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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Reverse endocytosis of transmembrane ephrin-B ligands via a clathrin-mediated pathway.

Eph/ephrin receptors and ligands mediate cell-cell interaction through reciprocal signaling upon juxtacrine contact, and play a critical role in embryonic patterning, neuronal targeting, and vascular assembly. To study transmembrane ephrin-B ligand trafficking, we determined the cellular localization of ephrin-B1-GFP upon engagement by EphB1. Under normal culture conditions ephrin-B1-GFP is localized to the plasma membrane, mostly at the lateral cell borders. Addition of soluble EphB1-Fc receptor induces ephrin-B1-GFP clustering on the cell surface and subsequent internalization, as judged by biochemical studies, electron microscopy, and co-localization with endosomal markers. A dominant-negative mutant of dynamin or potassium depletion blocks ephrin-B1 endocytosis. These results suggest that ephrin-B1 internalization is an active receptor-mediated process that utilizes the clathrin-mediated endocytic pathway.[1]

References

  1. Reverse endocytosis of transmembrane ephrin-B ligands via a clathrin-mediated pathway. Parker, M., Roberts, R., Enriquez, M., Zhao, X., Takahashi, T., Pat Cerretti, D., Daniel, T., Chen, J. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
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