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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

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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
Alternative Title:
Subjects: Q Science > QH Natural history > QH301 Biology
Q Science > QL Zoology
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:
DateEvent
31 May 2022Published
11 May 2022Accepted
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:
Project/Grant IDRIOXX Funder NameFunder ID
BB/L006324/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/P007856/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/V014838/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
RPG-2017-023Leverhulme Trusthttp://dx.doi.org/10.13039/501100000275
KKP 129797Nemzeti Kutatási Fejlesztési és Innovációs Hivatalhttp://dx.doi.org/10.13039/501100011019
National Laboratory for Biotechnology programNemzeti Kutatási Fejlesztési és Innovációs Hivatalhttp://dx.doi.org/10.13039/501100011019
PhD studentship[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BO-00514-21-8Magyar Tudományos Akadémiahttp://dx.doi.org/10.13039/501100003825
FK 138851Nemzeti Kutatási Fejlesztési és Innovációs Hivatalhttp://dx.doi.org/10.13039/501100011019
UNKP-21-5-ELTE-1122Nemzeti Kutatási Fejlesztési és Innovációs Hivatalhttp://dx.doi.org/10.13039/501100011019
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