| First Author | Mishra S | Year | 2012 |
| Journal | FEBS Lett | Volume | 586 |
| Issue | 4 | Pages | 330-6 |
| PubMed ID | 22289178 | Mgi Jnum | J:200485 |
| Mgi Id | MGI:5508714 | Doi | 10.1016/j.febslet.2012.01.019 |
| Citation | Mishra S, et al. (2012) Cataract-linked gammaD-crystallin mutants have weak affinity to lens chaperones alpha-crystallins. FEBS Lett 586(4):330-6 |
| abstractText | To test the hypothesis that alpha-crystallin chaperone activity plays a central role in maintenance of lens transparency, we investigated its interactions with gamma-crystallin mutants that cause congenital cataract in mouse models. Although the two substitutions, I4F and V76D, stabilize a partially unfolded gammaD-crystallin intermediate, their affinities to alpha-crystallin are marginal even at relatively high concentrations. Detectable binding required further reduction of gammaD-crystallin stability which was achieved by combining the two mutations. Our results demonstrate that mutants and possibly age-damaged gamma-crystallin can escape quality control by lens chaperones rationalizing the observation that they nucleate protein aggregation and lead to cataract. |
