Clathrin internalises EPH:EFN complexes

Stable Identifier
Reaction [omitted]
Homo sapiens
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During endocytosis the EPH-ephrin (EFN) intact complex and, possibly, associated cytoplasmic proteins, together with the surrounding plasma membrane, can be internalized into the EPH- or EFN-expressing cell. The clathrin pathway has been linked to EFNB endocytosis. C-terminal portion of EFNB1 encodes a putative endocytosis signal, a sequence that is recognized by the clathrin-associated adapter proteins required for loading molecules into clathrin-coated pits and vesicles. Treatment of cells expressing GFP-tagged EFNB1 with soluble, recombinant EPHB1/Fc fusion protein were internalized and observed in clathrin-coated vesicles. Internalized EFNB1 co-localizes with EEA1, an endosomal marker. EFNB1 internalization is inhibited by a dominant-negative dynamin mutant and potassium depletion. These results suggest that classical, clathrin-dependent endocytosis is responsible for EFNB internalization. (Parker at al. 2004).

Literature References
PubMed ID Title Journal Year
15351694 Reverse endocytosis of transmembrane ephrin-B ligands via a clathrin-mediated pathway

Daniel, T, Enriquez, M, Chen, J, Pat Cerretti, D, Takahashi, T, Parker, M, Zhao, X, Roberts, R

Biochem. Biophys. Res. Commun. 2004
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