The HECT Domain of the Ubiquitin Ligase Rsp5 Contributes to Substrate Recognition
Open Access
- 1 November 2009
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 284 (46) , 32126-32137
- https://doi.org/10.1074/jbc.m109.048629
Abstract
No abstract availableThis publication has 56 references indexed in Scilit:
- Control of the activity of WW‐HECT domain E3 ubiquitin ligases by NDFIP proteinsEMBO Reports, 2009
- Opposing Activities of the Snx3-Retromer Complex and ESCRT Proteins Mediate Regulated Cargo Sorting at a Common EndosomeMolecular Biology of the Cell, 2008
- Arrestin-Related Ubiquitin-Ligase Adaptors Regulate Endocytosis and Protein Turnover at the Cell SurfaceCell, 2008
- Arrestin‐like proteins mediate ubiquitination and endocytosis of the yeast metal transporter Smf1EMBO Reports, 2008
- Ear1p and Ssh4p Are New Adaptors of the Ubiquitin Ligase Rsp5p for Cargo Ubiquitylation and Sorting at Multivesicular BodiesMolecular Biology of the Cell, 2008
- Characterization of Multiple Multivesicular Body Sorting Determinants within Sna3: A Role for the Ubiquitin Ligase Rsp5Molecular Biology of the Cell, 2007
- Direct Binding to Rsp5 Mediates Ubiquitin-independent Sorting of Sna3 via the Multivesicular Body PathwayMolecular Biology of the Cell, 2007
- Hse1, a Component of the Yeast Hrs-STAM Ubiquitin-sorting Complex, Associates with Ubiquitin Peptidases and a Ligase to Control Sorting Efficiency into Multivesicular BodiesMolecular Biology of the Cell, 2007
- Regulation of Smurf2 Ubiquitin Ligase Activity by Anchoring the E2 to the HECT DomainMolecular Cell, 2005
- The Nedd4 family of E3 ubiquitin ligases: functional diversity within a common modular architectureOncogene, 2004