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Protein-RNA Networks Regulated by Normal and ALS-Associated Mutant HNRNPA2B1 in the Nervous System

Martinez, Fernando J., Pratt, Gabriel A., Van Nostrand, Eric L., Batra, Ranjan, Huelga, Stephanie C., Kapeli, Katannya, Freese, Peter, Chun, Seung J., Ling, Karen, Gelboin-Burkhart, Chelsea, Fijany, Layla, Wang, Harrison C., Nussbacher, Julia K., Broski, Sara M., Kim, Hong Joo, Lardelli, Rea, Sundararaman, Balaji, Donohue, John P., Javaherian, Ashkan, Lykke-Andersen, Jens, Finkbeiner, Steven, Bennett, C. Frank, Ares, Manuel, Burge, Christopher B., Taylor, J. Paul, Rigo, Frank, Yeo, Gene W.·2016·Neuron
DOI 10.1016/j.neuron.2016.09.050PMC PMC5123850
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  1. Ainger, 1997, Transport and localization elements in myelin basic protein mRNA, J. Cell Biol., 138, 1077, 10.1083/jcb.138.5.1077 · DOI
  2. Belzil, 2013, RNA-mediated toxicity in neurodegenerative disease, Mol. Cell. Neurosci., 56, 406, 10.1016/j.mcn.2012.12.006 · DOI
  3. Berson, 2012, Cholinergic-associated loss of hnRNP-A/B in Alzheimer’s disease impairs cortical splicing and cognitive function in mice, EMBO Mol. Med., 4, 730, 10.1002/emmm.201100995 · DOI
  4. Burkhardt, 2013, A cellular model for sporadic ALS using patient-derived induced pluripotent stem cells, Mol. Cell. Neurosci., 56, 355, 10.1016/j.mcn.2013.07.007 · DOI
  5. Burnet, 2008, D-amino acid oxidase activity and expression are increased in schizophrenia, Mol. Psychiatry, 13, 658, 10.1038/mp.2008.47 · DOI
  6. Clower, 2010, The alternative splicing repressors hnRNP A1/A2 and PTB influence pyruvate kinase isoform expression and cell metabolism, Proc. Natl. Acad. Sci. USA, 107, 1894, 10.1073/pnas.0914845107 · DOI · Paper page
  7. Couthouis, 2011, A yeast functional screen predicts new candidate ALS disease genes, Proc. Natl. Acad. Sci. USA, 108, 20881, 10.1073/pnas.1109434108 · DOI
  8. Du, 2015, Generation and expansion of highly pure motor neuron progenitors from human pluripotent stem cells, Nat. Commun., 6, 6626, 10.1038/ncomms7626 · DOI
  9. Fähling, 2006, Heterogeneous nuclear ribonucleoprotein-A2/B1 modulate collagen prolyl 4-hydroxylase, alpha (I) mRNA stability, J. Biol. Chem., 281, 9279, 10.1074/jbc.M510925200 · DOI
  10. Horiike, 1994, D-amino-acid oxidase is confined to the lower brain stem and cerebellum in rat brain: regional differentiation of astrocytes, Brain Res., 652, 297, 10.1016/0006-8993(94)90240-2 · DOI
  11. Huelga, 2012, Integrative genome-wide analysis reveals cooperative regulation of alternative splicing by hnRNP proteins, Cell Rep., 1, 167, 10.1016/j.celrep.2012.02.001 · DOI · Paper page
  12. Huppertz, 2014, iCLIP: protein-RNA interactions at nucleotide resolution, Methods, 65, 274, 10.1016/j.ymeth.2013.10.011 · DOI
  13. Hutchison, 2002, Distinct sets of adjacent heterogeneous nuclear ribonucleoprotein (hnRNP) A1/A2 binding sites control 5′ splice site selection in the hnRNP A1 mRNA precursor, J. Biol. Chem., 277, 29745, 10.1074/jbc.M203633200 · DOI
  14. Iguchi, 2013, Loss of TDP-43 causes age-dependent progressive motor neuron degeneration, Brain, 136, 1371, 10.1093/brain/awt029 · DOI
  15. Kabashi, 2008, TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis, Nat. Genet., 40, 572, 10.1038/ng.132 · DOI · Paper page
  16. Kapeli, 2016, Distinct and shared functions of ALS-associated proteins TDP-43, FUS and TAF15 revealed by multisystem analyses, Nat. Commun., 7, 12143, 10.1038/ncomms12143 · DOI
  17. Kawazoe, 2006, Crystal structure of human D-amino acid oxidase: context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring, Protein Sci., 15, 2708, 10.1110/ps.062421606 · DOI
