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Vol. 12, Issue 2, 421-435, February 2001
Department of Biochemistry, Molecular Biology, and Cell Biology,
Northwestern University, Evanston, Illinois 60208
Yeast Rsp5p and its mammalian homologue, Nedd4, are
hect domain ubiquitin-protein ligases (E3s) required for
the ubiquitin-dependent endocytosis of plasma membrane proteins.
Because ubiquitination is sufficient to induce internalization,
E3-mediated ubiquitination is a key regulatory event in plasma membrane
protein endocytosis. Rsp5p is an essential, multidomain protein
containing an amino-terminal C2 domain, three WW protein-protein
interaction domains, and a carboxy-terminal hect domain
that carries E3 activity. In this study, we demonstrate that Rsp5p is
peripherally associated with membranes and provide evidence that Rsp5p
functions as part of a multimeric protein complex. We define the
function of Rsp5p and its domains in the ubiquitin-dependent
internalization of the yeast 
-factor receptor, Ste2p.
Temperature-sensitive rsp5 mutants were unable to
ubiquitinate or to internalize Ste2p at the nonpermissive temperature.
Deletion of the entire C2 domain had no effect on -factor
internalization; however, point mutations in any of the three WW
domains impaired both receptor ubiquitination and internalization.
These observations indicate that the WW domains play a role in the
important regulatory event of selecting phosphorylated proteins as
endocytic cargo. In addition, mutations in the C2 and WW1 domains had
more severe defects on transport of fluid-phase markers to the vacuole
than on receptor internalization, suggesting that Rsp5p functions at
multiple steps in the endocytic pathway.
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