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Paget disease of bone-associated UBA domain mutations of SQSTM1 exert distinct effects on protein structure and function
Journal article   Open access   Peer reviewed

Paget disease of bone-associated UBA domain mutations of SQSTM1 exert distinct effects on protein structure and function

Alice Goode, Jed E. Long, Barry Shaw, Stuart H. Ralston, Micaela Rios Visconti, Fernando Gianfrancesco, Teresa Esposito, Luigi Gennari, Daniela Merlotti, Domenico Rendina, …
Biochimica et biophysica acta. Molecular basis of disease, Vol.1842(7), pp.992-1000
2014
PMID: 24642144
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Abstract

Biochemistry & Molecular Biology Biophysics Cell Biology Life Sciences & Biomedicine Science & Technology
SQSTM1 mutations are common in patients with Paget disease of bone (PDB), with most affecting the C-terminal ubiquitin-associated (UBA) domain of the SQSTM1 protein. We performed structural and functional analyses of two UBA domain mutations, an I424S mutation relatively common in UK PDB patients, and an A427D mutation associated with a severe phenotype in Southern Italian patients. Both impaired SQSTM1's ubiquitin-binding function in pull-down assays and resulted in activation of basal NF-kappa B signalling, compared to wild-type, in reporter assays. We found evidence for a relationship between the ability of different UBA domain mutants to activate NF-kappa B signalling in vitro and number of affected sites in vivo in 1152 PDB patients from the UK and Italy, with A427D-SQSTM1 producing the greatest level of activation (relative to wild-type) of all PDB mutants tested to date. NMR and isothermal titration calorimetry studies were able to demonstrate that I424S is associated with global structural changes in the UBA domain, resulting in 10-fold weaker UBA dimer stability than wild-type and reduced ubiquitin-binding affinity of the UBA monomer. Our observations provide insights into the role of SQSTM1-mediated NF-kappa B signalling in PDB aetiology, and demonstrate that different mutations in close proximity within loop 2/helix 3 of the SQSTM1 UBA domain exert distinct effects on protein structure and stability, including indirect effects at the UBA/ubiquitin-binding interface. (C) 2014 The Authors. Published by Elsevier B.V.

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Collaboration types
Domestic collaboration
International collaboration
Citation topics
1 Clinical & Life Sciences
1.80 Bone Diseases
1.80.1211 Bisphosphonates
Web Of Science research areas
Biochemistry & Molecular Biology
Biophysics
Cell Biology
ESI research areas
Clinical Medicine
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