  18. Kedersha, 2000, Dynamic shuttling of TIA-1 accompanies the recruitment of mRNA to mammalian stress granules, J. Cell Biol., 151, 1257, 10.1083/jcb.151.6.1257 · DOI
  19. Kim, 2013, Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS, Nature, 495, 467, 10.1038/nature11922 · DOI
  20. Kosturko, 2006, Heterogeneous nuclear ribonucleoprotein (hnRNP) E1 binds to hnRNP A2 and inhibits translation of A2 response element mRNAs, Mol. Biol. Cell, 17, 3521, 10.1091/mbc.E05-10-0946 · DOI
  21. Kosuge, 2009, Characterization of chronic glutamate-mediated motor neuron toxicity in organotypic spinal cord culture prepared from ALS model mice, Neurosci. Lett., 454, 165, 10.1016/j.neulet.2009.03.017 · DOI
  22. Lagier-Tourenne, 2010, TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration, Hum. Mol. Genet., 19, R46, 10.1093/hmg/ddq137 · DOI · Paper page
  23. Lagier-Tourenne, 2012, Divergent roles of ALS-linked proteins FUS/TLS and TDP-43 intersect in processing long pre-mRNAs, Nat. Neurosci., 15, 1488, 10.1038/nn.3230 · DOI
  24. Lalmansingh, 2011, TDP-43 is a transcriptional repressor: the testis-specific mouse acrv1 gene is a TDP-43 target in vivo, J. Biol. Chem., 286, 10970, 10.1074/jbc.M110.166587 · DOI
  25. Lambert, 2014, RNA Bind-n-Seq: quantitative assessment of the sequence and structural binding specificity of RNA binding proteins, Mol. Cell, 54, 887, 10.1016/j.molcel.2014.04.016 · DOI
  26. Liu-Yesucevitz, 2010, Tar DNA binding protein-43 (TDP-43) associates with stress granules: analysis of cultured cells and pathological brain tissue, PLoS ONE, 5, e13250, 10.1371/journal.pone.0013250 · DOI
  27. Mackenzie, 2007, Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations, Ann. Neurol., 61, 427, 10.1002/ana.21147 · DOI · Paper page
  28. McGlincy, 2010, Expression proteomics of UPF1 knockdown in HeLa cells reveals autoregulation of hnRNP A2/B1 mediated by alternative splicing resulting in nonsense-mediated mRNA decay, BMC Genomics, 11, 565, 10.1186/1471-2164-11-565 · DOI
  29. Mitchell, 2010, Familial amyotrophic lateral sclerosis is associated with a mutation in D-amino acid oxidase, Proc. Natl. Acad. Sci. USA, 107, 7556, 10.1073/pnas.0914128107 · DOI
  30. Mohagheghi, 2016, TDP-43 functions within a network of hnRNP proteins to inhibit the production of a truncated human SORT1 receptor, Hum. Mol. Genet., 25, 534, 10.1093/hmg/ddv491 · DOI
  31. Molliex, 2015, Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization, Cell, 163, 123, 10.1016/j.cell.2015.09.015 · DOI · Paper page
  32. Paul, 2014, The role of D-serine and glycine as co-agonists of NMDA receptors in motor neuron degeneration and amyotrophic lateral sclerosis (ALS), Front. Synaptic Neurosci., 6, 10, 10.3389/fnsyn.2014.00010 · DOI
  33. Paul, 2014, Pathogenic effects of amyotrophic lateral sclerosis-linked mutation in D-amino acid oxidase are mediated by D-serine, Neurobiol. Aging, 35, 876, 10.1016/j.neurobiolaging.2013.09.005 · DOI
  34. Polymenidou, 2012, Misregulated RNA processing in amyotrophic lateral sclerosis, Brain Res., 1462, 3, 10.1016/j.brainres.2012.02.059 · DOI · Paper page
  35. Sasabe, 2007, D-serine is a key determinant of glutamate toxicity in amyotrophic lateral sclerosis, EMBO J., 26, 4149, 10.1038/sj.emboj.7601840 · DOI
  36. Sasabe, 2012, D-amino acid oxidase controls motoneuron degeneration through D-serine, Proc. Natl. Acad. Sci. USA, 109, 627, 10.1073/pnas.1114639109 · DOI
  37. Scekic-Zahirovic, 2016, Toxic gain of function from mutant FUS protein is crucial to trigger cell autonomous motor neuron loss, EMBO J., 35, 1077, 10.15252/embj.201592559 · DOI
  38. Schwartz, 2012, FUS binds the CTD of RNA polymerase II and regulates its phosphorylation at Ser2, Genes Dev., 26, 2690, 10.1101/gad.204602.112 · DOI
