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J Biol Chem, Vol. 275, Issue 18, 13940-13947, May 5, 2000
From the Institute of Pathology, University of Oslo, National
Hospital, 0027 Oslo, Norway
We have previously shown that, although
overexpression of mutant dynamin inhibits
clathrin-dependent endocytosis and disrupts high affinity
binding of epidermal growth factor (EGF) to the EGF receptor (EGFR), it
does not inhibit ligand-induced translocation of the EGFR into
clathrin-coated pits. In the present study, we demonstrate that, upon
ligand binding and incubation at 37 °C, the EGFR was
polyubiquitinated regardless of overexpression of mutant dynamin. In
cells not overexpressing mutant dynamin, the EGFR was rapidly
internalized and deubiquitinated. In cells being endocytosis-deficient,
due to overexpression of mutant dynamin, however, the EGFR was upon
prolonged chase first found in deeply invaginated coated pits, and then
eventually moved out of the coated pits and back onto the smooth plasma
membrane. Polyubiquitination occurred equally efficiently in cells with
or without intact clathrin-dependent endocytosis, while the
kinetics of ubiquitination and deubiquitination was somewhat different.
We further found that the EGF-induced ubiquitination of Eps15 occurred
both in the absence and presence of endocytosis with the same kinetics
as polyubiquitination of the EGFR, but that the EGF-induced
monoubiquitination of Eps15 was somewhat reduced upon overexpression of
mutant dynamin. Our data show that EGF-induced polyubiquitination of
the EGFR occurs at the plasma membrane.
Polyubiquitination of the Epidermal Growth Factor Receptor Occurs
at the Plasma Membrane upon Ligand-induced Activation*
,
*
This work was supported in part by the National Council for
Science and the Humanities, Medinnova, Norwegian Cancer Society, Novo
Foundation, Anders Jahre's Foundation for the Promotion of Science,
Blix Legacy, Bruun's Legacy, and Bull's Legacy.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.
Supported by a research fellowship from the Norwegian Cancer
Society. To whom all correspondence should be addressed. E-mail: espenst@ulrik.uio.no.
§
Supported by a fellowship from the National Council for Science and
the Humanities.
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