Ccr4-Not complex subunits Ccr4, Caf1, and Not4 are novel proteolysis factors promoting the degradation of ubiquitin-dependent substrates by the 26S proteasome
- 1 May 2021
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Vol. 1868 (6) , 119010
Abstract
No abstract availableKeywords
Funding Information
- Department of Biotechnology Ministry of Science and Technology
- Anusandhan National Research Foundation
This publication has 78 references indexed in Scilit:
- The structural basis for the interaction between the CAF1 nuclease and the NOT1 scaffold of the human CCR4–NOT deadenylase complexNucleic Acids Research, 2012
- Rpn1 and Rpn2 Coordinate Ubiquitin Processing Factors at ProteasomeJournal of Biological Chemistry, 2012
- Obesity resistance and increased hepatic expression of catabolism‐related mRNAs in Cnot3+/− miceThe EMBO Journal, 2011
- The Cdc48 ATPase modulates the interaction between two proteolytic factors Ufd2 and Rad23Proceedings of the National Academy of Sciences, 2011
- The N‐end rule pathway and regulation by proteolysisProtein Science, 2011
- The N-end rule pathway is mediated by a complex of the RING-type Ubr1 and HECT-type Ufd4 ubiquitin ligasesNature Cell Biology, 2010
- Polyubiquitination of the demethylase Jhd2 controls histone methylation and gene expressionGenes & Development, 2009
- Proteasome subunit Rpn13 is a novel ubiquitin receptorNature, 2008
- CCR4/NOT complex associates with the proteasome and regulates histone methylationProceedings of the National Academy of Sciences, 2007
- The N-end rule is mediated by the UBC2(RAD6) ubiquitin-conjugating enzyme.Proceedings of the National Academy of Sciences, 1991