Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 29, Issue -, Pages 488-493Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST0290488
Keywords
degradation; EGF receptor; endocytosis; lysosome; ubiquitination
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The growth hormone (GH) receptor (GHR) is a mammalian plasma membrane protein whose internalization is mediated by the ubiquitin-proteasome pathway. GH internalization and degradation are inhibited when cells are treated with proteasome inhibitors. Here we show that a GHR truncated at residue 369 can enter the cells in the presence of a proteasome inhibitor, but that the subsequent lysosomal degradation of GH is blocked. Lysosomal inhibitors prolong the half-life of both receptor and ligand. Experiments with antibodies against different receptor tail sections show that degradation of the GHR cytosolic domain precedes degradation of the extracellular GH-binding domain. A possible role for the ubiquitin-proteasome pathway in the degradation of the receptor and ligand is discussed.
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