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SNX19 restricts endolysosome motility through contacts with the endoplasmic reticulum

Author

Listed:
  • Amra Saric

    (Neurosciences and Cellular and Structural Biology Division, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health)

  • Spencer A. Freeman

    (Program in Cell Biology, Peter Gilgan Centre for Research and Learning, Hospital for Sick Children
    Department of Biochemistry, University of Toronto)

  • Chad D. Williamson

    (Neurosciences and Cellular and Structural Biology Division, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health)

  • Michal Jarnik

    (Neurosciences and Cellular and Structural Biology Division, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health)

  • Carlos M. Guardia

    (Neurosciences and Cellular and Structural Biology Division, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health)

  • Michael S. Fernandopulle

    (Neurogenetics Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health)

  • David C. Gershlick

    (Neurosciences and Cellular and Structural Biology Division, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health
    Cambridge Institute for Medical Research, University of Cambridge)

  • Juan S. Bonifacino

    (Neurosciences and Cellular and Structural Biology Division, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health)

Abstract

The ability of endolysosomal organelles to move within the cytoplasm is essential for the performance of their functions. Long-range movement involves coupling of the endolysosomes to motor proteins that carry them along microtubule tracks. This movement is influenced by interactions with other organelles, but the mechanisms involved are incompletely understood. Herein we show that the sorting nexin SNX19 tethers endolysosomes to the endoplasmic reticulum (ER), decreasing their motility and contributing to their concentration in the perinuclear area of the cell. Tethering depends on two N-terminal transmembrane domains that anchor SNX19 to the ER, and a PX domain that binds to phosphatidylinositol 3-phosphate on the endolysosomal membrane. Two other domains named PXA and PXC negatively regulate the interaction of SNX19 with endolysosomes. These studies thus identify a mechanism for controlling the motility and positioning of endolysosomes that involves tethering to the ER by a sorting nexin.

Suggested Citation

  • Amra Saric & Spencer A. Freeman & Chad D. Williamson & Michal Jarnik & Carlos M. Guardia & Michael S. Fernandopulle & David C. Gershlick & Juan S. Bonifacino, 2021. "SNX19 restricts endolysosome motility through contacts with the endoplasmic reticulum," Nature Communications, Nature, vol. 12(1), pages 1-17, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-24709-1
    DOI: 10.1038/s41467-021-24709-1
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    Cited by:

    1. Rahul Kumar & Maleeha Khan & Vincent Francis & Adriana Aguila & Gopinath Kulasekaran & Emily Banks & Peter S. McPherson, 2024. "DENND6A links Arl8b to a Rab34/RILP/dynein complex, regulating lysosomal positioning and autophagy," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    2. Tal Keren-Kaplan & Amra Sarić & Saikat Ghosh & Chad D. Williamson & Rui Jia & Yan Li & Juan S. Bonifacino, 2022. "RUFY3 and RUFY4 are ARL8 effectors that promote coupling of endolysosomes to dynein-dynactin," Nature Communications, Nature, vol. 13(1), pages 1-22, December.

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