The retromer is a protein complex containing sorting nexin (Snx) and vacuolar protein sorting (Vps) components. It has an essential role in recycling cargo molecules from endosomes to the trans-Golgi network, and mediates certain endosome-to-plasma membrane recycling events.

Latest Research and Reviews

  • Research | | open

    Though ubiquitin is known to broadly influence endosomal trafficking, few ubiquitin-utilizing enzymes targeting endosomal regulators are known. Here, the authors find that the deubiquitylating enzyme (DUB) USP32 influences endosomal membrane dynamics by deubiquitinating Rab7.

    • Aysegul Sapmaz
    • , Ilana Berlin
    • , Erik Bos
    • , Ruud H. Wijdeven
    • , Hans Janssen
    • , Rebecca Konietzny
    • , Jimmy J. Akkermans
    • , Ayse E. Erson-Bensan
    • , Roman I. Koning
    • , Benedikt M. Kessler
    • , Jacques Neefjes
    •  & Huib Ovaa
  • Research |

    The retromer complex (the vacuolar protein sorting heterotrimer Vps26–Vps29–Vps35) has been resolved in association with membranes and the sorting nexin protein Vps5 using cryo-electron tomography.

    • Oleksiy Kovtun
    • , Natalya Leneva
    • , Yury S. Bykov
    • , Nicholas Ariotti
    • , Rohan D. Teasdale
    • , Miroslava Schaffer
    • , Benjamin D. Engel
    • , David. J. Owen
    • , John A. G. Briggs
    •  & Brett M. Collins
    Nature 561, 561-564
  • Research | | open

    Sustained Wnt secretion requires the endosomal SNX3-retromer complex for endosome-to-trans-Golgi network transport of the internalised Wnt chaperone Wntless. Here the authors show that in both C. elegans and human cells, SNX3-retromer requires an evolutionary conserved membrane remodelling complex for Wntless sorting and Wnt secretion.

    • Ian J. McGough
    • , Reinoud E. A. de Groot
    • , Adam P. Jellett
    • , Marco C. Betist
    • , Katherine C. Varandas
    • , Chris M. Danson
    • , Kate J. Heesom
    • , Hendrik C. Korswagen
    •  & Peter J. Cullen
  • Reviews |

    Endocytosed membrane proteins can either be degraded in the lysosome or recycled back to the membrane. This decision, which has an impact on protein levels, spatial distribution and function, is controlled by recycling machineries at the endosome that recognize and segregate cargo destined for recycling, thereby preventing its degradation.

    • Peter J. Cullen
    •  & Florian Steinberg
  • Research | | open

    Retromer is recruited to endosomes by the small GTPase Rab7 and sorting nexin 3. Here, the authors report the interaction between a GTPase-activating protein TBC1d5 and Rab7, examine the biochemical details of the interaction with retromer, and discuss the implications for receptor trafficking.

    • Da Jia
    • , Jin-San Zhang
    • , Fang Li
    • , Jing Wang
    • , Zhihui Deng
    • , Mark A. White
    • , Douglas G. Osborne
    • , Christine Phillips-Krawczak
    • , Timothy S. Gomez
    • , Haiying Li
    • , Amika Singla
    • , Ezra Burstein
    • , Daniel D. Billadeau
    •  & Michael K. Rosen

News and Comment

  • News and Views |

    Recycling from endosomes to the plasma membrane is an important step in cell homeostasis. The retromer/SNX27/WASH complex recycles numerous receptors, but key ones are still unaccounted for. Now a related conserved heterotrimer, called retriever, has been identified that, together with SNX17, the CCC complex and WASH, mediates the recycling of α5β1 integrins.

    • Catherine Rabouille
    Nature Cell Biology 19, 1144-1146
  • News and Views |

    Parathyroid hormone analog PTH(1–34), used clinically to treat osteoporosis, forms a stable complex with its receptor and prolongs cAMP production even after internalization and recruitment to endosomes. New data suggest this signaling cascade is stimulated by β-arrestins and terminated by retromer.

    • Jan R T van Weering
    •  & Peter J Cullen
  • Research Highlights |

    The protein complex retromer mediates the recycling of cell surface receptors that are essential for 'corpse clearance' in roundworms

    • Felix Cheung