Removal of Aggregation-Prone Protein Fragments Associated with Neurodegeneration

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dc.contributor.authorManzano, Jasmin
dc.contributor.authorArfat Kasu, Yasar
dc.contributor.authorBrower, Christopher S.
dc.date.accessioned2021-03-19T18:01:58Z
dc.date.available2021-03-19T18:01:58Z
dc.date.issued2021
dc.descriptionCreative Arts and Research Symposium
dc.descriptionCreative Arts and Research Symposiumen_US
dc.description.abstractIntracellular protein aggregates associated with amyotrophic lateral sclerosis and other forms of neurodegeneration include fragments of the TAR DNA binding protein 43 (TDP43). Due to multiple cleavage sites within TDP43, a variety of protein fragments with different N-termini are produced during pathology. These fragments aggregate if not efficiently removed from cells. Previously, we reported that the aggregation of fragments bearing specific destabilizing N-terminal amino acids is prevented by their removal through the N-degron pathway of the ubiquitin proteasome system (UPS). However, it is unclear how fragments lacking destabilizing N-terminal amino are removed from cells. Here, we report that the chaperone BCL2-Associated Athanogene 6 (BAG6) interacts with aggregation-prone fragments, irrespective of their N-termini, and prevents their aggregation. We also found a separate E3-ubiquitin ligase of the UPS, RNF126, which may participate in the removal of TDP43 fragments. This work has identified novel players that help prevent protein aggregation associated with neurodegeneration.
dc.description.departmentBiology
dc.description.sponsorshipSupported by an NIH grant R15NS095317 and TWU Pioneer Center for Student Excellence
dc.identifier.urihttps://hdl.handle.net/11274/12828
dc.language.isoen_USen_US
dc.titleRemoval of Aggregation-Prone Protein Fragments Associated with Neurodegenerationen_US
dc.typePosteren_US

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Student Creative Arts and Research Symposium | 2021