| First Author | Saito Y | Year | 2011 |
| Journal | Biochem Biophys Res Commun | Volume | 408 |
| Issue | 2 | Pages | 329-33 |
| PubMed ID | 21513700 | Mgi Jnum | J:177229 |
| Mgi Id | MGI:5294516 | Doi | 10.1016/j.bbrc.2011.04.033 |
| Citation | Saito Y, et al. (2011) PICOT is a molecule which binds to anamorsin. Biochem Biophys Res Commun 408(2):329-33 |
| abstractText | Anamorsin (AM) (also called CIAPIN-1) is a cell-death-defying factor. AM deficient mice die during late gestation; AM deficient embryos are anemic and very small compared to wild type (WT) embryos. It is thought that AM plays crucial roles in hematopoiesis and embryogenesis. To clarify the mechanisms of AM functions, we performed the yeast-two-hybrid assay to identify AM-interacting molecules; we found that PICOT (PKCtheta interacting cousin of thioredoxin) preferentially bound to AM. We also showed that the N-terminal regions of both AM and PICOT were essential for their bindings and the inhibition of interaction of both molecules might lead to the cell growth retardation. Both PICOT and the yeast homolog of AM are known to be iron-sulfur proteins. The phenotype of PICOT deficient mice is very similar to that of anamorsin deficient mice; both mice are embryonic lethal. These data suggest that AM and PICOT might play cooperatively essential roles in embryogenesis as iron-sulfur cluster proteins. |
