MiniCORVET is a Vps8-containing early endosomal tether in Drosophila.

Elife 2016 06 2;5. Epub 2016 Jun 2.

Department of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest, Hungary.

Yeast studies identified two heterohexameric tethering complexes, which consist of 4 shared (Vps11, Vps16, Vps18 and Vps33) and 2 specific subunits: Vps3 and Vps8 (CORVET) versus Vps39 and Vps41 (HOPS). CORVET is an early and HOPS is a late endosomal tether. The function of HOPS is well known in animal cells, while CORVET is poorly characterized. Here we show that Drosophila Vps8 is highly expressed in hemocytes and nephrocytes, and localizes to early endosomes despite the lack of a clear Vps3 homolog. We find that Vps8 forms a complex and acts together with Vps16A, Dor/Vps18 and Car/Vps33A, and loss of any of these proteins leads to fragmentation of endosomes. Surprisingly, Vps11 deletion causes enlargement of endosomes, similar to loss of the HOPS-specific subunits Vps39 and Lt/Vps41. We thus identify a 4 subunit-containing miniCORVET complex as an unconventional early endosomal tether in Drosophila.

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http://dx.doi.org/10.7554/eLife.14226DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4935465PMC
June 2016
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References

(Supplied by CrossRef)
The CORVET complex promotes tethering and fusion of Rab5/Vps21-positive membranes
Balderhaar et al.
Proceedings of the National Academy of Sciences of the United States of America 2013
Vps34 deficiency reveals the importance of endocytosis for podocyte homeostasis
Bechtel et al.
Journal of the American Society of Nephrology 2013
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Belyaeva et al.
1982
Molecular architecture of the multisubunit homotypic fusion and vacuole protein sorting (HOPS) tethering complex
Bröcker et al.
Proceedings of the National Academy of Sciences of the United States of America 2012
Toward a comprehensive map of the effectors of rab GTPases
Gillingham et al.
Developmental Cell 2014
Tethering the assembly of SNARE complexes
Hong et al.
Trends in Cell Biology 2014

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