The HECT domain of the ubiquitin ligase Rsp5 contributes to substrate recognition

Jacqueline R R Lee, Andrea J. Oestreich, Johanna A. Payne, Mia S. Gunawan, Andrew P. Norgan, David J Katzmann

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Ubiquitin modification of endosomal membrane proteins is a signal for active inclusion into the Multivesicular Body (MVB) pathway, resulting in lysosomal degradation. However, the endosome represents a dynamic site of protein sorting with a majority of proteins destined for recycling, rather than MVB targeting. Substrate recognition by ubiquitin ligases is therefore highly regulated. We have investigated substrate recognition by the Nedd4 ortholog Rsp5 as a model for understanding ligasesubstrate interactions. Rsp5 interacts directly with its substrate Cps1 via a novel interaction mode. Perturbation of this mode of interaction revealed a compensatory role for the Rsp5 adaptor Bsd2. These results highlight the ability of Rsp5 to interact with substrates via multiple modalities, suggesting additional mechanisms of regulating this interaction and relevant outcomes.

Original languageEnglish (US)
Pages (from-to)32126-32137
Number of pages12
JournalJournal of Biological Chemistry
Volume284
Issue number46
DOIs
StatePublished - 2009

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Multivesicular Bodies
Ligases
Ubiquitin
Endosomes
Recycling
Protein Transport
Substrates
Membrane Proteins
Sorting
Proteins
Degradation

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

The HECT domain of the ubiquitin ligase Rsp5 contributes to substrate recognition. / Lee, Jacqueline R R; Oestreich, Andrea J.; Payne, Johanna A.; Gunawan, Mia S.; Norgan, Andrew P.; Katzmann, David J.

In: Journal of Biological Chemistry, Vol. 284, No. 46, 2009, p. 32126-32137.

Research output: Contribution to journalArticle

Lee, Jacqueline R R ; Oestreich, Andrea J. ; Payne, Johanna A. ; Gunawan, Mia S. ; Norgan, Andrew P. ; Katzmann, David J. / The HECT domain of the ubiquitin ligase Rsp5 contributes to substrate recognition. In: Journal of Biological Chemistry. 2009 ; Vol. 284, No. 46. pp. 32126-32137.
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