| First Author | Bernot KM | Year | 2005 |
| Journal | J Cell Biol | Volume | 168 |
| Issue | 6 | Pages | 965-74 |
| PubMed ID | 15767464 | Mgi Jnum | J:98251 |
| Mgi Id | MGI:3577697 | Doi | 10.1083/jcb.200408116 |
| Citation | Bernot KM, et al. (2005) A small surface hydrophobic stripe in the coiled-coil domain of type I keratins mediates tetramer stability. J Cell Biol 168(6):965-74 |
| abstractText | Intermediate filaments (IFs) are fibrous polymers encoded by a large family of differentially expressed genes that provide crucial structural support in the cytoplasm and nucleus in higher eukaryotes. The mechanisms involved in bringing together approximately 16 elongated coiled-coil dimers to form an IF are poorly defined. Available evidence suggests that tetramer subunits play a key role during IF assembly and regulation. Through molecular modeling and site-directed mutagenesis, we document a hitherto unnoticed hydrophobic stripe exposed at the surface of coiled-coil keratin heterodimers that contributes to the extraordinary stability of heterotetramers. The inability of K16 to form urea-stable tetramers in vitro correlates with an increase in its turnover rate in vivo. The data presented support a specific conformation for the assembly competent IF tetramer, provide a molecular basis for their differential stability in vitro, and point to the physiological relevance associated with this property in vivo. |
