Mechanisms and function of substrate recruitment by F-box proteins
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TLDR
The evolution of substrate recruitment by F-box proteins, the dysregulation of substrates in disease and potential avenues for F- box protein-directed disease therapies are focused on.Abstract:
S phase kinase-associated protein 1 (SKP1)-cullin 1 (CUL1)-F-box protein (SCF) ubiquitin ligase complexes use a family of F-box proteins as substrate adaptors to mediate the degradation of a large number of regulatory proteins involved in diverse processes The dysregulation of SCF complexes and their substrates contributes to multiple pathologies In the 14 years since the identification and annotation of the F-box protein family, the continued identification and characterization of novel substrates has greatly expanded our knowledge of the regulation of substrate targeting and the roles of F-box proteins in biological processes Here, we focus on the evolution of our understanding of substrate recruitment by F-box proteins, the dysregulation of substrate recruitment in disease and potential avenues for F-box protein-directed disease therapiesread more
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Journal ArticleDOI
O2 sensing–associated glycosylation exposes the F-box–combining site of the Dictyostelium Skp1 subunit in E3 ubiquitin ligases
M. Osman Sheikh,David F. Thieker,Gordon R. Chalmers,Christopher M. Schafer,Mayumi Ishihara,Parastoo Azadi,Robert J. Woods,John Glushka,Brad Bendiak,James H. Prestegard,Christopher M. West +10 more
TL;DR: An unprecedented view of how a glycan modification influences a disordered region of a full-length protein is offered and the increased sampling of an open Skp1 conformation can explain how glycosylation enhances interactions with F-box proteins in cells.
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FBXO31 protects against genomic instability by capping FOXM1 levels at the G2/M transition.
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Regulation of the ubiquitylation and deubiquitylation of CREB-binding protein modulates histone acetylation and lung inflammation.
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