The SCF ubiquitin ligase: insights into a molecular machine
Top Cited Papers
- 1 September 2004
- journal article
- review article
- Published by Springer Nature in Nature Reviews Molecular Cell Biology
- Vol. 5 (9) , 739-751
- https://doi.org/10.1038/nrm1471
Abstract
Ubiquitin ligases are well suited to regulate molecular networks that operate on a post-translational timescale. The F-box family of proteins — which are the substrate-recognition components of the Skp1–Cul1–F-box-protein (SCF) ubiquitin ligase — are important players in many mammalian functions. Here we explore a unifying and structurally detailed view of SCF-mediated proteolytic control of cellular processes that has been revealed by recent studies.Keywords
This publication has 126 references indexed in Scilit:
- Structural principles of leucine‐rich repeat (LRR) proteinsProteins-Structure Function and Bioinformatics, 2003
- Ratchets and clocks: the cell cycle, ubiquitylation and protein turnoverNature Reviews Molecular Cell Biology, 2003
- Release of Ubiquitin-Charged Cdc34-S∼Ub from the RING Domain Is Essential for Ubiquitination of the SCFCdc4-Bound Substrate Sic1Cell, 2003
- Structure of a β-TrCP1-Skp1-β-Catenin ComplexMolecular Cell, 2003
- Structural Basis for Phosphodependent Substrate Selection and Orientation by the SCFCdc4 Ubiquitin LigaseCell, 2003
- The spindle checkpoint: structural insights into dynamic signallingNature Reviews Molecular Cell Biology, 2002
- Structural basis for the recognition of hydroxyproline in HIF-1α by pVHLNature, 2002
- Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complexNature, 2002
- IκBα Ubiquitination Is Catalyzed by an SCF-like Complex Containing Skp1, Cullin-1, and Two F-Box/WD40-Repeat Proteins, βTrCP1 and βTrCP2Biochemical and Biophysical Research Communications, 1999
- The human F box protein β-Trcp associates with the Cul1/Skp1 complex and regulates the stability of β-cateninOncogene, 1999