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Vol. 12, No. 23, pp. 3663-3674, December 1, 1998
Departments of
1 Biological Regulation and
2 Molecular Cell Biology, The Weizmann Institute of Science,
Rehovot 76100, Israel;
3 Department of Pathology, The
University of Western Australia, Queen Elizabeth II Medical Center,
Nedlands, Western Australia 6907, Australia;
4 Molecular
Oncology Unit, DIBIT, and Instituto di Neuroscienze e Biommagini del
CNR, H.S. Raffaele, Milan 20132, Italy
Ligand-induced down-regulation of two growth factor receptors, EGF
receptor (ErbB-1) and ErbB-3, correlates with differential ability to
recruit c-Cbl, whose invertebrate orthologs are negative regulators of
ErbB. We report that ligand-induced degradation of internalized ErbB-1,
but not ErbB-3, is mediated by transient mobilization of a minor
fraction of c-Cbl into ErbB-1-containing endosomes. This recruitment
depends on the receptor's tyrosine kinase activity and an intact
carboxy-terminal region. The alternative fate is recycling of
internalized ErbBs to the cell surface. Cbl-mediated receptor sorting
involves covalent attachment of ubiquitin molecules, and subsequent
lysosomal and proteasomal degradation. The oncogenic viral form of Cbl
inhibits down-regulation by shunting endocytosed receptors to the
recycling pathway. These results reveal an endosomal sorting machinery
capable of controlling the fate, and, hence, signaling potency, of
growth factor receptors.
[Key Words: Endocytosis; ErbB/HER; protein degradation; signal transduction; tyrosine kinase]
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