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Volumn 293, Issue , 2015, Pages 157-170

Proteomic analyses reveal that loss of TDP-43 affects RNA processing and intracellular transport

Author keywords

Amyotrophic lateral sclerosis; Comparative proteomics; Frontotemporal lobar degeneration; Intracellular transport; RanBP1; TDP 43

Indexed keywords

BINDING PROTEIN; CHROMOGRANIN B; DNA METHYLTRANSFERASE 3A; PROTEOME; RAN BINDING PROTEIN 1; RNA; TAR DNA BINDING PROTEIN; TRANSPORTIN 1; UNCLASSIFIED DRUG; CARRIER PROTEIN; DNA (CYTOSINE 5) METHYLTRANSFERASE; DNA BINDING PROTEIN; KARYOPHERIN BETA; NUCLEAR PROTEIN; RAN-BINDING PROTEIN 1; TDP-43 PROTEIN, HUMAN; TNPO1 PROTEIN, HUMAN;

EID: 84925307620     PISSN: 03064522     EISSN: 18737544     Source Type: Journal    
DOI: 10.1016/j.neuroscience.2015.02.046     Document Type: Article
Times cited : (41)

References (71)
  • 1
    • 33745277599 scopus 로고    scopus 로고
    • Cis-requirement for the maintenance of round spermatid-specific transcription
    • Acharya K.K., Govind C.K., Shore A.N., Stoler M.H., Reddi P.P. Cis-requirement for the maintenance of round spermatid-specific transcription. Dev Biol 2006, 295:781-790.
    • (2006) Dev Biol , vol.295 , pp. 781-790
    • Acharya, K.K.1    Govind, C.K.2    Shore, A.N.3    Stoler, M.H.4    Reddi, P.P.5
  • 3
    • 41649106307 scopus 로고    scopus 로고
    • TDP-43 regulates retinoblastoma protein phosphorylation through the repression of cyclin-dependent kinase 6 expression
    • Ayala Y.M., Misteli T., Baralle F.E. TDP-43 regulates retinoblastoma protein phosphorylation through the repression of cyclin-dependent kinase 6 expression. Proc Natl Acad Sci U S A 2008, 105:3785-3789.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 3785-3789
    • Ayala, Y.M.1    Misteli, T.2    Baralle, F.E.3
  • 6
    • 0028937195 scopus 로고
    • Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1
    • Bischoff F.R., Krebber H., Smirnova E., Dong W., Ponstingl H. Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1. EMBO J 1995, 14:705-715.
    • (1995) EMBO J , vol.14 , pp. 705-715
    • Bischoff, F.R.1    Krebber, H.2    Smirnova, E.3    Dong, W.4    Ponstingl, H.5
  • 7
    • 84455169931 scopus 로고    scopus 로고
    • Regulation of autophagy by neuropathological protein TDP-43
    • Bose J.K., Huang C.C., Shen C.K. Regulation of autophagy by neuropathological protein TDP-43. J Biol Chem 2011, 286:44441-44448.
    • (2011) J Biol Chem , vol.286 , pp. 44441-44448
    • Bose, J.K.1    Huang, C.C.2    Shen, C.K.3
  • 9
    • 0035965309 scopus 로고    scopus 로고
    • Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9
    • Buratti E., Baralle F.E. Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9. J Biol Chem 2001, 276:36337-36343.
    • (2001) J Biol Chem , vol.276 , pp. 36337-36343
    • Buratti, E.1    Baralle, F.E.2
  • 11
    • 84907697655 scopus 로고    scopus 로고
    • Motor neuron expression of the voltage-gated calcium channel cacophony restores locomotion defects in a Drosophila, TDP-43 loss of function model of ALS
    • Chang J.C., Hazelett D.J., Stewart J.A., Morton D.B. Motor neuron expression of the voltage-gated calcium channel cacophony restores locomotion defects in a Drosophila, TDP-43 loss of function model of ALS. Brain Res 2014, 1584:39-51.
