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J Cell Biol. 2017 Jul 3;216(7):1937-1947. doi: 10.1083/jcb.201611027. Epub 2017 May 8.

Rab2 promotes autophagic and endocytic lysosomal degradation.

Author information

1
Department of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest H-1117, Hungary.
2
Institute of Genetics, Biological Research Centre, Hungarian Academy of Sciences, Szeged H-6726, Hungary.
3
FIRC (Fondazione Italiana per la Ricerca sul Cancro) Institute of Molecular Oncology (IFOM), Milan 20139, Italy.
4
Department of Oncology and Hemato-Oncology, School of Medicine, University of Milan, Milan 20122, Italy.
5
Department of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest H-1117, Hungary szmrt@elte.hu.

Abstract

Rab7 promotes fusion of autophagosomes and late endosomes with lysosomes in yeast and metazoan cells, acting together with its effector, the tethering complex HOPS. Here we show that another small GTPase, Rab2, is also required for autophagosome and endosome maturation and proper lysosome function in Drosophila melanogaster We demonstrate that Rab2 binds to HOPS, and that its active, GTP-locked form associates with autolysosomes. Importantly, expression of active Rab2 promotes autolysosomal fusions unlike that of GTP-locked Rab7, suggesting that its amount is normally rate limiting. We also demonstrate that RAB2A is required for autophagosome clearance in human breast cancer cells. In conclusion, we identify Rab2 as a key factor for autophagic and endocytic cargo delivery to and degradation in lysosomes.

PMID:
28483915
PMCID:
PMC5496615
DOI:
10.1083/jcb.201611027
[Indexed for MEDLINE]
Free PMC Article

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