Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis

Susan C. Shih, David J Katzmann, Joshua D. Schnell, Myra Sutanto, Scott D. Emr, Linda Hicke

Research output: Contribution to journalArticle

342 Citations (Scopus)

Abstract

Ubiquitin functions as a signal for sorting cargo at multiple steps of the endocytic pathway and controls the activity of trans-acting components of the endocytic machinery (reviewed in refs 1 and 2). By contrast to proteasome degradation, which generally requires a polyubiquitin chain that is at least four subunits long3,4, internalization and sorting of endocytic cargo at the late endosome are mediated by mono-ubiquitination5-8. Here, we demonstrate that ubiquitin-interacting motifs (UIMs) found in epsins and Vps27p (ref. 9) from Saccharomyces cerevisiae are required for ubiquitin binding and protein transport. Epsin UIMs are important for the internalization of receptors into vesicles at the plasma membrane. Vps27p UIMs are necessary to sort biosynthetic and endocytic cargo into vesicles that bud into the lumen of a late endosomal compartment, the multivesicular body. We propose that mono-ubiquitin regulates internalization and endosomal sorting by interacting with modular ubiquitin-binding domains in core components of the protein transport machinery. UIM domains are found in a broad spectrum of proteins, consistent with the idea that mono-ubiquitin can function as a regulatory signal to control diverse biological activities.

Original languageEnglish (US)
Pages (from-to)389-393
Number of pages5
JournalNature Cell Biology
Volume4
Issue number5
DOIs
StatePublished - 2002
Externally publishedYes

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Ubiquitin
Endocytosis
Protein Transport
Polyubiquitin
Multivesicular Bodies
epsin
Endosomes
Proteasome Endopeptidase Complex
Saccharomyces cerevisiae
Carrier Proteins
Cell Membrane

ASJC Scopus subject areas

  • Cell Biology

Cite this

Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis. / Shih, Susan C.; Katzmann, David J; Schnell, Joshua D.; Sutanto, Myra; Emr, Scott D.; Hicke, Linda.

In: Nature Cell Biology, Vol. 4, No. 5, 2002, p. 389-393.

Research output: Contribution to journalArticle

Shih, Susan C. ; Katzmann, David J ; Schnell, Joshua D. ; Sutanto, Myra ; Emr, Scott D. ; Hicke, Linda. / Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis. In: Nature Cell Biology. 2002 ; Vol. 4, No. 5. pp. 389-393.
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