Meghan M. Heer

ORCID: 0009-0004-8693-947X
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About
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Research Areas
  • Ubiquitin and proteasome pathways
  • RNA modifications and cancer
  • Protein Degradation and Inhibitors
  • Protein Tyrosine Phosphatases
  • Peptidase Inhibition and Analysis
  • Mitochondrial Function and Pathology
  • Macrophage Migration Inhibitory Factor
  • ATP Synthase and ATPases Research
  • Genetics and Neurodevelopmental Disorders

uOttawa Brain and Mind Research Institute
2022-2025

University of Ottawa
2022-2025

Ottawa Institute of Systems Biology
2022-2025

Abstract Amyotrophic Lateral Sclerosis (ALS) and Frontotemporal Dementia (FTD) are overwhelmingly linked to TDP-43 dysfunction. Mutations in rare, indicating that the progressive accumulation of exogenous factors – such as cellular stressors converge on play a key role disease pathogenesis. Post translational modifications SUMOylation essential roles response stressors. We therefore set out understand how may regulate health disease. find is regulated dynamically via When this process...

10.1186/s13024-025-00826-z article EN cc-by Molecular Neurodegeneration 2025-03-28

SUMOylation is an evolutionarily conserved eukaryotic posttranslational protein modification with broad biological relevance. Differentiating between the major small ubiquitin-like modifier (SUMO) paralogs and uncovering paralog-specific functions in vivo has long been very difficult. To overcome this problem, we generated His6-HA-Sumo2 HA-Sumo2 knockin mouse lines, expanding upon our existing His6-HA-Sumo1 line, to establish a "toolbox" for Sumo1-Sumo2 comparisons vivo. Leveraging...

10.1016/j.isci.2023.106350 article EN cc-by iScience 2023-03-09

Abstract Amyotrophic Lateral Sclerosis (ALS) and Frontotemporal Dementia (FTD) are overwhelmingly linked to TDP-43 dysfunction. Mutations in rare, indicating that exogenous factors – such as cellular stressors converge on play a key role disease pathogenesis. Post translational modifications SUMOylation essential roles response stressors. We therefore set out understand how may regulate health disease. find is regulated dynamically via When this process blocked vivo , we note age-dependent...

10.1101/2024.04.12.589206 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2024-04-13

ABSTRACT SUMOylation is an evolutionarily conserved and essential mechanism whereby Small Ubiquitin Like Modifiers, or SUMO proteins (Sumo in mice), are covalently bound to protein substrates a highly dynamic reversible manner. involved variety of basic neurological processes including learning memory, central nervous system development, but also linked with disorders. However, studying vivo remains challenging due limited tools study Sumo their targets native context. More complexity arises...

10.1101/2022.09.09.507035 preprint EN cc-by-nc bioRxiv (Cold Spring Harbor Laboratory) 2022-09-10
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