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GMAP is an Atg8a-interacting protein that regulates Golgi turnover In Drosophila
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Rahman, Ashrafur, Lorincz, Peter , Gohel, Raksha, Nagy, Aniko , Csordas, Gabor, Zhang, Yan, Juhasz, Gabor and Nezis, Ioannis P. (2022) GMAP is an Atg8a-interacting protein that regulates Golgi turnover In Drosophila. Cell Reports, 39 (9). 110903. doi:10.1016/j.celrep.2022.110903 ISSN 2211-1247.
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Official URL: https://doi.org/10.1016/j.celrep.2022.110903
Abstract
Selective autophagy receptors and adapters contain short linear motifs called LIR motifs (LC3-interacting region), which are required for the interaction with the Atg8-family proteins. LIR motifs bind to the hydrophobic pockets of the LIR motif docking site (LDS) of the respective Atg8-family proteins. The physiological significance of LDS docking sites has not been clarified in vivo. Here, we show that Atg8a-LDS mutant Drosophila flies accumulate autophagy substrates and have reduced lifespan. Using quantitative proteomics to identify the proteins that accumulate in Atg8a-LDS mutants, we identify the cis-Golgi protein GMAP (Golgi microtubule-associated protein) as a LIR motif-containing protein that interacts with Atg8a. GMAP LIR mutant flies exhibit accumulation of Golgi markers and elongated Golgi morphology. Our data suggest that GMAP mediates the turnover of Golgi by selective autophagy to regulate its morphology and size via its LIR motif-mediated interaction with Atg8a.
| Item Type: | Journal Article | |||||||||||||||||||||||||||||||||
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| Alternative Title: | ||||||||||||||||||||||||||||||||||
| Subjects: | Q Science > QH Natural history > QH301 Biology Q Science > QL Zoology |
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| Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | |||||||||||||||||||||||||||||||||
| Library of Congress Subject Headings (LCSH): | Cell death, Small ubiquitin-related modifiers, Proteins, Apoptosis, Golgi apparatus, Drosophila -- Physiology | |||||||||||||||||||||||||||||||||
| Journal or Publication Title: | Cell Reports | |||||||||||||||||||||||||||||||||
| Publisher: | Elsevier | |||||||||||||||||||||||||||||||||
| ISSN: | 2211-1247 | |||||||||||||||||||||||||||||||||
| Official Date: | 31 May 2022 | |||||||||||||||||||||||||||||||||
| Dates: |
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| Volume: | 39 | |||||||||||||||||||||||||||||||||
| Number: | 9 | |||||||||||||||||||||||||||||||||
| Article Number: | 110903 | |||||||||||||||||||||||||||||||||
| DOI: | 10.1016/j.celrep.2022.110903 | |||||||||||||||||||||||||||||||||
| Status: | Peer Reviewed | |||||||||||||||||||||||||||||||||
| Publication Status: | Published | |||||||||||||||||||||||||||||||||
| Access rights to Published version: | Open Access (Creative Commons) | |||||||||||||||||||||||||||||||||
| Date of first compliant deposit: | 16 May 2022 | |||||||||||||||||||||||||||||||||
| Date of first compliant Open Access: | 6 June 2022 | |||||||||||||||||||||||||||||||||
| RIOXX Funder/Project Grant: |
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