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Wildtype and mutated hVAPB associate with components of the secretory pathway in non-human primate cells.

By Anice Moumen (342821), Isabelle Virard (342823) and Cédric Raoul (207086)


<p>(A–D) Thirty-six hours following transfection of COS-7 cells, hVAPB<sup>WT</sup> and hVAPB<sup>P56S</sup> mainly colocalize with components of the secretory pathway as demonstrated by the immunostaining of hVAPB with the ER marker KDEL (A), the COPI vesicle marker β-COP-CFP (B) and ERGIC marker ERGIC-53 (C). hVAPB<sup>P56S</sup> forms cytoplasmic aggregates that colocalize with ER, COPI and ERGIC markers. Both hVAPB<sup>WT</sup> and hVAPB<sup>P56S</sup> seldom colocalize (white arrow) with the COPII marker Sec23-YFP (D). Scale bar, 20 µm.</p

Topics: Biochemistry, Cell Biology, Neuroscience, mutated, hvapb, components, secretory, pathway, non-human, primate
Year: 2013
DOI identifier: 10.1371/journal.pone.0026066.g001
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Provided by: FigShare
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