| First Author | Hishiya A | Year | 2006 |
| Journal | EMBO J | Volume | 25 |
| Issue | 3 | Pages | 554-64 |
| PubMed ID | 16424905 | Mgi Jnum | J:105931 |
| Mgi Id | MGI:3617040 | Doi | 10.1038/sj.emboj.7600945 |
| Citation | Hishiya A, et al. (2006) A novel ubiquitin-binding protein ZNF216 functioning in muscle atrophy. EMBO J 25(3):554-64 |
| abstractText | The ubiquitin-proteasome system (UPS) is critical for specific degradation of cellular proteins and plays a pivotal role on protein breakdown in muscle atrophy. Here, we show that ZNF216 directly binds polyubiquitin chains through its N-terminal A20-type zinc-finger domain and associates with the 26S proteasome. ZNF216 was colocalized with the aggresome, which contains ubiquitinylated proteins and other UPS components. Expression of Znf216 was increased in both denervation- and fasting-induced muscle atrophy and upregulated by expression of constitutively active FOXO, a master regulator of muscle atrophy. Mice deficient in Znf216 exhibited resistance to denervation-induced atrophy, and ubiquitinylated proteins markedly accumulated in neurectomized muscle compared to wild-type mice. These data suggest that ZNF216 functions in protein degradation via the UPS and plays a crucial role in muscle atrophy. |
