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dc.contributor.authorNiepel, Mario
dc.contributor.authorMolloy, Kelly R.
dc.contributor.authorWilliams, Rosemary
dc.contributor.authorFarr, Julia C.
dc.contributor.authorMeinema, Anne C.
dc.contributor.authorVecchietti, Nicholas
dc.contributor.authorCristea, Ileana M.
dc.contributor.authorChait, Brian T.
dc.contributor.authorRout, Michael P.
dc.contributor.authorStrambio-De-Castillia, Caterina
dc.date2022-08-11T08:10:18.000
dc.date.accessioned2022-08-23T17:03:25Z
dc.date.available2022-08-23T17:03:25Z
dc.date.issued2013-12-01
dc.date.submitted2021-11-01
dc.identifier.citation<p>Niepel M, Molloy KR, Williams R, Farr JC, Meinema AC, Vecchietti N, Cristea IM, Chait BT, Rout MP, Strambio-De-Castillia C. The nuclear basket proteins Mlp1p and Mlp2p are part of a dynamic interactome including Esc1p and the proteasome. Mol Biol Cell. 2013 Dec;24(24):3920-38. doi: 10.1091/mbc.E13-07-0412. Epub 2013 Oct 23. PMID: 24152732; PMCID: PMC3861087. <a href="https://doi.org/10.1091/mbc.E13-07-0412">Link to article on publisher's site</a></p>
dc.identifier.issn1059-1524 (Linking)
dc.identifier.doi10.1091/mbc.E13-07-0412
dc.identifier.pmid24152732
dc.identifier.urihttp://hdl.handle.net/20.500.14038/44421
dc.description.abstractThe basket of the nuclear pore complex (NPC) is generally depicted as a discrete structure of eight protein filaments that protrude into the nucleoplasm and converge in a ring distal to the NPC. We show that the yeast proteins Mlp1p and Mlp2p are necessary components of the nuclear basket and that they also embed the NPC within a dynamic protein network, whose extended interactome includes the spindle organizer, silencing factors, the proteasome, and key components of messenger ribonucleoproteins (mRNPs). Ultrastructural observations indicate that the basket reduces chromatin crowding around the central transporter of the NPC and might function as a docking site for mRNP during nuclear export. In addition, we show that the Mlps contribute to NPC positioning, nuclear stability, and nuclear envelope morphology. Our results suggest that the Mlps are multifunctional proteins linking the nuclear transport channel to multiple macromolecular complexes involved in the regulation of gene expression and chromatin maintenance.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=24152732&dopt=Abstract">Link to Article in PubMed</a></p>
dc.rights© 2013 Niepel et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/
dc.subjectnuclear pore complex
dc.subjectNPC
dc.subjectMlp1p
dc.subjectMlp2p
dc.subjectmessenger ribonucleoproteins
dc.subjectmRNPs
dc.subjectAmino Acids, Peptides, and Proteins
dc.subjectBiochemistry, Biophysics, and Structural Biology
dc.subjectCell Biology
dc.subjectEnzymes and Coenzymes
dc.titleThe nuclear basket proteins Mlp1p and Mlp2p are part of a dynamic interactome including Esc1p and the proteasome
dc.typeJournal Article
dc.source.journaltitleMolecular biology of the cell
dc.source.volume24
dc.source.issue24
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1154&amp;context=pmm_pp&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/pmm_pp/154
dc.identifier.contextkey25697738
refterms.dateFOA2022-08-23T17:03:25Z
html.description.abstract<p>The basket of the nuclear pore complex (NPC) is generally depicted as a discrete structure of eight protein filaments that protrude into the nucleoplasm and converge in a ring distal to the NPC. We show that the yeast proteins Mlp1p and Mlp2p are necessary components of the nuclear basket and that they also embed the NPC within a dynamic protein network, whose extended interactome includes the spindle organizer, silencing factors, the proteasome, and key components of messenger ribonucleoproteins (mRNPs). Ultrastructural observations indicate that the basket reduces chromatin crowding around the central transporter of the NPC and might function as a docking site for mRNP during nuclear export. In addition, we show that the Mlps contribute to NPC positioning, nuclear stability, and nuclear envelope morphology. Our results suggest that the Mlps are multifunctional proteins linking the nuclear transport channel to multiple macromolecular complexes involved in the regulation of gene expression and chromatin maintenance.</p>
dc.identifier.submissionpathpmm_pp/154
dc.contributor.departmentProgram in Molecular Medicine
dc.source.pages3920-38


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© 2013 Niepel et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).
Except where otherwise noted, this item's license is described as © 2013 Niepel et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).