    • (2014) Brain Res , vol.1584 , pp. 39-51
    • Chang, J.C.1    Hazelett, D.J.2    Stewart, J.A.3    Morton, D.B.4
  • 12
    • 81255143014 scopus 로고    scopus 로고
    • Epigenetic regulation of motor neuron cell death through DNA methylation
    • Chestnut B.A., Chang Q., Price A., Lesuisse C., Wong M., Martin L.J. Epigenetic regulation of motor neuron cell death through DNA methylation. J Neurosci 2011, 31:16619-16636.
    • (2011) J Neurosci , vol.31 , pp. 16619-16636
    • Chestnut, B.A.1    Chang, Q.2    Price, A.3    Lesuisse, C.4    Wong, M.5    Martin, L.J.6
  • 18
    • 80855138138 scopus 로고    scopus 로고
    • Rodent models of TDP-43 proteinopathy: investigating the mechanisms of TDP-43-mediated neurodegeneration
    • Gendron T.F., Petrucelli L. Rodent models of TDP-43 proteinopathy: investigating the mechanisms of TDP-43-mediated neurodegeneration. J Mol Neurosci 2011, 45:486-499.
    • (2011) J Mol Neurosci , vol.45 , pp. 486-499
    • Gendron, T.F.1    Petrucelli, L.2
  • 21
    • 84883348833 scopus 로고    scopus 로고
    • Comparison of parallel high-throughput RNA sequencing between knockout of TDP-43 and its overexpression reveals primarily nonreciprocal and nonoverlapping gene expression changes in the central nervous system of Drosophila
    • Hazelett D.J., Chang J.C., Lakeland D.L., Morton D.B. Comparison of parallel high-throughput RNA sequencing between knockout of TDP-43 and its overexpression reveals primarily nonreciprocal and nonoverlapping gene expression changes in the central nervous system of Drosophila. G3 (Bethesda) 2012, 2:789-802.
    • (2012) G3 (Bethesda) , vol.2 , pp. 789-802
    • Hazelett, D.J.1    Chang, J.C.2    Lakeland, D.L.3    Morton, D.B.4
  • 23
    • 58549112996 scopus 로고    scopus 로고
    • Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists
    • Huang da W., Sherman B.T., Lempicki R.A. Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists. Nucleic Acids Res 2009, 37:1-13.
    • (2009) Nucleic Acids Res , vol.37 , pp. 1-13
    • Huang da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 24
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang da W., Sherman B.T., Lempicki R.A. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat Protoc 2009, 4:44-57.
    • (2009) Nat Protoc , vol.4 , pp. 44-57
    • Huang da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 26
    • 0030856315 scopus 로고    scopus 로고
    • The asymmetric distribution of the constituents of the Ran system is essential for transport into and out of the nucleus
    • Izaurralde E., Kutay U., von Kobbe C., Mattaj I.W., Gorlich D. The asymmetric distribution of the constituents of the Ran system is essential for transport into and out of the nucleus. EMBO J 1997, 16:6535-6547.
    • (1997) EMBO J , vol.16 , pp. 6535-6547
    • Izaurralde, E.1    Kutay, U.2    von Kobbe, C.3    Mattaj, I.W.4    Gorlich, D.5
  • 29
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller A., Nesvizhskii A.I., Kolker E., Aebersold R. Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal Chem 2002, 74:5383-5392.
    • (2002) Anal Chem , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 32
    • 67049158431 scopus 로고    scopus 로고
    • Proteolytic fragments of chromogranins A and B represent major soluble components of chromaffin granules, illustrated by two-dimensional proteomics with NH(2)-terminal Edman peptide sequencing and MALDI-TOF MS
    • Lee J.C., Hook V. Proteolytic fragments of chromogranins A and B represent major soluble components of chromaffin granules, illustrated by two-dimensional proteomics with NH(2)-terminal Edman peptide sequencing and MALDI-TOF MS. Biochemistry 2009, 48:5254-5262.
    • (2009) Biochemistry , vol.48 , pp. 5254-5262
    • Lee, J.C.1    Hook, V.2
  • 33
    • 84885358733 scopus 로고    scopus 로고
    • Disease animal models of TDP-43 proteinopathy and their pre-clinical applications
    • Liu Y.C., Chiang P.M., Tsai K.J. Disease animal models of TDP-43 proteinopathy and their pre-clinical applications. Int J Mol Sci 2013, 14:20079-20111.
