| Literature DB >> 21111236 |
Manojkumar A Puthenveedu1, Benjamin Lauffer, Paul Temkin, Rachel Vistein, Peter Carlton, Kurt Thorn, Jack Taunton, Orion D Weiner, Robert G Parton, Mark von Zastrow.
Abstract
The functional consequences of signaling receptor endocytosis are determined by the endosomal sorting of receptors between degradation and recycling pathways. How receptors recycle efficiently, in a sequence-dependent manner that is distinct from bulk membrane recycling, is not known. Here, in live cells, we visualize the sorting of a prototypical sequence-dependent recycling receptor, the beta-2 adrenergic receptor, from bulk recycling proteins and the degrading delta-opioid receptor. Our results reveal a remarkable diversity in recycling routes at the level of individual endosomes, and indicate that sequence-dependent recycling is an active process mediated by distinct endosomal subdomains distinct from those mediating bulk recycling. We identify a specialized subset of tubular microdomains on endosomes, stabilized by a highly localized but dynamic actin machinery, that mediate this sorting, and provide evidence that these actin-stabilized domains provide the physical basis for a two-step kinetic and affinity-based model for protein sorting into the sequence-dependent recycling pathway.Entities:
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Year: 2010 PMID： 21111236 PMCID： PMC3058345 DOI： 10.1016/j.cell.2010.10.003
Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582