalffy, B.3    DeFranco, D.B.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 17
    • 84874833124 scopus 로고    scopus 로고
    • DNAJ proteins and protein aggregation diseases
    • Kakkar, V., Prins, L.C. and Kampinga, H.H. (2012) DNAJ proteins and protein aggregation diseases. Curr. Top. Med. Chem., 12, 2479-2490.
    • (2012) Curr. Top. Med. Chem , vol.12 , pp. 2479-2490
    • Kakkar, V.1    Prins, L.C.2    Kampinga, H.H.3
  • 18
    • 84905389011 scopus 로고    scopus 로고
    • Myopathy-causing mutations in an HSP40 chaperone disrupt processing of specific client conformers
    • Stein, K.C., Bengoechea, R., Harms, M.B., Weihl, C.C. and True, H.L. (2014) Myopathy-causing mutations in an HSP40 chaperone disrupt processing of specific client conformers. J. Biol. Chem., 289, 21120-21130.
    • (2014) J. Biol. Chem , vol.289 , pp. 21120-21130
    • Stein, K.C.1    Bengoechea, R.2    Harms, M.B.3    Weihl, C.C.4    True, H.L.5
  • 21
    • 84962837583 scopus 로고    scopus 로고
    • Myofibrillar disruption and RNA-binding protein aggregation in a mouse model of limb-girdle muscular dystrophy 1D
    • Bengoechea, R., Pittman, S.K., Tuck, E.P., True, H.L. andWeihl, C.C. (2015) Myofibrillar disruption and RNA-binding protein aggregation in a mouse model of limb-girdle muscular dystrophy 1D. Hum. Mol. Genet., 24, 6588-6602.
    • (2015) Hum. Mol. Genet , vol.24 , pp. 6588-6602
    • Bengoechea, R.1    Pittman, S.K.2    Tuck, E.P.3    True H.L.andWeihl, C.C.4
  • 22
    • 76149120427 scopus 로고    scopus 로고
    • Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery
    • Freibaum, B.D., Chitta, R.K., High, A.A. and Taylor, J.P. (2010) Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery. J. Proteome Res., 9, 1104-1120.
    • (2010) J. Proteome Res , vol.9 , pp. 1104-1120
    • Freibaum, B.D.1    Chitta, R.K.2    High, A.A.3    Taylor, J.P.4
  • 24
    • 78951492184 scopus 로고    scopus 로고
    • Modulation of stress granules and P bodies during dicistrovirus infection
    • Khong, A. and Jan, E. (2011) Modulation of stress granules and P bodies during dicistrovirus infection. J. Virol., 85, 1439-1451.
    • (2011) J. Virol , vol.85 , pp. 1439-1451
    • Khong, A.1    Jan, E.2
  • 34
    • 84878661360 scopus 로고    scopus 로고
    • Stress granules as crucibles of ALS pathogenesis
    • Li, Y.R., King, O.D., Shorter, J. and Gitler, A.D. (2013) Stress granules as crucibles of ALS pathogenesis. J. Cell Biol., 201, 361-372.
    • (2013) J. Cell Biol , vol.201 , pp. 361-372
    • Li, Y.R.1    King, O.D.2    Shorter, J.3    Gitler, A.D.4
  • 36
    • 84882801549 scopus 로고    scopus 로고
    • Altered ribostasis: RNA-protein granules in degenerative disorders
    • Ramaswami, M., Taylor, J.P. and Parker, R. (2013) Altered ribostasis: RNA-protein granules in degenerative disorders. Cell, 154, 727-736.
    • (2013) Cell , vol.154 , pp. 727-736
    • Ramaswami, M.1    Taylor, J.P.2    Parker, R.3
  • 37
    • 0027987996 scopus 로고
    • NMR structure determination of the Escherichia coli DnaJ molecular chaperone: secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain
    • Szyperski, T., Pellecchia, M., Wall, D., Georgopoulos, C. and Wuthrich, K. (1994) NMR structure determination of the Escherichia coli DnaJ molecular chaperone: secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain. Proc. Natl Acad. Sci. USA, 91, 11343-11347.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 11343-11347
    • Szyperski, T.1    Pellecchia, M.2    Wall, D.3    Georgopoulos, C.4    Wuthrich, K.5
  • 38
    • 0030930513 scopus 로고    scopus 로고
    • The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiae
    • Corsi, A.K. and Schekman, R. (1997) The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiae. J. Cell Biol., 137, 1483-1493.
    • (1997) J. Cell Biol , vol.137 , pp. 1483-1493
    • Corsi, A.K.1    Schekman, R.2
  • 39
    • 33751265748 scopus 로고    scopus 로고
    • The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones
    • Qiu, X.B., Shao, Y.M., Miao, S. and Wang, L. (2006) The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones. Cell. Mol. Life Sci., 63, 2560-2570.
    • (2006) Cell. Mol. Life Sci , vol.63 , pp. 2560-2570
    • Qiu, X.B.1    Shao, Y.M.2    Miao, S.3    Wang, L.4
  • 40
    • 77957244650 scopus 로고    scopus 로고
    • Search and clustering orders of magnitude faster than BLAST
    • Edgar, R.C. (2010) Search and clustering orders of magnitude faster than BLAST. Bioinformatics, 26, 2460-2461.
    • (2010) Bioinformatics , vol.26 , pp. 2460-2461
    • Edgar, R.C.1
  • 41
    • 68049142320 scopus 로고    scopus 로고
    • Multiple alignment of DNA sequences with MAFFT
    • Katoh, K., Asimenos, G. and Toh, H. (2009) Multiple alignment of DNA sequences with MAFFT. Methods Mol. Biol., 537, 39-64.
    • (2009) Methods Mol. Biol , vol.537 , pp. 39-64
    • Katoh, K.1    Asimenos, G.2    Toh, H.3
  • 42
    • 34547840166 scopus 로고    scopus 로고
    • SQUINT: a multiple alignment program and editor
    • Goode, M.G. and Rodrigo, A.G. (2007) SQUINT: a multiple alignment program and editor. Bioinformatics, 23, 1553-1555.
    • (2007) Bioinformatics , vol.23 , pp. 1553-1555
    • Goode, M.G.1    Rodrigo, A.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.