Drosophila Golgi membrane protein Ema promotes autophagosomal growth and function
Open accessAbstract
Autophagy is a self-degradative process in which cellular material is enclosed within autophagosomes and trafficked to lysosomes for degradation. Autophagosomal biogenesis is well described; however mechanisms controlling the growth and ultimate size of autophagosomes are unclear. Here we demonstrate that the Drosophila membrane protein Ema is required for the growth of autophagosomes. In an ema mutant, autophagosomes form in response to starvation and developmental cues, and these autophagosomes can mature into autolysosomes; however the autophagosomes are very small, and autophagy is impaired. In fat body cells, Ema localizes to the Golgi complex and is recruited to the membrane of autophagosomes in response to starvation. The Drosophila Golgi protein Lva also is recruited to the periphery of autophagosomes in response to starvation, and this recruitment requires ema . Therefore, we propose that Golgi is a membrane source for autophagosomal growth and that Ema facilitates this process. Clec16A, the human ortholog of Ema, is a candidate autoimmune susceptibility locus. Expression of Clec16A can rescue the autophagosome size defect in the ema mutant, suggesting that regulation of autophagosome morphogenesis may be a fundamental function of this gene family.
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Studies in Drosophila with the homologue of Clec16a, ema, demonstrate the importance of the gene to the autophagy pathway and protein trafficking in the endosomal pathway.
“Studies in Drosophila with the homologue of Clec16a, ema, demonstrate the importance of the gene to the autophagy pathway and protein trafficking in the endosomal pathway89.”
From Clec16a is Critical for Autolysosome Function and Purkinje Cell Survival (2016) · cites this paper as [9]
In ema-deficient Drosophila cells there is no observed defect in fusion between lysosomes and autophagosomes.
“While in ema-deficient Drosophila cells there is no observed defect in fusion between lysosomes and autophagosomes, reduced fusion has been suggested in studies of mitophagy induction in islet cells lacking Clec16a916.”
From Clec16a is Critical for Autolysosome Function and Purkinje Cell Survival (2016) · cites this paper as [9]
Flies mutant for ema exhibit decreased turnover of p62 and decreased mitophagy.
“Flies mutant for ema exhibit decreased turnover of p62 and decreased mitophagy9.”
From Clec16a is Critical for Autolysosome Function and Purkinje Cell Survival (2016) · cites this paper as [9]
The Drosophila CLEC16A homolog ema is required for efficient recruitment of the Golgi complex protein Lava lamp (Lva) to autophagic structures in fat body cells.
“The Drosophila CLEC16A homolog ema is required for efficient recruitment of the Golgi complex protein Lava lamp (Lva) to autophagic structures in fat body cells”
From Clec16a is Critical for Autolysosome Function and Purkinje Cell Survival (2016) · cites this paper as [9]
ema is required for proper endosomal maturation in Garland cells.
“and for proper endosomal maturation in Garland cells947.”
From Clec16a is Critical for Autolysosome Function and Purkinje Cell Survival (2016) · cites this paper as [9]
Ema plays a role in autophagosomal growth but fusion between the autophagosome and the lysosome is unaltered in the absence of the gene.
“These studies supported the concept that Ema played a role in autophagosomal growth but that fusion between the autophagosome and the lysosome was unaltered in the absence of the gene9.”
From Clec16a is Critical for Autolysosome Function and Purkinje Cell Survival (2016) · cites this paper as [9]
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GOP-1 promotes apoptotic cell degradation by activating the small GTPase Rab2 in C. elegans
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Clarifying the function of genes at the chromosome 16p13 locus in type 1 diabetes: CLEC16A and DEXI
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Genetic Modifiers of Thymic Selection and Central Tolerance in Type 1 Diabetes
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Drosophila Rab39 Attenuates Lysosomal Degradation
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Inducible knockout of Clec16a in mice results in sensory neurodegeneration
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Khalil, B. (2016) · theses.fr (ABES) · doi:10.70675/4446111fz4182z4737zae76z7f117887a893
- Authors
- Kim, S., Naylor, S. A., & DiAntonio, A.
- Affiliations
- Department of Developmental Biology, Washington University in St. Louis, St. Louis, MO 63110
- Washington University in St. Louis (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2012-04-09
- Volume
- 109
- Issue
- 18
- Pages
- E1072-81
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC3344964
- OpenAlex
- W2113382515
- Cited by
- 53
- References
- 52
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 5 · 2023: 3 · 2022: 4 · 2021: 5 · 2020: 1 · 2019: 3 · 2018: 1 · 2017: 6 · 2016: 5 · 2015: 7 · 2014: 3 · 2013: 5 · 2012: 1
- FWCI
- 3.83
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute on Drug Abuse (DA020812, R01DA020812)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- EMA, autophagy, Golgi apparatus, CLEC16A, autophagosome formation, starvation, fat body, autolysosomes, Drosophila
- MeSH terms
- Animals, Autophagy, Drosophila, Fat Body, Golgi Apparatus, Humans, Lysosomes, Membrane Fusion, Monosaccharide Transport Proteins, Mutation, Phagosomes, Endosomes, Genes, Insect, Drosophila Proteins, Lectins, C-Type, Microscopy, Electron, Transmission
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