| First Author | Ceci M | Year | 2002 |
| Journal | Biochem Biophys Res Commun | Volume | 295 |
| Issue | 2 | Pages | 295-9 |
| PubMed ID | 12150946 | Mgi Jnum | J:77914 |
| Mgi Id | MGI:2182891 | Doi | 10.1016/s0006-291x(02)00671-x |
| Citation | Ceci M, et al. (2002) Formation of nuclear matrix filaments by p27(BBP)/eIF6. Biochem Biophys Res Commun 295(2):295-9 |
| abstractText | p27(BBP)/eIF6 is an evolutionarily conserved protein necessary for ribosome biogenesis which was cloned in mammals for its ability to bind the cytodomain of beta4 integrin. In cultured cells, a conspicuous fraction of p27(BBP)/eIF6 is associated with the intermediate filaments/nuclear matrix (IF/NM) cytoskeleton. The mechanism of this association is not known. Here we show that in epidermis p27(BBP)/eIF6 is naturally associated with IF/NM. To analyze the intrinsic capability of p27(BBP)/eIF6 to generate cytoskeletal networks, the properties of the pure, recombinant, untagged protein were studied. Recombinant p27(BBP)/eIF6 binds beta4 integrin. Upon dialysis against IF buffer, p27(BBP)/eIF6 forms polymers which, strikingly, have a morphology identical to NM filaments. Cross-linking experiments suggested that polymerization is favored by the formation of disulphide bridges. These data suggest that p27(BBP)/eIF6 is associated with the cytoskeleton, and contributes to formation of NM filaments. These findings help to settle the controversy on nuclear matrix. |
