Author

E. A. Fon

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 5 Cell Biology· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Research Focus:cell type annotation· 5 Organism:human· 5 Assay:proteomics· 3 Assay:bulk RNA-seq· 2 Research Focus:cell signaling & trafficking· 2 Research Focus:differential expression· 2 Research Focus:protein folding & dynamics· 2

Frequent Co-Authors

J.-F. Trempe· 5 shared T. M. Durcan· 4 shared C. X.- Q. Chen· 3 shared I. Shlaifer· 3 shared W. Luo· 3 shared B. Vanderperre· 2 shared K. Gehring· 2 shared M.-F. Dorion· 2 shared

Activity by Year

2020-2023 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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5 shared papersBiochemistry

J.-F. Trempe

Mutual co-authors in cluster

Author profile →

9 papers

Recent·Most cited

A genome-wide CRISPR/Cas9 screen identifies genes that regulate the cellular uptake of α-synuclein fibrils by modulating heparan sulfate proteoglycans

B. Vanderperre, A. Muraleedharan, M.-F. Dorion, F. Larroquette, E. Del Cid Pellitero, N. Rajakulendran, C. X.- Q. Chen, R. Lariviere, C. Michaud-Tardif, R. Chidiac, D. Lipuma, G. Macleod, R. Thomas, Z. Wang, W. E. Reintsch, , E. A. Fon

This study uses CRISPR/Cas9 screening to identify genes regulating α-synuclein fibril uptake via heparan sulfate proteoglycans, revealing SLC39A9 and C3orf58 as key modulators.

bioRxiv · Sep 29, 2023 · PreprintCell Biology

MerTK mediates the immunologically silent uptake of alpha-synuclein fibrils by human microglia

M.-F. Dorion, K. Senkevich, M. Yaqubi, N. W. Kieran, C. X.- Q. Chen, A. MacDonald, W. Luo, A. Wallis, I. Shlaifer, J. Hall, R. W. R. Dudley, I. A. Glass, Birth Defects Research Laboratory, J. A. Straton, E. A. Fon, , L. M. Healy

This study shows MerTK mediates microglial uptake of alpha-synuclein fibrils without triggering inflammation and links MERTK variants to Parkinson's disease.

bioRxiv · Mar 4, 2023 · PreprintCell Biology

Structure-based design and characterization of Parkin activating mutations

J.-F. Trempe, M. U. Stevens, N. Croteau, M. A. Eldeeb, Z. W. Zeng, R. Toth, T. M. Durcan, W. Springer, E. A. Fon, M. M. K. Muqit

The paper identifies three Parkin activating mutations that rescue mitophagy defects in cell-based studies, suggesting therapeutic potential for Parkinson's disease.

bioRxiv · Feb 22, 2022Biochemistry

Rapid macropinocytic transfer of α-synuclein to lysosomes

A. Bayati, E. Banks, C. Han, W. Luo, W. E. Reintsch, C. E. Zorca, I. Shlaifer, E. D. C. Pellitero, B. Vanderperre, H. M. McBride, E. A. Fon, T. A. Durcan, P. S. McPherson

This study shows alpha-synuclein fibrils are rapidly internalized via macropinocytosis and directed to lysosomes, with some transferred to neighboring cells.

bioRxiv · Jan 6, 2022Cell Biology

Selective localization of Mfn2 near PINK1 enable its preferential ubiquitination by Parkin on mitochondria

M. Vranas, Y. Lu, S. Rasool, N. Croteau, J. D. Krett, V. Sauve, K. Gehring, E. A. Fon, T. M. Durcan, J.-F. Trempe

The paper identifies Mfn2 as a preferred Parkin substrate due to its proximity to PINK1, which facilitates Parkin activation and ubiquitination on mitochondria.

bioRxiv · Aug 25, 2021Biochemistry

Structural basis for feedforward control in the PINK1/parkin pathway

V. Sauve, G. Sung, E. MacDougall, G. Kozlov, A. Saran, R. Fakih, E. A. Fon, K. Gehring

The paper elucidates how phospho-ubiquitin binds to parkin's RING domains to activate the PINK1/parkin pathway through a feedforward mechanism.

bioRxiv · Aug 16, 2021Biochemistry

Structure of PINK1 reveals autophosphorylation dimer and provides insights into binding to the TOM complex

S. Rasool, S. Veyron, N. Soya, M. Eldeeb, G. Lukacs, E. A. Fon, J.-F. Trempe

The paper reports crystal structures of insect PINK1, revealing a dimeric autophosphorylation complex and insights into its binding to the TOM complex.

bioRxiv · Aug 5, 2021Biochemistry

Standardized quality control workflow to evaluate the reproducibility and differentiation potential of human iPSCs into neurons

C. X.- Q. Chen, N. Abdian, G. Maussion, R. A. Thomas, I. Demirova, E. Cai, M. Tabatabaei, L. K. Beitel, J. Karamchandani, E. A. Fon, T. M. Durcan

The paper establishes a standardized quality control workflow to assess variability and reproducibility of human iPSCs in differentiation into neurons and other germ layers.

bioRxiv · Jan 13, 2021 · PreprintCell Biology

Proteomic profiling of mitochondrial-derived vesicles in brain reveals enrichment of respiratory complex sub-assemblies and small TIM chaperones

R. F. Roberts, A. N. Bayne, T. Goiran, D. Levesque, F. M. Boisvert, J.-F. Trempe, E. A. Fon

The paper identifies proteins enriched in brain mitochondrial-derived vesicles (MDVs), revealing OXPHOS proteins and small TIM chaperones, and shows no significant difference in MDV proteomes between wild-type and PINK1-/- or Parkin-/- mice.

bioRxiv · Jul 6, 2020Biochemistry