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

Divyanshu Mahajan, Hieng Chiong Tie, Bing Chen and Lei Lu ()
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Divyanshu Mahajan: Nanyang Technological University
Hieng Chiong Tie: Nanyang Technological University
Bing Chen: Nanyang Technological University
Lei Lu: Nanyang Technological University

Nature Communications, 2019, vol. 10, issue 1, 1-19

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-11056-5

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