ACS Publications. Most Trusted. Most Cited. Most Read
My Activity
CONTENT TYPES

The SMN Interactome Includes Myb-Binding Protein 1a

View Author Information
Wolfson Centre for Inherited Neuromuscular Disease, RJAH Orthopaedic Hospital, Oswestry, SY10 7AG, United Kingdom, Institute for Science and Technology in Medicine, Keele University, Staffordshire, United Kingdom, School of Biomedical Sciences, The Ohio State University, Columbus, Ohio 43210, School of Molecular and Biomedical Science, University of Adelaide, Adelaide, SA 5005, Australia, Bruker Daltonik GmbH, Bremen, Germany, and Diamantina Institute for Cancer, Immunology and Metabolic Medicine, University of Queensland, Brisbane, QLD 4102, Australia
* To whom correspondence should be addressed. E-mail: [email protected]. Telephone: 44-1691-404155. Fax: 44-1691-404170.
†RJAH Orthopaedic Hospital.
‡Keele University.
§The Ohio State University.
∥University of Adelaide.
⊥Bruker Daltonik GmbH.
#University of Queensland.
Cite this: J. Proteome Res. 2010, 9, 1, 556–563
Publication Date (Web):November 23, 2009
https://doi.org/10.1021/pr900884g
Copyright © 2009 American Chemical Society

    Article Views

    1574

    Altmetric

    -

    Citations

    LEARN ABOUT THESE METRICS
    Other access options

    Abstract

    Abstract Image

    Understanding networks of interacting proteins is a major goal in cell biology. The survival of motor neurons protein (SMN) interacts, directly or indirectly, with a large number of other proteins and reduced levels of SMN cause the inherited disorder spinal muscular atrophy (SMA). Some SMN interactions are stable and stoichiometric, such as those with gemins, while others are expected to be transient and substoichiometric, such as the functional interaction of SMN with coilin in Cajal bodies. This study set out to determine whether novel components of the extensive SMN interactome can be identified by a proteomic approach. SMN complexes were immuno-precipitated from HeLa nuclear extracts, using anti-SMN monoclonal antibody attached to magnetic beads, digested with trypsin, separated by capillary-liquid chromatography and analyzed by MALDI TOF/TOF mass spectrometry. One-hundred and one proteins were detected with a p value of <0.05, SMN, gemins and U snRNPs being the dominant “hits”. Sixty-nine of these were rejected after MALDI analysis of two control pull-downs using antibodies against unrelated nuclear proteins. The proteins found only in anti-SMN pulldowns were either known SMN partners, and/or contained dimethylated RG domains involved in direct interaction with the SMN tudor domain, or they were known binding partners of such direct SMN interactors. Myb-binding protein 1a, identified as a novel candidate, is a mainly nucleolar protein of unknown function but it partially colocalized with SMN in Cajal bodies in HeLa cell nucleoplasm and, like SMN, was reduced in cells from an SMA patient.

    Read this article

    To access this article, please review the available access options below.

    Get instant access

    Purchase Access

    Read this article for 48 hours. Check out below using your ACS ID or as a guest.

    Recommended

    Access through Your Institution

    You may have access to this article through your institution.

    Your institution does not have access to this content. You can change your affiliated institution below.

    Cited By

    This article is cited by 27 publications.

