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https://doi.org/10.1038/srep03362
Title: | Mammalian Mon2/Ysl2 regulates endosome-to-Golgi trafficking but possesses no guanine nucleotide exchange activity toward Arl1 GTPase | Authors: | Mahajan, D Boh, B.K Zhou, Y Chen, L Cornvik, T.C Hong, W Lu, L |
Keywords: | adenosine diphosphate ribosylation factor ADP-ribosylation factor related proteins cation-dependent mannose-6-phosphate receptor furin guanine nucleotide exchange factor membrane protein MON2 protein, human proton transporting adenosine triphosphatase Sec7 guanine nucleotide exchange factors small interfering RNA somatomedin B receptor animal cell line Chlorocebus aethiops endocytosis endosome genetics Golgi complex HeLa cell line human metabolism physiology protein transport RNA interference ADP-Ribosylation Factors Animals Cell Line Cercopithecus aethiops Endocytosis Endosomes Furin Golgi Apparatus Guanine Nucleotide Exchange Factors HeLa Cells Humans Membrane Proteins Protein Transport Proton-Translocating ATPases Receptor, IGF Type 2 RNA Interference RNA, Small Interfering |
Issue Date: | 2013 | Citation: | Mahajan, D, Boh, B.K, Zhou, Y, Chen, L, Cornvik, T.C, Hong, W, Lu, L (2013). Mammalian Mon2/Ysl2 regulates endosome-to-Golgi trafficking but possesses no guanine nucleotide exchange activity toward Arl1 GTPase. Scientific Reports 3 : 3362. ScholarBank@NUS Repository. https://doi.org/10.1038/srep03362 | Rights: | Attribution 4.0 International | 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. | Source Title: | Scientific Reports | URI: | https://scholarbank.nus.edu.sg/handle/10635/182046 | ISSN: | 20452322 | DOI: | 10.1038/srep03362 | Rights: | Attribution 4.0 International |
Appears in Collections: | Elements Staff Publications |
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