    • (2013) Int J Mol Sci , vol.14 , pp. 20079-20111
    • Liu, Y.C.1    Chiang, P.M.2    Tsai, K.J.3
  • 34
    • 36248944562 scopus 로고    scopus 로고
    • Cerebrospinal fluid concentrations of peptides derived from chromogranin B and secretogranin II are decreased in multiple sclerosis
    • Mattsson N., Ruetschi U., Podust V.N., Stridsberg M., Li S., Andersen O., Haghighi S., Blennow K., Zetterberg H. Cerebrospinal fluid concentrations of peptides derived from chromogranin B and secretogranin II are decreased in multiple sclerosis. J Neurochem 2007, 103:1932-1939.
    • (2007) J Neurochem , vol.103 , pp. 1932-1939
    • Mattsson, N.1    Ruetschi, U.2    Podust, V.N.3    Stridsberg, M.4    Li, S.5    Andersen, O.6    Haghighi, S.7    Blennow, K.8    Zetterberg, H.9
  • 35
    • 0027714921 scopus 로고
    • Inhibition of nuclear protein import by nonhydrolyzable analogues of GTP and identification of the small GTPase Ran/TC4 as an essential transport factor
    • Melchior F., Paschal B., Evans J., Gerace L. Inhibition of nuclear protein import by nonhydrolyzable analogues of GTP and identification of the small GTPase Ran/TC4 as an essential transport factor. J Cell Biol 1993, 123:1649-1659.
    • (1993) J Cell Biol , vol.123 , pp. 1649-1659
    • Melchior, F.1    Paschal, B.2    Evans, J.3    Gerace, L.4
  • 36
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii A.I., Keller A., Kolker E., Aebersold R. A statistical model for identifying proteins by tandem mass spectrometry. Anal Chem 2003, 75:4646-4658.
    • (2003) Anal Chem , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 39
    • 77953019135 scopus 로고    scopus 로고
    • Nuclear import impairment causes cytoplasmic trans-activation response DNA-binding protein accumulation and is associated with frontotemporal lobar degeneration
    • Nishimura A.L., Zupunski V., Troakes C., Kathe C., Fratta P., Howell M., Gallo J.M., Hortobagyi T., Shaw C.E., Rogelj B. Nuclear import impairment causes cytoplasmic trans-activation response DNA-binding protein accumulation and is associated with frontotemporal lobar degeneration. Brain 2010, 133:1763-1771.
    • (2010) Brain , vol.133 , pp. 1763-1771
    • Nishimura, A.L.1    Zupunski, V.2    Troakes, C.3    Kathe, C.4    Fratta, P.5    Howell, M.6    Gallo, J.M.7    Hortobagyi, T.8    Shaw, C.E.9    Rogelj, B.10
  • 40
    • 0029066110 scopus 로고
    • Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs
    • Ou S.H., Wu F., Harrich D., Garcia-Martinez L.F., Gaynor R.B. Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs. J Virol 1995, 69:3584-3596.
    • (1995) J Virol , vol.69 , pp. 3584-3596
    • Ou, S.H.1    Wu, F.2    Harrich, D.3    Garcia-Martinez, L.F.4    Gaynor, R.B.5
  • 41
    • 84879607516 scopus 로고    scopus 로고
    • Tat-activating regulatory DNA-binding protein regulates glycolysis in hepatocellular carcinoma by regulating the platelet isoform of phosphofructokinase through microRNA 520
    • Park Y.Y., Kim S.B., Han H.D., Sohn B.H., Kim J.H., Liang J., Lu Y., Rodriguez-Aguayo C., Lopez-Berestein G., Mills G.B., Sood A.K., Lee J.S. Tat-activating regulatory DNA-binding protein regulates glycolysis in hepatocellular carcinoma by regulating the platelet isoform of phosphofructokinase through microRNA 520. Hepatology 2013, 58:182-191.
