Ubiquilin-2 (UBQLN2) binds with high affinity to the C-terminal region of TDP-43 and modulates TDP-43 levels in H4 cells: Characterization of inhibition by nucleic acids and 4-aminoquinolines

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1834, Issue 6, 2013, Pages 964-971

  Cassel, Joel A ^a   Reitz, Allen B ^a  

^a Pennsylvania Biotechnology Center   (United States)

Author keywords

4 Aminoquinoline; Protein protein interaction; TDP 43; UBQLN2

Indexed keywords

4 AMINOQUINOLINE; BINDING PROTEIN; OLIGONUCLEOTIDE; TAR DNA BINDING PROTEIN; UBIQUILIN 2; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; GENE OVEREXPRESSION; GLIOMA; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; NEUROTOXICITY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN INTERACTION;

AMINOQUINOLINES; APTAMERS, NUCLEOTIDE; CELL CYCLE PROTEINS; CELL LINE, TUMOR; DNA-BINDING PROTEINS; HUMANS; IMMUNOPRECIPITATION; MUTATION; NUCLEIC ACIDS; PEPTIDE FRAGMENTS; PROTEIN INTERACTION DOMAINS AND MOTIFS; TRANSFECTION; UBIQUITINS;

EID: 84878110204     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2013.03.020     Document Type: Article

References (41)

