| First Author | Kamiya Y | Year | 2012 |
| Journal | FEBS Lett | Volume | 586 |
| Issue | 8 | Pages | 1141-6 |
| PubMed ID | 22575648 | Mgi Jnum | J:201294 |
| Mgi Id | MGI:5512939 | Doi | 10.1016/j.febslet.2012.03.027 |
| Citation | Kamiya Y, et al. (2012) NMR characterization of the interaction between the PUB domain of peptide:N-glycanase and ubiquitin-like domain of HR23. FEBS Lett 586(8):1141-6 |
| abstractText | PUB domains are identified in several proteins functioning in the ubiquitin (Ub)-proteasome system and considered as p97-binding modules. To address the further functional roles of these domains, we herein characterized the interactions of the PUB domain of peptide:N-glycanase (PNGase) with Ub and Ub-like domain (UBL) of the proteasome shuttle factor HR23. NMR data indicated that PNGase-PUB exerts an acceptor preferentially for HR23-UBL, electrostatically interacting with the UBL surface employed for binding to other Ub/UBL motifs. Our findings imply that PNGase-PUB serves not only as p97-binding module but also as a possible activator of HR23 in endoplasmic reticulum-associated degradation mechanisms. |