    • (2013) Hepatology , vol.58 , pp. 182-191
    • Park, Y.Y.1    Kim, S.B.2    Han, H.D.3    Sohn, B.H.4    Kim, J.H.5    Liang, J.6    Lu, Y.7    Rodriguez-Aguayo, C.8    Lopez-Berestein, G.9    Mills, G.B.10    Sood, A.K.11    Lee, J.S.12
  • 42
    • 84948708727 scopus 로고    scopus 로고
    • Ranbp1, deleted in DiGeorge/22q11.2 deletion syndrome, is a microcephaly gene that selectively disrupts Layer 2/3 Cortical Projection Neuron Generation
    • Paronett E.M., Meechan D.W., Karpinski B.A., LaMantia A.S., Maynard T.M. Ranbp1, deleted in DiGeorge/22q11.2 deletion syndrome, is a microcephaly gene that selectively disrupts Layer 2/3 Cortical Projection Neuron Generation. Cereb Cortex 2014.
    • (2014) Cereb Cortex
    • Paronett, E.M.1    Meechan, D.W.2    Karpinski, B.A.3    LaMantia, A.S.4    Maynard, T.M.5
  • 49
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A., Wilm M., Vorm O., Mann M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem 1996, 68:850-858.
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 52
    • 80052936462 scopus 로고    scopus 로고
    • Pathological hallmarks of amyotrophic lateral sclerosis/frontotemporal lobar degeneration in transgenic mice produced with TDP-43 genomic fragments
    • Swarup V., Phaneuf D., Bareil C., Robertson J., Rouleau G.A., Kriz J., Julien J.P. Pathological hallmarks of amyotrophic lateral sclerosis/frontotemporal lobar degeneration in transgenic mice produced with TDP-43 genomic fragments. Brain 2011, 134:2610-2626.
    • (2011) Brain , vol.134 , pp. 2610-2626
    • Swarup, V.1    Phaneuf, D.2    Bareil, C.3    Robertson, J.4    Rouleau, G.A.5    Kriz, J.6    Julien, J.P.7
  • 54
    • 36549085093 scopus 로고    scopus 로고
    • RANBP1 localizes a subset of mitotic regulatory factors on spindle microtubules and regulates chromosome segregation in human cells
    • Tedeschi A., Ciciarello M., Mangiacasale R., Roscioli E., Rensen W.M., Lavia P. RANBP1 localizes a subset of mitotic regulatory factors on spindle microtubules and regulates chromosome segregation in human cells. J Cell Sci 2007, 120:3748-3761.
    • (2007) J Cell Sci , vol.120 , pp. 3748-3761
    • Tedeschi, A.1    Ciciarello, M.2    Mangiacasale, R.3    Roscioli, E.4    Rensen, W.M.5    Lavia, P.6
  • 56
    • 84880177442 scopus 로고    scopus 로고
    • Transportin 1 colocalization with Fused in Sarcoma (FUS) inclusions is not characteristic for amyotrophic lateral sclerosis-FUS confirming disrupted nuclear import of mutant FUS and distinguishing it from frontotemporal lobar degeneration with FUS inclusions
    • Troakes C., Hortobagyi T., Vance C., Al-Sarraj S., Rogelj B., Shaw C.E. Transportin 1 colocalization with Fused in Sarcoma (FUS) inclusions is not characteristic for amyotrophic lateral sclerosis-FUS confirming disrupted nuclear import of mutant FUS and distinguishing it from frontotemporal lobar degeneration with FUS inclusions. Neuropathol Appl Neurobiol 2013, 39:553-561.
    • (2013) Neuropathol Appl Neurobiol , vol.39 , pp. 553-561
    • Troakes, C.1    Hortobagyi, T.2    Vance, C.3    Al-Sarraj, S.4    Rogelj, B.5    Shaw, C.E.6
  • 60
    • 73949134014 scopus 로고    scopus 로고
    • Tar DNA binding protein of 43kDa (TDP-43), 14-3-3 proteins and copper/zinc superoxide dismutase (SOD1) interact to modulate NFL mRNA stability. Implications for altered RNA processing in amyotrophic lateral sclerosis (ALS)
    • Volkening K., Leystra-Lantz C., Yang W., Jaffee H., Strong M.J. Tar DNA binding protein of 43kDa (TDP-43), 14-3-3 proteins and copper/zinc superoxide dismutase (SOD1) interact to modulate NFL mRNA stability. Implications for altered RNA processing in amyotrophic lateral sclerosis (ALS). Brain Res 2009, 1305:168-182.
