Abstract
We have studied the effects of various PDB-causing mutations of SQSTMl on the in vitro ubiquitin-binding properties of the p62 protein. All mutations caused loss of monoubiquitin-binding and impaired K48-linked polyubiquitin-binding, which was only evident at physiological temperature. This suggests that SQSTMI mutations predispose to PDB through a common mechanism that depends on loss of ubiquitin-binding by p62.
| Original language | English |
|---|---|
| Pages (from-to) | 619-624 |
| Number of pages | 5 |
| Journal | Journal of Bone and Mineral Research |
| Volume | 20 |
| Issue number | 4 |
| Early online date | 6 Dec 2004 |
| DOIs | |
| Publication status | Published - Apr 2005 |
Keywords
- SQSTM1
- p62
- ubiquitin
- Paget's disease of bone
- ubiquitin-associated domain
- familial expansile osteolysis
- interacting protein P62
- UBA domain
- gene
- TNFRSF11A
- rank
- osteoclastogenesis
- duplication
- pathway