Journal
NATURE CELL BIOLOGY
Volume 9, Issue 12, Pages 1370-U55Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb1656
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Funding
- MRC [G117/554] Funding Source: UKRI
- Medical Research Council [G117/554] Funding Source: researchfish
- Medical Research Council [G117/554(71630), G117/554] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
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SNX-BAR proteins are a sub-family of sorting nexins implicated in endosomal sorting. Here, we establish that through its phox homology (PX) and Bin-Amphiphysin-Rvs ( BAR) domains, sorting nexin-4 (SNX4) is associated with tubular and vesicular elements of a compartment that overlaps with peripheral early endosomes and the juxtanuclear endocytic recycling compartment ( ERC). Suppression of SNX4 perturbs transport between these compartments and causes lysosomal degradation of the transferrin receptor (TfnR). Through an interaction with KIBRA, a protein previously shown to bind dynein light chain 1, we establish that SNX4 associates with the minus end-directed microtubule motor dynein. Although suppression of KIBRA and dynein perturbs early endosome-to-ERC transport, TfnR sorting is maintained. We propose that by driving membrane tubulation, SNX4 coordinates iterative, geometric-based sorting of the TfnR with the long-range transport of carriers from early endosomes to the ERC. Finally, these data suggest that by associating with molecular motors, SNX-BAR proteins may coordinate sorting with carrier transport between donor and recipient membranes.
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