The DOI matches its Crossref record; 88 of the 88 references it cites were found in a registry or an index.
E2-RING Expansion of the NEDD8 Cascade Confers Specificity to Cullin Modification
Open accessAbstract
Summary Ubiquitin and ubiquitin-like proteins (UBLs) are directed to targets by cascades of E1, E2, and E3 enzymes. The largest ubiquitin E3 subclass consists of cullin-RING ligases (CRLs), which contain one each of several cullins (CUL1, 2, 3, 4, or 5) and RING proteins (RBX1 or 2). CRLs are activated by ligation of the UBL NEDD8 to a conserved cullin Lys. How is cullin NEDD8ylation specificity established? Here we report that like UBE2M (aka UBC12), the previously uncharacterized E2 UBE2F is a NEDD8 conjugating enzyme in vitro and in vivo. Biochemical and structural analyses indicate how plasticity of hydrophobic E1–E2 interactions and E1 conformational flexibility allow one E1 to charge multiple E2s. The E2s have distinct functions, with UBE2M/RBX1 and UBE2F/RBX2 displaying different target cullin specificities. Together, these studies reveal the molecular basis for and functional importance of hierarchical expansion of the NEDD8 conjugation system in establishing selective CRL activation.
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Metadata
- Authors
- Huang, D. T., Ayrault, O., Hunt, H. W., Taherbhoy, A. M., Duda, D. M., Scott, D. C., Borg, L. A., Neale, G., Murray, P. J., Roussel, M. F., & Schulman, B. A.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2009-02
- Volume
- 33
- Issue
- 4
- Pages
- 483-495
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W1982834717
- Cited by
- 282
- References
- 88
- FWCI
- 8.04
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Huang, D. T., Ayrault, O., Hunt, H. W., Taherbhoy, A. M., Duda, D. M., Scott, D. C., Borg, L. A., Neale, G., Murray, P. J., Roussel, M. F., & Schulman, B. A. (2009). E2-RING Expansion of the NEDD8 Cascade Confers Specificity to Cullin Modification. Molecular Cell. https://doi.org/10.1016/j.molcel.2009.01.011
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