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Endocytosis

Sorting the recycling

Nature Reviews Molecular Cell Biology volume 12, page 3 (2011)Cite this article

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To investigate the molecular details of receptor recycling, the authors used two receptors, β2 adrenergic receptor (B2AR), which is recycled back to the membrane in a sequence-specific manner, and δ-opioid receptor (DOR), which is selectively degraded in the lysosome. Both receptors were internalized after agonist addition, but B2AR was preferentially enriched in tubules extending from the endosomes. Vesicles containing B2AR, but not DOR, budded off the endosomal tubules, travelled to the cell surface and fused with the plasma membrane, confirming their role in receptor recycling. Furthermore, these tubules were distinct from those mediating bulk recycling, as B2AR did not colocalize with tubules containing transferrin receptors (TfRs), which travel through the bulk-recycling route. The PDZ domain-interacting sequence of B2AR, which is known to affect sequence-specific sorting, was found to be necessary and sufficient for entry into endosomal tubules.

actin regulates sequence-specific recycling by stabilizing a subset of endosomal tubules

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References

ORIGINAL RESEARCH PAPER

  1. Puthenveedu, M. A. et al. Sequence-dependent sorting of recycling proteins by actin-stabilized endosomal microdomains. Cell 143, 761–773 (2010)

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FURTHER READING

  1. Grant, B. D. & Donaldson, J G. Pathways and mechanisms of endocytic recycling. Nature Rev. Mol. Cell Biol. 10, 597–608 (2009)

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Authors
  1. Rachel David
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David, R. Sorting the recycling. Nat Rev Mol Cell Biol 12, 3 (2011). https://doi.org/10.1038/nrm3038

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