  39. Shan, 2003, A molecular mechanism for mRNA trafficking in neuronal dendrites, J. Neurosci., 23, 8859, 10.1523/JNEUROSCI.23-26-08859.2003 · DOI
  40. Siomi, 1997, Transportin-mediated nuclear import of heterogeneous nuclear RNP proteins, J. Cell Biol., 138, 1181, 10.1083/jcb.138.6.1181 · DOI
  41. Skibinski, 2013, Longitudinal measures of proteostasis in live neurons: features that determine fate in models of neurodegenerative disease, FEBS Lett., 587, 1139, 10.1016/j.febslet.2013.02.043 · DOI
  42. Sofola, 2007, RNA-binding proteins hnRNP A2/B1 and CUGBP1 suppress fragile X CGG premutation repeat-induced neurodegeneration in a Drosophila model of FXTAS, Neuron, 55, 565, 10.1016/j.neuron.2007.07.021 · DOI
  43. Sun, 2015, ALS-causative mutations in FUS/TLS confer gain and loss of function by altered association with SMN and U1-snRNP, Nat. Commun., 6, 6171, 10.1038/ncomms7171 · DOI
  44. Thompson, 2012, Paradoxical roles of serine racemase and D-serine in the G93A mSOD1 mouse model of amyotrophic lateral sclerosis, J. Neurochem., 120, 598, 10.1111/j.1471-4159.2011.07601.x · DOI
  45. Udan-Johns, 2014, Prion-like nuclear aggregation of TDP-43 during heat shock is regulated by HSP40/70 chaperones, Hum. Mol. Genet., 23, 157, 10.1093/hmg/ddt408 · DOI
  46. Van Deerlin, 2008, TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: a genetic and histopathological analysis, Lancet Neurol., 7, 409, 10.1016/S1474-4422(08)70071-1 · DOI · Paper page
  47. Van Nostrand, 2016, Robust transcriptome-wide discovery of RNA-binding protein binding sites with enhanced CLIP (eCLIP), Nat. Methods, 13, 508, 10.1038/nmeth.3810 · DOI · Paper page
  48. Vance, 2009, Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6, Science, 323, 1208, 10.1126/science.1165942 · DOI
  49. Wu, 2012, 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., 287, 27335, 10.1074/jbc.M112.359000 · DOI
  50. Xia, 2014, Dynamic analyses of alternative polyadenylation from RNA-seq reveal a 3′-UTR landscape across seven tumour types, Nat. Commun., 5, 5274, 10.1038/ncomms6274 · DOI
  51. Xiang, 2015, The LC domain of hnRNPA2 adopts similar conformations in hydrogel polymers, liquid-like droplets, and nuclei, Cell, 163, 829, 10.1016/j.cell.2015.10.040 · DOI
  52. Yang, 2013, The DAO gene is associated with schizophrenia and interacts with other genes in the Taiwan Han Chinese population, PLoS ONE, 8, e60099, 10.1371/journal.pone.0060099 · DOI
  53. Yang, 2014, Partial loss of TDP-43 function causes phenotypes of amyotrophic lateral sclerosis, Proc. Natl. Acad. Sci. USA, 111, E1121, 10.1073/pnas.1322641111 · DOI
  54. Zisoulis, 2010, Comprehensive discovery of endogenous Argonaute binding sites in Caenorhabditis elegans, Nat. Struct. Mol. Biol., 17, 173, 10.1038/nsmb.1745 · DOI

Cited by

Metadata

Authors
Martinez, F. J., Pratt, G. A., Van Nostrand, E. L., Batra, R., Huelga, S. C., Kapeli, K., Freese, P., Chun, S. J., Ling, K., Gelboin-Burkhart, C., Fijany, L., Wang, H. C., Nussbacher, J. K., Broski, S. M., Kim, H. J., Lardelli, R., Sundararaman, B., Donohue, J. P., Javaherian, A., Lykke-Andersen, J., Finkbeiner, S., Bennett, C. F., Ares, M., Burge, C. B., Taylor, J. P., Rigo, F., & Yeo, G. W.
Venue
Neuron
Publisher
Elsevier BV
Published
2016-11
Volume
92
Issue
4
Pages
780-795
ISSN
0896-6273
DOI
10.1016/j.neuron.2016.09.050
PMC
PMC5123850
Cited by
185
References
11
Language
en
Licence
Funders
  • National Institute of General Medical Sciences (T32GM008666)
  • NIH (HG004659, NS075449, U54HG007005)
  • California Institute of Regenerative Medicine (RB3-05009, RB4-06045)
  • ALS Association (VC8K27)

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