Show simple item record

dc.contributor.authorDing, Baojin
dc.contributor.authorMirza, Anne M.
dc.contributor.authorAshley, James A.
dc.contributor.authorBudnik, Vivian
dc.contributor.authorMunson, Mary
dc.date2022-08-11T08:08:23.000
dc.date.accessioned2022-08-23T15:53:08Z
dc.date.available2022-08-23T15:53:08Z
dc.date.issued2017-11-22
dc.date.submitted2018-06-07
dc.identifier.citation<p>bioRxiv 224055; doi: https://doi.org/10.1101/224055. <a href="https://doi.org/10.1101/224055" target="_blank">Link to preprint on bioRxiv service.</a></p>
dc.identifier.doi10.1101/224055
dc.identifier.urihttp://hdl.handle.net/20.500.14038/29291
dc.description.abstractIn eukaryotes, subsets of exported mRNAs are organized into large ribonucleoprotein (megaRNP) granules. How megaRNPs exit the nucleus is unclear, as their diameters are much larger than the nuclear pore complex (NPC) central channel. We previously identified a non-canonical nuclear export mechanism in Drosophila (Speese et al., Cell 2012) and mammals (Ding et al., in preparation), in which megaRNPs exit the nucleus by budding across nuclear envelope (NE) membranes. Here, we present evidence for a similar pathway in the nucleus of the budding yeast S. cerevisiae, which contain morphologically similar granules bearing mRNAs. Wild-type yeast displayed these granules at very low frequency, but this frequency was dramatically increased when the non-essential NPC protein Nup116 was deleted. These granules were not artifacts of defective NPCs; a mutation in the exportin XPO1 (CRM1), in which NPCs are normal, induced similar megaRNP upregulation. We hypothesize that a non-canonical nuclear export pathway, analogous to those observed in Drosophila and in mammalian cells, exists in yeast, and that this pathway is upregulated for use when NPCs or nuclear export are impaired.
dc.language.isoen_US
dc.rightsThe copyright holder for this preprint (which was not peer-reviewed) is the author/funder. It is made available under a CC-BY-NC 4.0 International license.
dc.rights.urihttp://creativecommons.org/licenses/by-nc/4.0/
dc.subjecteukaryotes
dc.subjectnuclear envelope remodeling
dc.subjectmRNA
dc.subjectribonucleoprotein
dc.subjectS. cerevisiae
dc.subjectNup116
dc.subjectcell biology
dc.subjectAmino Acids, Peptides, and Proteins
dc.subjectCell Biology
dc.subjectNeuroscience and Neurobiology
dc.subjectNucleic Acids, Nucleotides, and Nucleosides
dc.titleNuclear Export Through Nuclear Envelope Remodeling in Saccharomyces cerevisiae [preprint]
dc.typePreprint
dc.source.journaltitlebioRxiv
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=2525&amp;context=faculty_pubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/faculty_pubs/1519
dc.identifier.contextkey12274226
refterms.dateFOA2022-08-23T15:53:08Z
html.description.abstract<p>In eukaryotes, subsets of exported mRNAs are organized into large ribonucleoprotein (megaRNP) granules. How megaRNPs exit the nucleus is unclear, as their diameters are much larger than the nuclear pore complex (NPC) central channel. We previously identified a non-canonical nuclear export mechanism in Drosophila (Speese et al., Cell 2012) and mammals (Ding et al., in preparation), in which megaRNPs exit the nucleus by budding across nuclear envelope (NE) membranes. Here, we present evidence for a similar pathway in the nucleus of the budding yeast S. cerevisiae, which contain morphologically similar granules bearing mRNAs. Wild-type yeast displayed these granules at very low frequency, but this frequency was dramatically increased when the non-essential NPC protein Nup116 was deleted. These granules were not artifacts of defective NPCs; a mutation in the exportin XPO1 (CRM1), in which NPCs are normal, induced similar megaRNP upregulation. We hypothesize that a non-canonical nuclear export pathway, analogous to those observed in Drosophila and in mammalian cells, exists in yeast, and that this pathway is upregulated for use when NPCs or nuclear export are impaired.</p>
dc.identifier.submissionpathfaculty_pubs/1519
dc.contributor.departmentBudnik Lab
dc.contributor.departmentBiochemistry and Molecular Pharmacology
dc.contributor.departmentNeurobiology
dc.contributor.studentJames Ashley
dc.description.thesisprogramNeuroscience


Files in this item

Thumbnail
Name:
224055.full.pdf
Size:
1.129Mb
Format:
PDF

This item appears in the following Collection(s)

Show simple item record

The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. It is made available under a CC-BY-NC 4.0 International license.
Except where otherwise noted, this item's license is described as The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. It is made available under a CC-BY-NC 4.0 International license.