J
Jason Schapansky
Researcher at University of Manitoba
Publications - 14
Citations - 958
Jason Schapansky is an academic researcher from University of Manitoba. The author has contributed to research in topics: Amyloid beta & LRRK2. The author has an hindex of 11, co-authored 14 publications receiving 804 citations. Previous affiliations of Jason Schapansky include Brigham and Women's Hospital & St. Boniface General Hospital.
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Journal ArticleDOI
Membrane recruitment of endogenous LRRK2 precedes its potent regulation of autophagy
TL;DR: It is established that stimulation of specific Toll-like receptors results in a complex biochemical activation of endogenous L RRK2, with early phosphorylation of LRRK2 preceding its dimerization and membrane translocation and the importance of the kinase domain in the regulation of autophagy is suggested.
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Impaired adenosine monophosphate-activated protein kinase signalling in dorsal root ganglia neurons is linked to mitochondrial dysfunction and peripheral neuropathy in diabetes
Subir K. Roy Chowdhury,Darrell R. Smith,Ali Saleh,Jason Schapansky,Alexandra Marquez,Suzanne Gomes,Eli Akude,Dwane Morrow,Nigel A. Calcutt,Paul Fernyhough +9 more
TL;DR: The data suggest that the development of distal axonopathy in diabetic neuropathy is linked to nutrient excess and mitochondrial dysfunction via defective signalling of the adenosine monophosphate-activated protein kinase/PGC-1α pathway.
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Miro phosphorylation sites regulate Parkin recruitment and mitochondrial motility.
TL;DR: It is proposed that the status of Miro phosphorylation influences the decision to undergo Parkin-dependent mitochondrial arrest, which, in the context of PINK1 action on other substrates, can restrict mitochondrial dynamics before mitophagy.
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The complex relationships between microglia, alpha-synuclein, and LRRK2 in Parkinson's disease.
TL;DR: This review will focus on how PD-associated mutations in LRRK2 could potentially alter microglial biology with respect to neuronally secreted αSyn, resulting in cell dysfunction and neurodegeneration.
Journal ArticleDOI
Familial knockin mutation of LRRK2 causes lysosomal dysfunction and accumulation of endogenous insoluble α-synuclein in neurons.
Jason Schapansky,Saurabh Khasnavis,Mark P. DeAndrade,Jonathan D. Nardozzi,Samuel R. Falkson,Justin D. Boyd,John B. Sanderson,Tim Bartels,Heather L. Melrose,Matthew J. LaVoie +9 more
TL;DR: Mutation of LRRK2 induces modest but significant changes in lysosomal morphology and acidification, and decreased basal autophagic flux when compared to WT neurons, which demonstrate a critical and disease-relevant influence of native neuronal L RRK2 kinase activity on lysOSome function and α-synuclein homeostasis.