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Gln40 deamidation blocks structural reconfiguration and activation of SCF ubiquitin ligase complex by Nedd8
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Gln40 deamidation blocks structural reconfiguration and activation of SCF ubiquitin ligase complex by Nedd8
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Journal Article
Gln40 deamidation blocks structural reconfiguration and activation of SCF ubiquitin ligase complex by Nedd8
2015
Overview
The full enzymatic activity of the cullin-RING ubiquitin ligases (CRLs) requires a ubiquitin-like protein (that is, Nedd8) modification. By deamidating Gln40 of Nedd8 to glutamate (Q40E), the bacterial cycle-inhibiting factor (Cif) family is able to inhibit CRL E3 activities, thereby interfering with cellular functions. Despite extensive structural studies on CRLs, the molecular mechanism by which Nedd8 Gln40 deamidation affects CRL functions remains unclear. We apply a new quantitative cross-linking mass spectrometry approach to characterize three different types of full-length human Cul1–Rbx1 complexes and uncover major Nedd8-induced structural rearrangements of the CRL1 catalytic core. More importantly, we find that those changes are not induced by Nedd8(Q40E) conjugation, indicating that the subtle change of a single Nedd8 amino acid is sufficient to revert the structure of the CRL catalytic core back to its unmodified form. Our results provide new insights into how neddylation regulates the conformation and activity of CRLs.
Cullin-RING ubiquitin ligases (CRLs) require neddylation of their cullin scaffolds for full activity. Here the authors use a quantitative cross-linking mass spectrometry approach to characterize three different full-length human Cul1-Rbx1 complexes to shed light on how neddylation regulates the activity of CRLs.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 82/58
/ Carrier Proteins - chemistry
/ Carrier Proteins - metabolism
/ Cullin Proteins - metabolism
/ Humanities and Social Sciences
/ Humans
/ Science
/ SKP Cullin F-Box Protein Ligases - chemistry
/ SKP Cullin F-Box Protein Ligases - genetics
/ SKP Cullin F-Box Protein Ligases - metabolism
/ Ubiquitin-Protein Ligases - chemistry
/ Ubiquitin-Protein Ligases - genetics