    1. Patrick Lomonte, Faouzi Baklouti, Olivier Binda. The Biochemistry of Survival Motor Neuron Protein Is Paving the Way to Novel Therapies for Spinal Muscle Atrophy. Biochemistry 2020, 59 (14) , 1391-1397. https://doi.org/10.1021/acs.biochem.9b01124
    2. Heidi R. Fuller, Nguyen Thi Man, Le Thanh Lam, Vladimir A. Shamanin, Elliot J. Androphy and Glenn E. Morris . Valproate and Bone Loss: iTRAQ Proteomics Show that Valproate Reduces Collagens and Osteonectin in SMA Cells. Journal of Proteome Research 2010, 9 (8) , 4228-4233. https://doi.org/10.1021/pr1005263
    3. Gaurav Sharma, Martina Paganin, Fabio Lauria, Elena Perenthaler, Gabriella Viero. The SMN-ribosome interplay: a new opportunity for Spinal Muscular Atrophy therapies. Biochemical Society Transactions 2024, 52 (1) , 465-479. https://doi.org/10.1042/BST20231116
    4. Piotr Kozlowski. Thirty Years with ERH: An mRNA Splicing and Mitosis Factor Only or Rather a Novel Genome Integrity Protector?. Cells 2023, 12 (20) , 2449. https://doi.org/10.3390/cells12202449
    5. Olivier Binda, Franceline Juillard, Julia Novion Ducassou, Constance Kleijwegt, Geneviève Paris, Andréanne Didillon, Faouzi Baklouti, Armelle Corpet, Yohann Couté, Jocelyn Côté, Patrick Lomonte. SMA-linked SMN mutants prevent phase separation properties and SMN interactions with FMRP family members. Life Science Alliance 2023, 6 (1) , e202201429. https://doi.org/10.26508/lsa.202201429
    6. Nora Tula Detering, Tobias Schüning, Niko Hensel, Peter Claus. The phospho-landscape of the survival of motoneuron protein (SMN) protein: relevance for spinal muscular atrophy (SMA). Cellular and Molecular Life Sciences 2022, 79 (9) https://doi.org/10.1007/s00018-022-04522-9
    7. Katharina Hutter, Michael Lohmüller, Almina Jukic, Felix Eichin, Seymen Avci, Verena Labi, Tamas G. Szabo, Simon M. Hoser, Alexander Hüttenhofer, Andreas Villunger, Sebastian Herzog. SAFB2 Enables the Processing of Suboptimal Stem-Loop Structures in Clustered Primary miRNA Transcripts. Molecular Cell 2020, 78 (5) , 876-889.e6. https://doi.org/10.1016/j.molcel.2020.05.011
    8. Dan Zhang, Yi-jing Chu, Ke-juan Song, Yu-long Chen, Wei Liu, Teng Lv, Jing Wang, Han Zhao, Yuan-zhong Ren, Jin-xang Xu, Nan-nan Xia, Hong-xuan Li, Qin Yao. Knockdown of enhancer of rudimentary homolog inhibits proliferation and metastasis in ovarian cancer by regulating epithelial-mesenchymal transition. Biomedicine & Pharmacotherapy 2020, 125 , 109974. https://doi.org/10.1016/j.biopha.2020.109974
    9. Qingmin Zeng, Fuming Lei, Yigang Chang, Zhaoya Gao, Yanzhao Wang, Qingkun Gao, Pengfei Niu, Qiang Li. An oncogenic gene, SNRPA1, regulates PIK3R1, VEGFC, MKI67, CDK1 and other genes in colorectal cancer. Biomedicine & Pharmacotherapy 2019, 117 , 109076. https://doi.org/10.1016/j.biopha.2019.109076
    10. Paola Bernabò, Toma Tebaldi, Ewout J.N. Groen, Fiona M. Lane, Elena Perenthaler, Francesca Mattedi, Helen J. Newbery, Haiyan Zhou, Paola Zuccotti, Valentina Potrich, Hannah K. Shorrock, Francesco Muntoni, Alessandro Quattrone, Thomas H. Gillingwater, Gabriella Viero. In Vivo Translatome Profiling in Spinal Muscular Atrophy Reveals a Role for SMN Protein in Ribosome Biology. Cell Reports 2017, 21 (4) , 953-965. https://doi.org/10.1016/j.celrep.2017.10.010
    11. Seyyedmohsen Hosseinibarkooie, Svenja Schneider, Brunhilde Wirth. Advances in understanding the role of disease-associated proteins in spinal muscular atrophy. Expert Review of Proteomics 2017, 14 (7) , 581-592. https://doi.org/10.1080/14789450.2017.1345631
    12. Ravindra N. Singh, Matthew D. Howell, Eric W. Ottesen, Natalia N. Singh. Diverse role of survival motor neuron protein. Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms 2017, 1860 (3) , 299-315. https://doi.org/10.1016/j.bbagrm.2016.12.008
    13. Heidi R. Fuller, Thomas H. Gillingwater, Thomas M. Wishart. Commonality amid diversity: Multi-study proteomic identification of conserved disease mechanisms in spinal muscular atrophy. Neuromuscular Disorders 2016, 26 (9) , 560-569. https://doi.org/10.1016/j.nmd.2016.06.004
    14. David Piñeiro, Javier Fernandez-Chamorro, Rosario Francisco-Velilla, Encarna Martinez-Salas. Gemin5: A Multitasking RNA-Binding Protein Involved in Translation Control. Biomolecules 2015, 5 (2) , 528-544. https://doi.org/10.3390/biom5020528
