Orchestration of cell surface proteins by Rab11

Welz, Tobias; Wellbourne-Wood, Joel; Kerkhoff, Eugen

doi:10.1016/j.tcb.2014.02.004

Cited by 283 publications

(308 citation statements)

References 92 publications

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“…Rab11 orchestrates the intersection between endocytic-and exocytic-trafficking pathways (41). Silencing Rab11 decreased sortilin protein and TNAP activity, indicating the participation of Rab11 transport of these proteins to the plasma membrane, rendering them susceptible to lysosomal degradation.…”

Section: Discussionmentioning

confidence: 99%

Sortilin mediates vascular calcification via its recruitment into extracellular vesicles

Goettsch¹,

Hutcheson²,

Aikawa³

et al. 2016

Journal of Clinical Investigation

213

206

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Section: Discussionmentioning

confidence: 99%

Sortilin mediates vascular calcification via its recruitment into extracellular vesicles

Goettsch¹,

Hutcheson²,

Aikawa³

et al. 2016

Journal of Clinical Investigation

213

206

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“…Rab11 has been well characterized in many systems as the master regulator of endocytic recycling, responsible for directing intracellular cargo to the apical cell surface by acting as an upstream mediator of exocytic trafficking pathways and vesicle fusion (24,31). Rab11 is apically localized in many polarized epithelial cells, which could aid intracellular pathogens that need to egress from such cells in a directional manner to exit from hosts.…”

Section: Discussionmentioning

confidence: 99%

The small GTPase RAB-11 directs polarized exocytosis of the intracellular pathogen N. parisii for fecal-oral transmission from C. elegans

Szumowski

Botts

Popovich

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Pathogen exit is a key stage in the spread and propagation of infectious disease, with the fecal-oral route being a common mode of disease transmission. However, it is poorly understood which molecular pathways provide the major modes for intracellular pathogen exit and fecal-oral transmission in vivo. Here, we use the transparent nematode Caenorhabditis elegans to investigate intestinal cell exit and fecal-oral transmission by the natural intracellular pathogen Nematocida parisii, which is a recently identified species of microsporidia. We show that N. parisii exits from polarized host intestinal cells by co-opting the host vesicle trafficking system and escaping into the lumen. Using a genetic screen, we identified components of the host endocytic recycling pathway that are required for N. parisii spore exit via exocytosis. In particular, we show that the small GTPase RAB-11 localizes to apical spores, is required for spore-containing compartments to fuse with the apical plasma membrane, and is required for spore exit. In addition, we find that RAB-11-deficient animals exhibit impaired contagiousness, supporting an in vivo role for this host trafficking factor in microsporidia disease transmission. Altogether, these findings provide an in vivo example of the major mode of exit used by a natural pathogen for disease spread via fecal-oral transmission.

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“…Examination of the ATP7B distribution in the apical pole showed a high degree of coincidence between ATP7B and Rab11a, the small GTPase associated with the SAC that regulates the apical transport and recycling of proteins (Welz et al, 2014) ( Fig. 6A1-A3,B).…”

Section: Atp7b Is Inserted Into the Basolateral Membrane And Endocytosedmentioning

confidence: 99%

Basolateral sorting and transcytosis define the Cu+-regulated translocation of ATP7B to the bile canaliculus

Lalioti

Peiró

Pérez‐Berlanga

et al. 2016

Journal of Cell Science

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The Cu + pump ATP7B plays an irreplaceable role in the elimination of excess Cu + by the hepatocyte into the bile. The trafficking and site of action of ATP7B are subjects of controversy. One current proposal is that an increase in intracellular Cu + results in the translocation of ATP7B to the lysosomes and excretion of excess Cu + through lysosomal-mediated exocytosis at the bile canaliculus. Here, we show that ATP7B is transported from the trans-Golgi network (TGN) to the bile canaliculus by basolateral sorting and endocytosis, and microtubule-mediated transcytosis through the subapical compartment. Trafficking ATP7B is not incorporated into lysosomes, and addition of Cu + does not cause relocalization of lysosomes and the appearance of lysosome markers in the bile canaliculus. Our data reveal the pathway of the Cu + -mediated transport of ATP7B from the TGN to the bile canaliculus and indicates that the bile canaliculus is the primary site of ATP7B action in the elimination of excess Cu + .

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Orchestration of cell surface proteins by Rab11

Cited by 283 publications

References 92 publications

Sortilin mediates vascular calcification via its recruitment into extracellular vesicles

Sortilin mediates vascular calcification via its recruitment into extracellular vesicles

The small GTPase RAB-11 directs polarized exocytosis of the intracellular pathogen N. parisii for fecal-oral transmission from C. elegans

Basolateral sorting and transcytosis define the Cu+-regulated translocation of ATP7B to the bile canaliculus

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