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J. Biol. Chem., Vol. 277, Issue 34, 30746-30753, August 23, 2002
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From Molecular Cell Biology, Institute of Biomembranes,
Universiteit Utrecht, 3584 CH Utrecht, The Netherlands
An important negative control mechanism in the
signaling of epidermal growth factor (EGF) is the endocytosis and
subsequent degradation of activated EGF receptors. Eps15 and its
related partner Eps15R play a key role in clathrin-mediated endocytosis of transmembrane receptors. Upon EGF stimulation of the cell, Eps15
becomes both phosphorylated on tyrosine residues and monoubiquitinated. Although tyrosine phosphorylation of Eps15 has been implicated in EGF
receptor internalization, the function of Eps15 ubiquitination is not
known. Using a mutational approach, we have found that the second
ubiquitin-interacting motif (UIM) of Eps15 and Eps15R is essential for
their ubiquitination. This UIM partially overlaps with the recently
characterized nuclear export signal in Eps15. We show that these
two overlapping motifs have different structural requirements with
respect to nuclear export signal versus ubiquitination signal activity. Our data demonstrate that the UIM does not contain the
ubiquitin acceptor site but functions as a recruitment site for the
ubiquitination machinery leading to the monoubiquitination of both
Eps15 and Eps15R.
A Ubiquitin-interacting Motif (UIM) Is Essential for Eps15 and
Eps15R Ubiquitination*
*
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.
To whom correspondence should be addressed: Molecular Cell
Biology, Inst. of Biomembranes, Universiteit Utrecht, Padualaan 8, 3584 CH Utrecht, The Netherlands. Tel.: 31-30-253-3349; Fax: 31-30-251-3655;
E-mail: bergenp@bio.uu.nl.
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