The SMN interactome includes Myb-binding protein 1a

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dc.contributor.authorFuller, H.
dc.contributor.authorNguyen, T.
dc.contributor.authorLam, L.
dc.contributor.authorThanh, L.
dc.contributor.authorKeough, R.
dc.contributor.authorAsperger, A.
dc.contributor.authorGonda, T.
dc.contributor.authorMorris, G.
dc.date.issued2010
dc.description.abstractUnderstanding 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.
dc.description.statementofresponsibilityHeidi R. Fuller, Nguyen Thi Man, Le Thanh Lam, Le Thiet Thanh, Rebecca A. Keough, Arndt Asperger, Thomas J. Gonda and Glenn E. Morris
dc.identifier.citationJournal of Proteome Research, 2010; 9(1):556-563
dc.identifier.doi10.1021/pr900884g
dc.identifier.issn1535-3893
dc.identifier.issn1535-3907
dc.identifier.orcidGonda, T. [0000-0002-8792-3021]
dc.identifier.urihttp://hdl.handle.net/2440/60740
dc.language.isoen
dc.publisherAmerican Chemical Society
dc.rights© 2010 American Chemical Society
dc.source.urihttps://doi.org/10.1021/pr900884g
dc.subjectSMN
dc.subjectMyb-binding protein 1a
dc.subjectCajal body
dc.subjectnucleolus
dc.subjectMALDI TOF/TOF
dc.subjectmass spectrometry
dc.subjectimmunoprecipitation
dc.subjectinteraction
dc.subjectSMA
dc.titleThe SMN interactome includes Myb-binding protein 1a
dc.typeJournal article
pubs.publication-statusPublished

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