1. D.Y. Lee, and E.J. Brown Ubiquilins in the crosstalk among proteolytic pathways Biol. Chem. 393 6 2012 441 447
2. C. Rothenberg, and M.J. Monteiro Ubiquilin at a crossroads in protein degradation pathways Autophagy 6 7 2010 979 980
3. D. Conklin, S. Holderman, T.E. Whitmore, M. Maurer, and A.L. Feldhaus Molecular cloning, chromosome mapping and characterization of UBQLN3 a testis-specific gene that contains an ubiquitin-like domain Gene 249 1-2 2000 91 98
4. A.L. Wu, J. Wang, A. Zheleznyak, and E.J. Brown Ubiquitin-related proteins regulate interaction of vimentin intermediate filaments with the plasma membrane Mol. Cell 4 4 1999 619 625
5. H.S. Ko, T. Uehara, and Y. Nomura Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death J. Biol. Chem. 277 38 2002 35386 35392
6. P. Persson, M.T. Stockhausen, S. Pahlman, and H. Axelson Ubiquilin-1 is a novel HASH-1-complexing protein that regulates levels of neuronal bHLH transcription factors in human neuroblastoma cells Int. J. Oncol. 25 5 2004 1213 1221
7. K.J. Walters, M.F. Kleijnen, A.M. Goh, G. Wagner, and P.M. Howley Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a Biochemistry 41 6 2002 1767 1777
8. K.J. Walters, A.M. Goh, Q. Wang, G. Wagner, and P.M. Howley Ubiquitin family proteins and their relationship to the proteasome: A structural perspective Biochim. Biophys. Acta 1695 1-3 2004 73 87
9. M.F. Kleijnen, A.H. Shih, P. Zhou, S. Kumar, R.E. Soccio, and N.L. Kedersha The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome Mol. Cell 6 2 2000 409 419
10. P. Feng, C.W. Scott, N.H. Cho, H. Nakamura, Y.H. Chung, and M.J. Monteiro Kaposi's sarcoma-associated herpesvirus K7 protein targets a ubiquitin-like/ubiquitin-associated domain-containing protein to promote protein degradation Mol. Cell. Biol. 24 9 2004 3938 3948
11. D. Zhang, S. Raasi, and D. Fushman Affinity makes the difference: Nonselective interaction of the UBA domain of ubiquilin-1 with monomeric ubiquitin and polyubiquitin chains J. Mol. Biol. 377 1 2008 162 180
12. H.S. Ko, T. Uehara, K. Tsuruma, and Y. Nomura Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains FEBS Lett. 566 1-3 2004 110 114
13. E.N. N'Diaye, J. Debnath, and E.J. Brown Ubiquilins accelerate autophagosome maturation and promote cell survival during nutrient starvation Autophagy 5 4 2009 573 575
14. E.N. N'Diaye, K.K. Kajihara, I. Hsieh, H. Morisaki, J. Debnath, and E.J. Brown PLIC proteins or ubiquilins regulate autophagy-dependent cell survival during nutrient starvation EMBO Rep. 10 2 2009 173 179
15. M. Orazizadeh, H.S. Lee, B. Groenendijk, S.J. Sadler, M.O. Wright, and F.P. Lindberg CD47 associates with alpha 5 integrin and regulates responses of human articular chondrocytes to mechanical stimulation in an in vitro model Arthritis Res. Ther. 10 1 2008 R4
16. E.N. N'Diaye, and E.J. Brown The ubiquitin-related protein PLIC-1 regulates heterotrimeric G protein function through association with Gbetagamma J. Cell Biol. 163 5 2003 1157 1165
17. E.N. N'Diaye, A.C. Hanyaloglu, K.K. Kajihara, M.A. Puthenveedu, P. Wu, and M. von Zastrow The ubiquitin-like protein PLIC-2 is a negative regulator of G protein-coupled receptor endocytosis Mol. Biol. Cell 19 3 2008 1252 1260
18. H.X. Deng, W. Chen, S.T. Hong, K.M. Boycott, G.H. Gorrie, and N. Siddique Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia Nature 477 7363 2011 211 215
19. K.L. Williams, S.T. Warraich, S. Yang, J.A. Solski, R. Fernando, and G.A. Rouleau UBQLN2/ubiquilin 2 mutation and pathology in familial amyotrophic lateral sclerosis Neurobiol. Aging 33 10 2012 2527 e3-10
20. H. Daoud, H. Suhail, A. Szuto, W. Camu, F. Salachas, and V. Meininger UBQLN2 mutations are rare in French and French-Canadian amyotrophic lateral sclerosis Neurobiol. Aging 33 9 2012 2230 e1-e5
21. M. Synofzik, W. Maetzler, T. Grehl, J. Prudlo, J.M. Vom Hagen, and T. Haack Screening in ALS and FTD patients reveals 3 novel UBQLN2 mutations outside the PXX domain and a pure FTD phenotype Neurobiol. Aging 33 12 2012 2949 e13-7
22. L.J. Ball, R. Kuhne, J. Schneider-Mergener, and H. Oschkinat Recognition of proline-rich motifs by protein-protein-interaction domains Angew. Chem. Int. Ed Engl. 44 19 2005 2852 2869
23. H.R. Morris, A.J. Waite, N.M. Williams, J.W. Neal, and D.J. Blake Recent advances in the genetics of the ALS-FTLD complex Curr. Neurol. Neurosci. Rep. 12 3 2012 243 250
24. L.K. Kwong, M. Neumann, D.M. Sampathu, V.M. Lee, and J.Q. Trojanowski TDP-43 proteinopathy: The neuropathology underlying major forms of sporadic and familial frontotemporal lobar degeneration and motor neuron disease Acta Neuropathol. 114 1 2007 63 70
25. E. Buratti, and F.E. Baralle Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease Front. Biosci. 13 2008 867 878
26. E. Buratti, and F.E. Baralle The molecular links between TDP-43 dysfunction and neurodegeneration Adv. Genet. 66 2009 1 34
27. F. Geser, M. Martinez-Lage, L.K. Kwong, V.M. Lee, and J.Q. Trojanowski Amyotrophic lateral sclerosis, frontotemporal dementia and beyond: The TDP-43 diseases J. Neurol. 256 8 2009 1205 1214
28. M.J. Strong The syndromes of frontotemporal dysfunction in amyotrophic lateral sclerosis Amyotroph. Lateral Scler. 9 6 2008 323 338
29. A.C. Pawlyk, J.A. Cassel, and A.B. Reitz Current nervous system related drug targets for the treatment of amyotrophic lateral sclerosis Curr. Pharm. Des. 16 18 2010 2053 2073
30. N.A. Lanson Jr., and U.B. Pandey FUS-related proteinopathies: Lessons from animal models Brain Res. 1462 2012 44 60
31. G.T. Banks, A. Kuta, A.M. Isaacs, and E.M. Fisher TDP-43 is a culprit in human neurodegeneration, and not just an innocent bystander Mamm. Genome 19 5 2008 299 305
32. C. Lagier-Tourenne, and D.W. Cleveland Rethinking ALS: The FUS about TDP-43 Cell 136 6 2009 1001 1004
33. R.M. Liscic, L.T. Grinberg, J. Zidar, M.A. Gitcho, and N.J. Cairns ALS and FTLD: Two faces of TDP-43 proteinopathy Eur. J. Neurol. 15 8 2008 772 780
34. P.H. Kuo, L.G. Doudeva, Y.T. Wang, C.K. Shen, and H.S. Yuan Structural insights into TDP-43 in nucleic-acid binding and domain interactions Nucleic Acids Res. 37 6 2009 1799 1808
35. S.H. Ou, F. Wu, D. Harrich, L.F. Garcia-Martinez, and R.B. Gaynor Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs J. Virol. 69 6 1995 3584 3596
36. E. Buratti, and F.E. Baralle 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. 276 39 2001 36337 36343
37. J.A. Cassel, M.E. McDonnell, V. Velvadapu, V. Andrianov, and A.B. Reitz Characterization of a series of 4-aminoquinolines that stimulate caspase-7 mediated cleavage of TDP-43 and inhibit its function Biochimie 94 9 2012 1974 1981
38. E. Buratti, A. Brindisi, M. Giombi, S. Tisminetzky, Y.M. Ayala, and F.E. Baralle TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: An important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing J. Biol. Chem. 280 45 2005 37572 37584
39. A. D'Ambrogio, E. Buratti, C. Stuani, C. Guarnaccia, M. Romano, and Y.M. Ayala Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo Nucleic Acids Res. 37 12 2009 4116 4126
40. J.K. Bose, C.C. Huang, and C.K. Shen Regulation of autophagy by the neuropathological protein TDP-43 J. Biol. Chem. 286 52 2011 44441 44448
41. X. Wang, H. Fan, Z. Ying, B. Li, H. Wang, and G. Wang Degradation of TDP-43 and its pathogenic form by autophagy and the ubiquitin-proteasome system Neurosci. Lett. 469 1 2010 112 116