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Basolateral Endocytic Recycling Requires RAB-10 and AMPH-1 Mediated Recruitment of RAB-5 GAP TBC-2 to Endosomes

English version České info

When cargo is internalized from the cell surface by endocytosis, it enters a series of intracellular organelles called endosomes. Endosomes sort cargo, such that some cargos are sent to the lysosome for degradation, while others are recycled to the plasma membrane. Small GTPase proteins of the Rabs family are master regulators of endosomes, functioning by acting as molecular switches. As cargo moves through the endosomal system, it must pass from the domain controlled by one Rab-GTPase to the domain controlled by another. Little is known about how transitions along the recycling pathway are controlled. Here we analyze a group of protein interactions that act along the early-to-recycling pathway. Our work shows that RAB-5 deactivation mediated by TBC-2 and its recruiters RAB-10 and AMPH-1 is important for cargo recycling. This work provides mechanistic insight into how Rab proteins controlling different steps of trafficking interact during endocytic recycling.

Vyšlo v časopise: Basolateral Endocytic Recycling Requires RAB-10 and AMPH-1 Mediated Recruitment of RAB-5 GAP TBC-2 to Endosomes. PLoS Genet 11(9): e32767. doi:10.1371/journal.pgen.1005514
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.pgen.1005514

Souhrn

When cargo is internalized from the cell surface by endocytosis, it enters a series of intracellular organelles called endosomes. Endosomes sort cargo, such that some cargos are sent to the lysosome for degradation, while others are recycled to the plasma membrane. Small GTPase proteins of the Rabs family are master regulators of endosomes, functioning by acting as molecular switches. As cargo moves through the endosomal system, it must pass from the domain controlled by one Rab-GTPase to the domain controlled by another. Little is known about how transitions along the recycling pathway are controlled. Here we analyze a group of protein interactions that act along the early-to-recycling pathway. Our work shows that RAB-5 deactivation mediated by TBC-2 and its recruiters RAB-10 and AMPH-1 is important for cargo recycling. This work provides mechanistic insight into how Rab proteins controlling different steps of trafficking interact during endocytic recycling.

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