    • (2009) Brain Res , vol.1305 , pp. 168-182
    • Volkening, K.1    Leystra-Lantz, C.2    Yang, W.3    Jaffee, H.4    Strong, M.J.5
  • 61
    • 73249152831 scopus 로고    scopus 로고
    • TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration
    • Wegorzewska I., Bell S., Cairns N.J., Miller T.M., Baloh R.H. TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration. Proc Natl Acad Sci U S A 2009, 106:18809-18814.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 18809-18814
    • Wegorzewska, I.1    Bell, S.2    Cairns, N.J.3    Miller, T.M.4    Baloh, R.H.5
  • 62
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
    • Wilm M., Shevchenko A., Houthaeve T., Breit S., Schweigerer L., Fotsis T., Mann M. Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry. Nature 1996, 379:466-469.
    • (1996) Nature , vol.379 , pp. 466-469
    • Wilm, M.1    Shevchenko, A.2    Houthaeve, T.3    Breit, S.4    Schweigerer, L.5    Fotsis, T.6    Mann, M.7
  • 63
    • 44749091997 scopus 로고    scopus 로고
    • Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation
    • Winton M.J., Igaz L.M., Wong M.M., Kwong L.K., Trojanowski J.Q., Lee V.M. Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation. J Biol Chem 2008, 283:13302-13309.
    • (2008) J Biol Chem , vol.283 , pp. 13302-13309
    • Winton, M.J.1    Igaz, L.M.2    Wong, M.M.3    Kwong, L.K.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 64
    • 84891533924 scopus 로고    scopus 로고
    • Mitochondrial DNMT3A and DNA methylation in skeletal muscle and CNS of transgenic mouse models of ALS
    • Wong M., Gertz B., Chestnut B.A., Martin L.J. Mitochondrial DNMT3A and DNA methylation in skeletal muscle and CNS of transgenic mouse models of ALS. Front Cell Neurosci 2013, 7:279.
    • (2013) Front Cell Neurosci , vol.7 , pp. 279
    • Wong, M.1    Gertz, B.2    Chestnut, B.A.3    Martin, L.J.4
  • 65
    • 84865028374 scopus 로고    scopus 로고
    • Targeted depletion of TDP-43 expression in the spinal cord motor neurons leads to the development of amyotrophic lateral sclerosis-like phenotypes in mice
    • Wu L.S., Cheng W.C., Shen C.K. Targeted depletion of TDP-43 expression in the spinal cord motor neurons leads to the development of amyotrophic lateral sclerosis-like phenotypes in mice. J Biol Chem 2012, 287:27335-27344.
    • (2012) J Biol Chem , vol.287 , pp. 27335-27344
    • Wu, L.S.1    Cheng, W.C.2    Shen, C.K.3
  • 67
    • 77649109602 scopus 로고    scopus 로고
    • Proteomics analysis of the cardiac myofilament subproteome reveals dynamic alterations in phosphatase subunit distribution
    • Yin X., Cuello F., Mayr U., Hao Z., Hornshaw M., Ehler E., Avkiran M., Mayr M. Proteomics analysis of the cardiac myofilament subproteome reveals dynamic alterations in phosphatase subunit distribution. Mol Cell Proteomics 2010, 9:497-509.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 497-509
    • Yin, X.1    Cuello, F.2    Mayr, U.3    Hao, Z.4    Hornshaw, M.5    Ehler, E.6    Avkiran, M.7    Mayr, M.8
  • 69
    • 84863307704 scopus 로고    scopus 로고
    • Neurodegeneration-associated TDP-43 interacts with fragile X mental retardation protein (FMRP)/Staufen (STAU1) and regulates SIRT1 expression in neuronal cells
    • Yu Z., Fan D., Gui B., Shi L., Xuan C., Shan L., Wang Q., Shang Y., Wang Y. Neurodegeneration-associated TDP-43 interacts with fragile X mental retardation protein (FMRP)/Staufen (STAU1) and regulates SIRT1 expression in neuronal cells. J Biol Chem 2012, 287:22560-22572.
    • (2012) J Biol Chem , vol.287 , pp. 22560-22572
    • Yu, Z.1    Fan, D.2    Gui, B.3    Shi, L.4    Xuan, C.5    Shan, L.6    Wang, Q.7    Shang, Y.8    Wang, Y.9


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