Mannose receptor polyubiquitination regulates endosomal recruitment of p97 and cytosolic antigen translocation for cross-presentation.

@article{Zehner2011MannoseRP,
  title={Mannose receptor polyubiquitination regulates endosomal recruitment of p97 and cytosolic antigen translocation for cross-presentation.},
  author={Matthias Zehner and Achmet Imam Chasan and Verena Schuette and Maria Embgenbroich and Thomas Quast and Waldemar Kolanus and Sven Burgdorf},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2011},
  volume={108 24},
  pages={9933-8}
}
The molecular mechanisms regulating noncanonical protein transport across cellular membranes are poorly understood. Cross-presentation of exogenous antigens on MHC I molecules by dendritic cells (DCs) generally requires antigen translocation from the endosomal compartment into the cytosol for proteasomal degradation. In this study, we demonstrate that such translocation is controlled by the endocytic receptor and regulated by ubiquitination. Antigens internalized by the mannose receptor (MR… CONTINUE READING
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