| Title | Signal integration and diversification through the p62 scaffold protein. |
| Publication Type | Journal Article |
| Year of Publication | 2007 |
| Authors | Moscat J, Diaz-Meco MT, Wooten MW |
| Journal | Trends Biochem Sci |
| Volume | 32 |
| Issue | 2 |
| Pagination | 95-100 |
| Date Published | 2007 Feb |
| ISSN | 0968-0004 |
| Keywords | Adaptor Proteins, Signal Transducing, Carrier Proteins, DNA-Binding Proteins, Humans, NF-kappa B, Nuclear Proteins, Sequestosome-1 Protein, Signal Transduction, TNF Receptor-Associated Factor 6, Transcription Factors, Ubiquitin |
| Abstract | Signal specificity of multifunctional enzymes is achieved through protein-protein interactions involving specific domains on scaffold proteins. p62 (also known as sequestosome 1) is such a scaffold protein that possesses PB1 and UBA domains, and the TRAF6 binding sequence. Proteins recruited to these domains enable p62 to integrate kinase-activated and ubiquitin-mediated signaling pathways. The biological function of p62 has been studied in diverse systems and processes such as osteoclastogenesis, inflammation, differentiation, neurotrophin biology and obesity. The availability of mice in which p62 has been genetically inactivated is providing new insight into the mechanism and function of p62 at a whole-organism level. |
| DOI | 10.1016/j.tibs.2006.12.002 |
| Alternate Journal | Trends Biochem Sci |
| PubMed ID | 17174552 |
Related Faculty:
Jorge Moscat, Ph.D. Maria Diaz-Meco Conde, Ph.D.