The novel endosomal membrane protein Ema interacts with the class C Vps–HOPS complex to promote endosomal maturation
Open accessAbstract
Endosomal maturation is critical for accurate and efficient cargo transport through endosomal compartments. Here we identify a mutation of the novel Drosophila gene, ema (endosomal maturation defective) in a screen for abnormal synaptic overgrowth and defective protein trafficking. Ema is an endosomal membrane protein required for trafficking of fluid-phase and receptor-mediated endocytic cargos. In the ema mutant, enlarged endosomal compartments accumulate as endosomal maturation fails, with early and late endosomes unable to progress into mature degradative late endosomes and lysosomes. Defective endosomal down-regulation of BMP signaling is responsible for the abnormal synaptic overgrowth. Ema binds to and genetically interacts with Vps16A, a component of the class C Vps–HOPS complex that promotes endosomal maturation. The human orthologue of ema, Clec16A, is a candidate susceptibility locus for autoimmune disorders, and its expression rescues the Drosophila mutant demonstrating conserved function. Characterizing this novel gene family identifies a new component of the endosomal pathway and provides insights into class C Vps–HOPS complex function.
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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 [47]
The Results section, “Ema orthologues are functionally conserved” (page unavailable), identifies human CLEC16A as an orthologue of Drosophila ema. The paper also lists a Lava lamp antibody in Materials and methods, but the retrieved Results passages concern endosomal maturation in garland cells, not Lva recruitment to autophagic structures in fat body cells. The claim’s central recruitment finding is therefore unsupported by our copy. (LLM, conf=0.86)
Experimental — accuracy not yet measuredThe phenotype of flies mutant in ema can be complemented by expression of human or mouse CLEC16A.
“the phenotype of flies mutant in ema can be complemented by expression of human or mouse CLEC16A”
From Clec16a is Critical for Autolysosome Function and Purkinje Cell Survival (2016) · cites this paper as [47]
The Results section, “Ema orthologues are functionally conserved” (page unavailable), reports that expression of human CLEC16A rescues lethality and other phenotypes in ema-mutant flies. The paper does not report a rescue experiment using mouse CLEC16A, so the mouse portion of the claim is unsupported. (LLM, conf=0.90)
Experimental — accuracy not yet measuredema 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 [47]
The function of CLEC16A is highly conserved.
“indicating that the function of this protein is highly conserved47.”
From Clec16a is Critical for Autolysosome Function and Purkinje Cell Survival (2016) · cites this paper as [47]
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- Authors
- Kim, S., Wairkar, Y. P., Daniels, R. W., & DiAntonio, A.
- Affiliations
- Department of Developmental Biology, Washington University in St. Louis, St. Louis, MO 63110
- Washington University in St. Louis (US)
- Corresponding author
- DiAntonio, Aaron
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2010-03-01
- Volume
- 188
- Issue
- 5
- Pages
- 717-734
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2835942
- OpenAlex
- W2014895591
- Cited by
- 82
- References
- 69
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 5 · 2023: 2 · 2022: 5 · 2021: 5 · 2020: 2 · 2019: 3 · 2018: 2 · 2017: 6 · 2016: 5 · 2015: 9 · 2014: 5 · 2013: 13 · 2012: 7
- FWCI
- 3.64
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Digital Commons@Becker (Washington University School of Medicine) (submittedVersion, cc-by-nc-sa)
- Funders
- National Institutes of Health
- National Institute on Drug Abuse (DA020812, R01DA020812)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- endosomal maturation, EMA, CLEC16A, BMP signaling, lysosomal biogenesis, Drosophila, protein trafficking
- MeSH terms
- Animals, Drosophila melanogaster, Humans, Intracellular Membranes, Molecular Sequence Data, Monosaccharide Transport Proteins, Neuromuscular Junction, Plant Proteins, Endosomes, Recombinant Fusion Proteins, Synapses, Bone Morphogenetic Proteins, Two-Hybrid System Techniques, Drosophila Proteins, Vesicular Transport Proteins, Lectins, C-Type, Multiprotein Complexes
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