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 journalArticlepeer-review

17 Scopus citations


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
Issue number46
StatePublished - 2009

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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