Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4.
basic_science · Level V
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- Record sourced from PubMed, PMID 24969970.
- Also identified by DOI 10.1038/ncomms5217 and PMC identifier 4083429.
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Abstract
The small ubiquitin-like modifier (SUMO) can form polymeric chains that are important signals in cellular processes such as meiosis, genome maintenance and stress response. The SUMO-targeted ubiquitin ligase RNF4 engages with SUMO chains on linked substrates and catalyses their ubiquitination, which targets substrates for proteasomal degradation. Here we use a segmental labelling approach combined with solution nuclear magnetic resonance (NMR) spectroscopy and biochemical characterization to reveal how RNF4 manipulates the conformation of the SUMO chain, thereby facilitating optimal delivery of the distal SUMO domain for ubiquitin transfer.
Medical subject headings
- Nuclear Proteins
- Protein Interaction Mapping
- Small Ubiquitin-Related Modifier Proteins
- Transcription Factors
- Ubiquitination