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*
Intramural Research Support Program, Science Application International Corp.-Frederick, and
Basic Research Laboratory, Division of Basic Sciences, National Cancer Institute-Frederick Cancer Research and Development Center, Frederick, MD 21702;
Department of Medicine and Biochemistry/Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202; and
Department of Integrative Biology and Pharmacology, University of Texas, Houston, TX 77030
The ubiquitin-dependent proteasome-mediated (Ub-Pr) degradation
pathway has been shown to regulate a large variety of substrates,
including nuclear, cytosolic, and membrane proteins. In mammalian
systems, polyubiquitin modification has been identified in a number of
cell surface receptors for more than a decade; however, its biological
significance has remained unclear until recently. For growth factor
receptors with intrinsic tyrosine kinase domains, polyubiquitination is
believed to trigger the internalization and subsequent degradation via
the lysosomal pathway. In this study we provide the first evidence that
non-tyrosine kinase-type cytokine surface receptors, IL-9R 
-chain,
IL-2 receptor 
-chain, and erythropoietin receptor, can be
polyubiquitinated and degraded by proteasomes. The Ub-Pr pathway
regulates both the basal level turnover and the ligand-induced
degradation of the receptors. A previously identified putative
molecular chaperon, valosin-containing protein, undergoes tyrosine
phosphorylation in a cytokine-dependent manner and associates with the
receptor complexes following receptor engagement, suggesting that
valosin-containing protein may target the ubiquitinated receptors to
the proteasome for degradation.
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