| First Author | Pessemesse L | Year | 2014 |
| Journal | FEBS Lett | Volume | 588 |
| Issue | 21 | Pages | 4037-43 |
| PubMed ID | 25263706 | Mgi Jnum | J:216450 |
| Mgi Id | MGI:5608826 | Doi | 10.1016/j.febslet.2014.09.026 |
| Citation | Pessemesse L, et al. (2014) p28, a truncated form of TRalpha1 regulates mitochondrial physiology. FEBS Lett 588(21):4037-43 |
| abstractText | We have previously identified in mitochondria two truncated forms of the T3 nuclear receptor TRalpha1, with molecular weights of 43kDa (p43) and 28kDa (p28) respectively located in the matrix and in the inner membrane. Previously, we have demonstrated that p43 stimulates mitochondrial transcription and protein synthesis in the presence of T3. Here we report that p28 is targeted into the organelle in a T3-dependent manner and displays an affinity for T3 higher than the nuclear receptor. We tried to generate mice overexpressing p28 using the human alpha-skeletal actin promoter, however we found an early embryonic lethality that was probably linked to a transient expression of p28 in trophoblast giant cells. This could be partly explained by the observation that overexpression of p28 in human fibroblasts induced alterations of mitochondrial physiology. |
