Endocytosis and intracellular trafficking of ErbBs

By A. Sorkin, Lai Kuan Goh. Experimental Cell Research, 2008

826 citations recorded by the source corpus.

This review article describes the pathways and mechanisms of endocytosis and post-endocytic sorting of the EGF receptor (EGFR/ErbB1) and other members of the ErbB family. Growth factor binding to EGFR accelerates its internalization through clathrin-coated pits which is followed by the efficient lysosomal targeting of internalized receptors and results in receptor down-regulation. The role of EGFR interaction with the Grb2 adaptor protein and Cbl ubiquitin ligase, and receptor ubiquitination in the clathrin-dependent internalization and sorting of EGFR in multivesicular endosomes is discussed. Activation and phosphorylation of ErbB2, ErbB3 and ErbB4 also results in their ubiquitination. However, these ErbBs are internalized and targeted to lysosomes less efficiently than EGFR. When overexpressed endocytosis-impaired ErbBs may inhibit the internalization and degradation of EGFR.

Subfields: Epidemiology, Parasitology, Physiology

View Paper: https://www.semanticscholar.org/paper/2ccc8284163bfbf1ab255d8ac5d824e5b5e4cdff

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Citations in the corpus

• Endosome maturation (2011, background): “…include a variety of activated growth factor and other signalling receptors, adhesion molecules such as integrins, ion channels, and other proteins such as unassembled caveolin1 oligomers (Staub et al, 1997; Vaccari and Bilder, 2005; Sorkin and Goh, 2008; Hayer et al, 2010; Lobert et al, 2010).”
• Focus on Extracellular Vesicles: Introducing the Next Small Big Thing (2016, background): “The ILVs within the MVB are then discharged into the lysosomal lumen resulting in degradation of the ILVs and the cargo they potentially carry; this is a particularly important process for limiting activated growth factor signaling [64,65].”