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Title: Mammalian Mon2/Ysl2 regulates endosome-to-Golgi trafficking but possesses no guanine nucleotide exchange activity toward Arl1 GTPase
Authors: Zhou, Y.
Mahajan, Divyanshu
Boh, Boon Kim
Chen, Li
Cornvik, Tobias Carl
Hong, Wanjin
Lu, Lei
Keywords: DRNTU::Science::Biological sciences
Issue Date: 2013
Source: Mahajan, D., Boh, B. K., Zhou, Y., Chen, L., Cornvik, T. C., Hong, W., et al. (2013). Mammalian Mon2/Ysl2 regulates endosome-to-Golgi trafficking but possesses no guanine nucleotide exchange activity toward Arl1 GTPase. Scientific reports, 3, 1-9.
Series/Report no.: Scientific reports
Abstract: Arl1 is a member of Arf family small GTPases that is essential for the organization and function of Golgi complex. Mon2/Ysl2, which shares significant homology with Sec7 family Arf guanine nucleotide exchange factors, was poorly characterized in mammalian cells. Here, we report the first in depth characterization of mammalian Mon2. We found that Mon2 localized to trans-Golgi network which was dependent on both its N and C termini. The depletion of Mon2 did not affect the Golgi localized or cellular active form of Arl1. Furthermore, our in vitro assay demonstrated that recombinant Mon2 did not promote guanine nucleotide exchange of Arl1. Therefore, our results suggest that Mon2 could be neither necessary nor sufficient for the guanine nucleotide exchange of Arl1. We demonstrated that Mon2 was involved in endosome-to-Golgi trafficking as its depletion accelerated the delivery of furin and CI-M6PR to Golgi after endocytosis.
ISSN: 2045-2322
DOI: 10.1038/srep03362
Rights: © 2013 The Authors. This paper was published in Scientific Reports and is made available as an electronic reprint (preprint) with permission of the authors. The paper can be found at the following official DOI: []. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law.
Fulltext Permission: open
Fulltext Availability: With Fulltext
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