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J. Biol. Chem., Vol. 276, Issue 28, 25974-25981, July 13, 2001
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From the Department of Biochemistry, Molecular Biology, and Cell
Biology, Northwestern University, Evanston, Illinois 60208
Ubiquitination of integral plasma membrane
proteins triggers their rapid internalization into the endocytic
pathway. The yeast ubiquitin ligase Rsp5p, a homologue of mammalian
Nedd4 and Itch, is required for the ubiquitination and
subsequent internalization of multiple plasma membrane proteins,
including the
Multiple Roles for Rsp5p-dependent Ubiquitination at
the Internalization Step of Endocytosis*
and
-factor receptor (Ste2p). Here we demonstrate that
Rsp5p plays multiple roles at the internalization step of endocytosis.
Temperature-sensitive rsp5 mutant cells were defective in
the internalization of -factor by a Ste2p-ubiquitin chimera, a
receptor that does not require post-translational ubiquitination.
Similarly, a modified version of Ste2p bearing a NPFXD
linear peptide sequence as its only internalization signal was not
internalized in rsp5 cells. Internalization of these
variant receptors was dependent on the catalytic cysteine residue of
Rsp5p and on ubiquitin-conjugating enzymes that bind Rsp5p. Thus, a
Rsp5p-dependent ubiquitination event is required for
internalization mediated by ubiquitin-dependent and
-independent endocytosis signals. Constitutive Ste2p-ubiquitin
internalization and fluid-phase endocytosis also required active
ubiquitination machinery, including Rsp5p. These observations indicate
that Rsp5p-dependent ubiquitination of a trans-acting
protein component of the endocytosis machinery is required for the
internalization step of endocytosis.
*
This work was supported in part by the Burroughs Wellcome
Fund, the Searles Scholar program, and National Institutes of Health Grant R01 DK 53257.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 National Institutes of Health Training Grant T32GM08061.
§
To whom correspondence should be addressed. Tel.: 847-467-4490;
Fax: 847-467-1380; E-mail:
l-hicke@northwestern.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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