The DOI matches its Crossref record; 94 of the 94 references it cites were found in a registry or an index.
The cullin protein family
Open accessAbstract
Cullin proteins are molecular scaffolds that have crucial roles in the post-translational modification of cellular proteins involving ubiquitin. The mammalian cullin protein family comprises eight members (CUL1 to CUL7 and PARC), which are characterized by a cullin homology domain. CUL1 to CUL7 assemble multi-subunit Cullin-RING E3 ubiquitin ligase (CRL) complexes, the largest family of E3 ligases with more than 200 members. Although CUL7 and PARC are present only in chordates, other members of the cullin protein family are found in Drosophila melanogaster, Caenorhabditis elegans, Arabidopsis thaliana and yeast. A cullin protein tethers both a substrate-targeting unit, often through an adaptor protein, and the RING finger component in a CRL. The cullin-organized CRL thus positions a substrate close to the RING-bound E2 ubiquitin-conjugating enzyme, which catalyzes the transfer of ubiquitin to the substrate. In addition, conjugation of cullins with the ubiquitin-like molecule Nedd8 modulates activation of the corresponding CRL complex, probably through conformational regulation of the interactions between cullin's carboxy-terminal tail and CRL's RING subunit. Genetic studies in several model organisms have helped to unravel a multitude of physiological functions associated with cullin proteins and their respective CRLs. CRLs target numerous substrates and thus have an impact on a range of biological processes, including cell growth, development, signal transduction, transcriptional control, genomic integrity and tumor suppression. Moreover, mutations in CUL7 and CUL4B genes have been linked to hereditary human diseases.
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Mechanisms Underlying Ubiquitination
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Function and regulation of cullin–RING ubiquitin ligases
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An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer
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Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex
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Nonproteolytic Functions of Ubiquitin in Cell Signaling
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Structure of the VHL-ElonginC-ElonginB Complex: Implications for VHL Tumor Suppressor Function
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Advancing targeted protein degradation for cancer therapy
Dale, B., Cheng, M., Park, K.-S., Kaniskan, H. Ü., Xiong, Y., & Jin, J. (2021) · Nature Reviews Cancer · doi:10.1038/s41568-021-00365-x · Cited by 632
Bulatov, E., & Ciulli, A. (2015) · Biochemical Journal · doi:10.1042/bj20141450 · Cited by 237
Cullin E3 Ligases and Their Rewiring by Viral Factors
Mahon, C., Krogan, N., Craik, C., & Pick, E. (2014) · Biomolecules · doi:10.3390/biom4040897 · Cited by 101
Understanding cullin-RING E3 biology through proteomics-based substrate identification
Harper, J. W., & Tan, M.-K. M. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r112.021154 · Cited by 66
Chen, Y.-A., Peng, Y.-J., Hu, M.-C., Huang, J.-J., Chien, Y.-C., Wu, J.-T., Chen, T.-Y., & Tang, C.-Y. (2015) · Scientific Reports · doi:10.1038/srep10667 · Cited by 61
Metadata
- Authors
- Sarikas, A., Hartmann, T., & Pan, Z.-Q.
- Venue
- Genome Biology
- Published
- 2011
- Volume
- 12
- Issue
- 4
- Pages
- 220
- ISSN
- 1465-6906 (ISSN-L)
- OpenAlex
- W2149931676
- Cited by
- 522
- References
- 94
- FWCI
- 11.64
- Type
- journal article
- Language
- en
- Open access
- gold
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