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J Biol Chem, Vol. 274, Issue 5, 3141-3150, January 29, 1999
From the Ligand binding causes the epidermal growth factor
(EGF) receptor to undergo accelerated internalization with eventual
degradation in lysosomes. The goal of this study was to investigate the
molecular basis of endocytic sorting, focussing on post-internalization events. We have identified a sequence located between amino acid residues 675 and 697, encompassing a dileucine motif at residues 679 and 680, that enhances endosome-to-lysosome transport when conformational restraints in the EGF receptor carboxyl terminus are
removed by truncation. The same dileucine motif is also necessary for
efficient lysosomal transport of ligand-occupied full-length EGF
receptors. A L679A,L680A substitution diminished the degradation of
occupied full-length EGF receptors without affecting internalization but had a significant effect on recycling. Rapid recycling of mutant
receptors resulted in reduced intracellular retention of occupied EGF
receptors and delayed down-regulation of cell surface receptors. We
propose that the L679A,L680A substitution acts primarily to impair
transport of ligand-receptor complexes through an early endosomal
compartment, diverting occupied receptors to a recycling compartment at
the expense of incorporation into lysosome transport vesicles. We also
found that mutant receptors with truncations at the distal half of
tyrosine kinase domain (residues 809-957) were not efficiently
delivered to the cell surface but were destroyed in an endoplasmic
reticulum-associated degradative pathway.
A Leucine-based Determinant in the Epidermal Growth Factor
Receptor Juxtamembrane Domain Is Required for the Efficient Transport
of Ligand-Receptor Complexes to Lysosomes
,, and¶
Department of Physiology and Biophysics,
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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