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Dopey1-Mon2 complex binds to dual-lipids and recruits kinesin-1 for membrane trafficking

Author

Listed:
  • Divyanshu Mahajan

    (Nanyang Technological University)

  • Hieng Chiong Tie

    (Nanyang Technological University)

  • Bing Chen

    (Nanyang Technological University)

  • Lei Lu

    (Nanyang Technological University)

Abstract

Proteins are transported among eukaryotic organelles along the cytoskeleton in membrane carriers. The mechanism regarding the motility of carriers and the positioning of organelles is a fundamental question in cell biology that remains incompletely understood. Here, we find that Dopey1 and Mon2 assemble into a complex and localize to the Golgi, endolysosome and endoplasmic reticulum exit site. The Golgi localization of Dopey1 and Mon2 requires their binding to phosphatidylinositol-4-phosphate and phosphatidic acid, respectively, two lipids known for the biogenesis of membrane carriers and the specification of organelle identities. The N-terminus of Dopey1 further interacts with kinesin-1, a plus-end or centrifugal-direction microtubule motor. Dopey1-Mon2 complex functions as a dual-lipid-regulated cargo-adaptor to recruit kinesin-1 to secretory and endocytic organelles or membrane carriers for centrifugally biased bidirectional transport. Dopey1-Mon2 complex therefore provides an important missing link to coordinate the budding of a membrane carrier and subsequent bidirectional transport along the microtubule.

Suggested Citation

  • Divyanshu Mahajan & Hieng Chiong Tie & Bing Chen & Lei Lu, 2019. "Dopey1-Mon2 complex binds to dual-lipids and recruits kinesin-1 for membrane trafficking," Nature Communications, Nature, vol. 10(1), pages 1-19, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-11056-5
    DOI: 10.1038/s41467-019-11056-5
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