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Protein Disulfide Isomerases Control the Secretion of Wnt proteins

Nanna Torpe, Sandeep Gopal, Oguzhan Balatci, Lorenzo Rella, Ava Handley, Henrik C Korswagen, Roger Pocock
doi: https://doi.org/10.1101/429845
Nanna Torpe
University of Copenhagen;
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Sandeep Gopal
Monash University;
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Oguzhan Balatci
Monash University;
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Lorenzo Rella
Hubrecht Institute;
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Ava Handley
Monash University;
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Henrik C Korswagen
Hubrecht Institute;
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Roger Pocock
Monash Univeristy
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  • For correspondence: roger.pocock@monash.edu
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Abstract

Appropriate Wnt morphogen secretion is required to control animal development and homeostasis. Although correct Wnt globular structure is essential for secretion, proteins that directly mediate Wnt folding and maturation are incompletely characterized. Here, we report that protein disulfide isomerase-1 (PDI-1), a protein folding catalyst and chaperone, controls secretion of the Caenorhabditis elegans Wnt ortholog EGL-20. We find that PDI-1 function is required to correctly form an anteroposterior EGL-20/Wnt gradient during embryonic development. Further, PDI-1 performs this role in EGL-20/Wnt-producing epidermal cells to cell-non-autonomously control EGL-20/Wnt-dependent neuronal migration. Using pharmacological inhibition, we further show that PDI function is required in human cells for Wnt3a secretion, revealing a conserved role for disulfide isomerases. Together, these results demonstrate a critical role for PDIs within Wnt-producing cells to control long-range developmental events that are dependent on Wnt secretion.

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Posted September 27, 2018.
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Protein Disulfide Isomerases Control the Secretion of Wnt proteins
Nanna Torpe, Sandeep Gopal, Oguzhan Balatci, Lorenzo Rella, Ava Handley, Henrik C Korswagen, Roger Pocock
bioRxiv 429845; doi: https://doi.org/10.1101/429845
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Protein Disulfide Isomerases Control the Secretion of Wnt proteins
Nanna Torpe, Sandeep Gopal, Oguzhan Balatci, Lorenzo Rella, Ava Handley, Henrik C Korswagen, Roger Pocock
bioRxiv 429845; doi: https://doi.org/10.1101/429845

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