The FBXL family of F-box proteins: variations on a theme
| Autor: | Heike Laman, Bethany Mason |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Subfamily
Ubiquitin-Protein Ligases Immunology Review Review Article Computational biology Biology Leucine-Rich Repeat Proteins F-box protein General Biochemistry Genetics and Molecular Biology Substrate Specificity Structure-Activity Relationship 03 medical and health sciences 0302 clinical medicine Ubiquitin ubiquitin S-Phase Kinase-Associated Proteins lcsh:QH301-705.5 Phylogeny 030304 developmental biology 0303 health sciences F-Box Proteins e3 ubiquitin ligases General Neuroscience Cell Cycle lrr Computational Biology Proteins Gene Expression Regulation lcsh:Biology (General) Proteasome Organ Specificity Multigene Family 030220 oncology & carcinogenesis biology.protein fbxl Hydrophobic and Hydrophilic Interactions Protein Processing Post-Translational f-box protein Signal Transduction |
| Zdroj: | Open Biology, Vol 10, Iss 11 (2020) Open Biology |
| ISSN: | 2046-2441 |
| Popis: | The ubiquitin–proteasome system (UPS) is responsible for the rapid targeting of proteins for degradation at 26S proteasomes and requires the orchestrated action of E1, E2 and E3 enzymes in a well-defined cascade. F-box proteins (FBPs) are substrate-recruiting subunits of Skp1-cullin1-FBP (SCF)-type E3 ubiquitin ligases that determine which proteins are ubiquitinated. To date, around 70 FBPs have been identified in humans and can be subdivided into distinct families, based on the protein-recruiting domains they possess. The FBXL subfamily is defined by the presence of multiple leucine-rich repeat (LRR) protein-binding domains. But how the 22 FBPs of the FBXL family achieve their individual specificities, despite having highly similar structural domains to recruit their substrates, is not clear. Here, we review and explore the FBXL family members in detail highlighting their structural and functional similarities and differences and how they engage their substrates through their LRRs to adopt unique interactomes. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|