SNX4 coordinates endosomal sorting of TfnR with dynein-mediated transport into the endocytic recycling compartment

Colin J. Traer, Anna C. Rutherford, Krysten J. Palmer, Thomas Wassmer, Jacqueline Oakley, Naomi Attar, Jez G. Carlton, Joachim Kremerskothen, David J. Stephens, Peter J. Cullen

Research output: Contribution to journalArticlepeer-review


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.
Original languageEnglish
Pages (from-to)1370-1380
Number of pages11
JournalNature Cell Biology
Issue number12
Publication statusPublished - 1 Dec 2007


  • cell compartmentation
  • cell membrane
  • dyneins
  • endocytosis
  • endosomes
  • HeLa cells
  • humans
  • intracellular signaling peptides and proteins
  • microtubules
  • phosphoproteins
  • protein binding
  • protein transport
  • proteins
  • transferring receptors
  • sorting nexins
  • vesicular transport proteins


Dive into the research topics of 'SNX4 coordinates endosomal sorting of TfnR with dynein-mediated transport into the endocytic recycling compartment'. Together they form a unique fingerprint.

Cite this