Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/107515
Title: Dopey1-Mon2 complex binds to dual-lipids and recruits kinesin-1 for membrane trafficking
Authors: Mahajan, Divyanshu
Tie, Hieng Chiong
Chen, Bing
Lu, Lei
Keywords: Endocytosis
Kinesin
Science::Biological sciences
Issue Date: 2019
Source: Mahajan, D., Tie, H. C., Chen, B., & Lu, L. (2019). Dopey1-Mon2 complex binds to dual-lipids and recruits kinesin-1 for membrane trafficking. Nature Communications, 10(1), 3218-. doi:10.1038/s41467-019-11056-5
Series/Report no.: Nature Communications
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.
URI: https://hdl.handle.net/10356/107515
http://hdl.handle.net/10220/49727
DOI: http://dx.doi.org/10.1038/s41467-019-11056-5
Rights: © 2019 The Author(s). Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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