Association of SAP130/SF3b-3 with Cullin-RING ubiquitin ligase complexes and its regulation by the COP9 signalosome
2008
SAP130's Role in Ubiquitin Ligase Complexes
publication
10 minutes
Evidence: moderate
Author Information
Author(s): Suchithra Menon, Tomohiko Tsuge, Naoshi Dohmae, Koji Takio, Ning Wei
Primary Institution: Yale University
Hypothesis
SAP130 may link CRL mediated ubiquitination to gene expression.
Conclusion
SAP130 is a cullin binding protein that is likely involved in the Nedd8 pathway.
Supporting Evidence
- SAP130 interacts with neddylated cullins in vivo.
- SAP130 forms tertiary complexes with active cullin-RING E3 ligases.
- The association of SAP130 with cullins is modulated by CAND1 and CSN.
- SAP130 exhibits polyubiquitination activity that can be inhibited by CSN.
Takeaway
SAP130 helps proteins called cullins work together to tag other proteins for destruction, which is important for many cell processes.
Methodology
Biochemical approaches including co-immunoprecipitation and mass spectrometry were used to identify interactions between SAP130 and cullin proteins.
Limitations
The study does not explore the specific mechanisms by which SAP130 influences cullin neddylation.
Digital Object Identifier (DOI)
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