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J Biol Chem, Vol. 275, Issue 3, 1575-1580, January 21, 2000
From the Department of Cell Biology, University Medical Center
Utrecht and Institute of Biomembranes, Heidelberglaan 100, AZU-G02.525,
3584CX Utrecht, The Netherlands
The ubiquitin conjugation system is involved in
ligand-induced endocytosis of the growth hormone receptor (GHR) via a
cytosolic 10-amino acid ubiquitin-dependent endocytosis
motif. Herein, we demonstrate that the proteasome is also involved in
growth hormone receptor down-regulation. Ligand-induced degradation was
blocked in the presence of specific proteasomal inhibitors. In
addition, growth hormone (GH) internalization was inhibited, whereas
the transferrin receptor cycle remained unaffected. A truncated GHR entered the cells independent of proteasome action. In addition, we
show that GH internalization is independent of the presence of lysine
residues in the cytosolic domain of the receptor, whereas its
internalization can still be inhibited by proteasomal inhibitors. Thus,
GHR internalization requires proteasome action in addition to an active
ubiquitin conjugation system, but ubiquitination of the GHR itself
seems not to be required.
Endocytosis and Degradation of the Growth Hormone Receptor Are
Proteasome-dependent*
,
*
This work was supported by Grants NWO-902-23-188 and
NWO-902-68-244 from the Netherlands Organization for Scientific
Research and by European Union Network Grant ERBFMRXCT96-0026.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Dept. of Nephrology and Hypertension, AZU,
Utrecht, The Netherlands.
§
To whom correspondence should be addressed. Tel.: 31-30-2506476;
Fax: 31-30-2541797; E-mail: strous@med.uu.nl.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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