| First Author | Hirasaka K | Year | 2016 |
| Journal | Biochem Biophys Res Commun | Volume | 472 |
| Issue | 1 | Pages | 108-13 |
| PubMed ID | 26915802 | Mgi Jnum | J:333168 |
| Mgi Id | MGI:6880400 | Doi | 10.1016/j.bbrc.2016.02.075 |
| Citation | Hirasaka K, et al. (2016) UCP3 is associated with Hax-1 in mitochondria in the presence of calcium ion. Biochem Biophys Res Commun 472(1):108-13 |
| abstractText | Uncoupling protein 3 (UCP3) is known to regulate energy dissipation, proton leakage, fatty acid oxidation, and oxidative stress. To identify the putative protein regulators of UCP3, we performed yeast two-hybrid screens. Here we report that UCP3 interacted with HS-1 associated protein X-1 (Hax-1), an anti-apoptotic protein that was localized in the mitochondria, and is involved in cellular responses to Ca(2+). The hydrophilic sequences within loop 2, and the matrix-localized hydrophilic domain of mouse UCP3, were necessary for binding to Hax-1 at the C-terminal domain, adjacent to the mitochondrial inner membrane. Interestingly, interaction of these proteins occurred in a calcium-dependent manner. Moreover, the NMR spectrum of the C-terminal domain of Hax-1 was dramatically changed by removal of Ca(2+), suggesting that the C-terminal domain of Hax-1 underwent a Ca(2+)-induced conformational change. In the Ca(2+)-free state, the C-terminal Hax-1 tended to unfold, suggesting that Ca(2+) binding may induce protein folding of the Hax-1 C-terminus. These results suggested that the UCP3-Hax-1 complex may regulate mitochondrial functional changes caused by mitochondrial Ca(2+). |