    15. Jonathan J. Cherry, Dione T. Kobayashi, Maureen M. Lynes, Nikolai N. Naryshkin, Francesco Danilo Tiziano, Phillip G. Zaworski, Lee L. Rubin, Jill Jarecki. Assays for the Identification and Prioritization of Drug Candidates for Spinal Muscular Atrophy. ASSAY and Drug Development Technologies 2014, 12 (6) , 315-341. https://doi.org/10.1089/adt.2014.587
    16. Fabio Mirabella, Alexander Murison, Lauren I. Aronson, Christopher P. Wardell, Andrew J. Thompson, Sarah J. Hanrahan, Jacqueline H. L. Fok, Charlotte Pawlyn, Martin F. Kaiser, Brian A. Walker, Faith E. Davies, Gareth J. Morgan, . A Novel Functional Role for MMSET in RNA Processing Based on the Link Between the REIIBP Isoform and Its Interaction with the SMN Complex. PLoS ONE 2014, 9 (6) , e99493. https://doi.org/10.1371/journal.pone.0099493
    17. Thomas M. Wishart, Chantal A. Mutsaers, Markus Riessland, Michell M. Reimer, Gillian Hunter, Marie L. Hannam, Samantha L. Eaton, Heidi R. Fuller, Sarah L. Roche, Eilidh Somers, Robert Morse, Philip J. Young, Douglas J. Lamont, Matthias Hammerschmidt, Anagha Joshi, Peter Hohenstein, Glenn E. Morris, Simon H. Parson, Paul A. Skehel, Thomas Becker, Iain M. Robinson, Catherina G. Becker, Brunhilde Wirth, Thomas H. Gillingwater. Dysregulation of ubiquitin homeostasis and β-catenin signaling promote spinal muscular atrophy. Journal of Clinical Investigation 2014, 124 (4) , 1821-1834. https://doi.org/10.1172/JCI71318
    18. Meng-Tzu Weng, Ji Luo. The enigmatic ERH protein: its role in cell cycle, RNA splicing and cancer. Protein & Cell 2013, 4 (11) , 807-812. https://doi.org/10.1007/s13238-013-3056-3
    19. Matthew W. Foster, J. Will Thompson, Michael T. Forrester, Yonggang Sha, Timothy J. McMahon, Dawn E. Bowles, M. Arthur Moseley, Harvey E. Marshall. Proteomic analysis of the NOS2 interactome in human airway epithelial cells. Nitric Oxide 2013, 34 , 37-46. https://doi.org/10.1016/j.niox.2013.02.079
    20. Le Thanh Lam, Heidi R. Fuller, Glenn E. Morris. The gemin2-binding site on SMN protein: Accessibility to antibody. Biochemical and Biophysical Research Communications 2013, 438 (4) , 624-627. https://doi.org/10.1016/j.bbrc.2013.08.005
    21. David Piñeiro, Noemi Fernández, Jorge Ramajo, Encarnación Martínez-Salas. Gemin5 promotes IRES interaction and translation control through its C-terminal region. Nucleic Acids Research 2013, 41 (2) , 1017-1028. https://doi.org/10.1093/nar/gks1212
    22. Meng-Tzu Weng, Jih-Hsiang Lee, Shu-Chen Wei, Qiuning Li, Sina Shahamatdar, Dennis Hsu, Aaron J. Schetter, Stephen Swatkoski, Poonam Mannan, Susan Garfield, Marjan Gucek, Marianne K. H. Kim, Christina M. Annunziata, Chad J. Creighton, Michael J. Emanuele, Curtis C. Harris, Jin-Chuan Sheu, Giuseppe Giaccone, Ji Luo. Evolutionarily conserved protein ERH controls CENP-E mRNA splicing and is required for the survival of KRAS mutant cancer cells. Proceedings of the National Academy of Sciences 2012, 109 (52) https://doi.org/10.1073/pnas.1207673110
    23. Chang-Ching Yang, Hsuan Liu, Shen Liang Chen, Tzu-Hao Wang, Chia-Ling Hsieh, Yi Huang, Shu-Jen Chen, Hua-Chien Chen, Benjamin Yat-Ming Yung, Bertrand Chin-Ming Tan. Epigenetic silencing of myogenic gene program by Myb-binding protein 1a suppresses myogenesis. The EMBO Journal 2012, 31 (7) , 1739-1751. https://doi.org/10.1038/emboj.2012.24
    24. Emma Humphrey, Heidi R. Fuller, Glenn E. Morris. Current research on SMN protein and treatment strategies for spinal muscular atrophy. Neuromuscular Disorders 2012, 22 (2) , 193-197. https://doi.org/10.1016/j.nmd.2011.06.002
    25. Ruben J. Cauchi. SMN and Gemins: ‘We are family’ … or are we?. BioEssays 2010, 32 (12) , 1077-1089. https://doi.org/10.1002/bies.201000088
    26. Heidi Fuller, Glenn Morris. SMN complexes of nucleus and cytoplasm: A proteomic study for SMA therapy. Translational Neuroscience 2010, 1 (4) , 261-267. https://doi.org/10.2478/v10134-010-0027-6
    27. Rachel Nlend Nlend, Kathrin Meyer, Daniel Schumperli. Repair of pre-mRNA splicing. RNA Biology 2010, 7 (4) , 430-440. https://doi.org/10.4161/rna.7.4.12206

    Pair your accounts.

    Export articles to Mendeley

    Get article recommendations from ACS based on references in your Mendeley library.

    Pair your accounts.

    Export articles to Mendeley

    Get article recommendations from ACS based on references in your Mendeley library.

    You’ve supercharged your research process with ACS and Mendeley!

    STEP 1:
    Click to create an ACS ID

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    MENDELEY PAIRING EXPIRED
    Your Mendeley pairing has expired. Please reconnect