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Viviane Poupon

Researcher at Montreal Neurological Institute and Hospital

Publications -  16
Citations -  1275

Viviane Poupon is an academic researcher from Montreal Neurological Institute and Hospital. The author has contributed to research in topics: Endocytic cycle & Endosome. The author has an hindex of 14, co-authored 16 publications receiving 1189 citations. Previous affiliations of Viviane Poupon include McGill University & Jewish General Hospital.

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Dissection of the Endogenous Cellular Pathways of PCSK9-induced Low Density Lipoprotein Receptor Degradation EVIDENCE FOR AN INTRACELLULAR ROUTE

TL;DR: It is shown that clathrin light chain small interfering RNAs that block intracellular trafficking from the trans-Golgi network to lysosomes rapidly increased LDLR levels within HepG2 cells in aPCSK9-dependent fashion without affecting the ability of exogenous PCSK9 to enhance LDLR degradation.
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Membrane dynamics and the biogenesis of lysosomes (Review)

TL;DR: The present review focuses on current understanding of the molecular mechanisms of fusion of lysosomes with both endosomes and the plasma membrane and on the sorting events required for delivery of newly synthesized membrane proteins, endocytosed membrane proteins and other endocyTosed macromolecules to lysOSomes.
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Mammalian late vacuole protein sorting orthologues participate in early endosomal fusion and interact with the cytoskeleton.

TL;DR: Data indicate that the late Vps proteins function during multiple soluble N-ethylmaleimide-sensitive factor attachment protein receptor-mediated fusion events throughout the endocytic pathway and that their activity may be coordinated with cytoskeletal function.
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Mapping of Eps15 domains involved in its targeting to clathrin-coated pits.

TL;DR: It is shown that the N-terminal Eps15homology (EH) domains are required for CCP targeting but not sufficient, and that targeting of Eps15 to CCPs likely results from the collaboration between EH domains and another domain of the protein.
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Nucleocytoplasmic shuttling of endocytic proteins.

TL;DR: In the nucleus, eps15 and CALM acted as positive modulators of transcription in a GAL4-based transactivation assay, thus raising the intriguing possibility that some endocytic proteins play a direct or indirect role in transcriptional regulation.