| First Author | Waters S | Year | 2009 |
| Journal | FEBS Lett | Volume | 583 |
| Issue | 12 | Pages | 1846-52 |
| PubMed ID | 19427866 | Mgi Jnum | J:150016 |
| Mgi Id | MGI:3849541 | Doi | 10.1016/j.febslet.2009.04.049 |
| Citation | Waters S, et al. (2009) Interactions with LC3 and polyubiquitin chains link nbr1 to autophagic protein turnover. FEBS Lett 583(12):1846-52 |
| abstractText | Nbr1, a ubiquitous kinase scaffold protein, contains a PB1, and a ubiquitin-associated (UBA) domain. We show here that the nbr1 UBA domain binds to lysine-48 and -63 linked polyubiquitin-B chains. Nbr1 also binds to the autophagic effector protein LC3-A via a novel binding site. Ubiquitin-binding, but not PB1-mediated p62/SQSTM1 interaction, is required to target nbr1 to LC3 and polyubiquitin-positive bodies. Nbr1 binds additionally to proteins implicated in ubiquitin-mediated protein turnover and vesicle trafficking: ubiquitin-specific peptidases USP8, and the endosomal transport regulator p14/Robld3. Nbr1 thus contributes to specific steps in protein turnover regulation disrupted in several hereditary human diseases. |
