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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August 2001
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Conference Article|
August 01 2001
The ubiquitin-proteasome pathway regulates lysosomal degradation of the growth hormone receptor and its ligand
P. van Kerkhof;
P. van Kerkhof
1Department of Cell Biology, University Medical Center Utrecht and Institute of Biomembranes, Heidelberglaan 100, 3584 CX Utrecht, The Netherlands
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G. J. Strous
G. J. Strous
1
1Department of Cell Biology, University Medical Center Utrecht and Institute of Biomembranes, Heidelberglaan 100, 3584 CX Utrecht, The Netherlands
1To whom correspondence should be addressed (e-mail strous@med.uu.nl)
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Publisher: Portland Press Ltd
Received:
February 26 2001
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2001 Biochemical Society
2001
Biochem Soc Trans (2001) 29 (4): 488–493.
Article history
Received:
February 26 2001
Citation
P. van Kerkhof, G. J. Strous; The ubiquitin-proteasome pathway regulates lysosomal degradation of the growth hormone receptor and its ligand. Biochem Soc Trans 1 August 2001; 29 (4): 488–493. doi: https://doi.org/10.1042/bst0290488
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