Investigating the granule forming properties of SMAUG1 and the consequence of interaction with the 14-3-3 protein family

Simple item page
dc.check.date2028-12-31
dc.contributor.advisorDean, Kellie
dc.contributor.authorFehilly, John Denisen
dc.date.accessioned2023-09-28T08:10:10Z
dc.date.available2023-09-28T08:10:10Z
dc.date.issued2023-03-01en
dc.date.submitted2023-03-01
dc.description.abstractSMAUG1 is an intrinsically disordered RNA binding protein that forms granules in cells containing RNA. SMAUG1 has been linked to several diseases such as Alzheimers, muscular dystrophy, and cancer. SMAUG1 represents a potentially distinct class of RNA granules and thus is a very interesting target for study. This work furthers our understanding of the SMAUG1 protein by showing that it undergoes rapid recovery following photobleaching indicative of liquid-liquid phase separated granules. Here we also report partial colocalization of SMAUG1 with P-body component Enhancer Of MRNA Decapping 4 (EDC4) and stress granule component Ras GTPase-activating protein-binding protein 1 (G3BP1). Previous work from the Dean lab identified interaction between the 14-3-3 family of proteins and SMAUG1. Here this interaction is validated via co-immunoprecipitation western blot analysis. Further to this potential 14-3-3 binding motifs within SMAUG were mutated and shown to be functional for 14-3-3 binding. Finally, the consequences of 14-3-3 interaction with SMAUG1 granules were assessed. 14-3-3 binding mutant form of SMAUG1 showed a higher propensity for granule formation within cells. Mutant forms of SMAUG1 also showed impaired recovery following photobleaching. This taken together suggests that the 14-3-3 family proteins are negative regulators of SMAUG1 granule formation.en
dc.description.statusNot peer revieweden
dc.description.versionAccepted Versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.citationFehilly, J. D. 2023. Investigating the granule forming properties of SMAUG1 and the consequence of interaction with the 14-3-3 protein family. MRes Thesis, University College Cork.
dc.identifier.endpage102
dc.identifier.urihttps://hdl.handle.net/10468/15042
dc.language.isoenen
dc.publisherUniversity College Corken
dc.rights© 2023, John Denis Fehilly.
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectRNAen
dc.subjectGranulesen
dc.subjectSMAUG1en
dc.titleInvestigating the granule forming properties of SMAUG1 and the consequence of interaction with the 14-3-3 protein familyen
dc.typeMasters thesis (Research)en
dc.type.qualificationlevelMastersen
dc.type.qualificationnameMRes - Master of Researchen
Files
Original bundle
Now showing 1 - 3 of 3
Thumbnail Image
Name:
FehillyJD_MRes2023.docx
Size:
17.15 MB
Format:
Microsoft Word XML
Description:
Full Text E-thesis (Word)
Thumbnail Image
Name:
FehillyJD_MRes2023.pdf
Size:
3.87 MB
Format:
Adobe Portable Document Format
Description:
Full Text E-thesis
Thumbnail Image
Name:
Submission for Examination Form
Size:
447.84 KB
Format:
Adobe Portable Document Format
License bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
license.txt
Size:
5.2 KB
Format:
Item-specific license agreed upon to submission
Description:
Download
Collections
Research Theses
Biochemistry and Cell Biology - Masters by Research Theses
College of Science, Engineering and Food Science - Masters by Research Theses