| First Author | Nakajima O | Year | 2006 |
| Journal | Biochem Biophys Res Commun | Volume | 346 |
| Issue | 1 | Pages | 140-9 |
| PubMed ID | 16756961 | Mgi Jnum | J:110447 |
| Mgi Id | MGI:3640241 | Doi | 10.1016/j.bbrc.2006.05.113 |
| Citation | Nakajima O, et al. (2006) FKBP133: a novel mouse FK506-binding protein homolog alters growth cone morphology. Biochem Biophys Res Commun 346(1):140-9 |
| abstractText | FK506-binding proteins are the peptidyl prolyl cis-trans isomerases that are involved in various intracellular events. We characterized a novel mouse FK506-binding protein homolog, FKBP133/KIAA0674, in the developing nervous system. FKBP133 contains a domain similar to Wiskott-Aldrich syndrome protein homology region 1 (WH1) and a domain homologous to FK506-binding protein motif. FKBP133 was predominantly expressed in cerebral cortex, hippocampus, and peripheral ganglia at embryonic day 18.5. FKBP133 protein was distributed in the axonal shafts and was partially co-localized with F-actin in the growth cones of dorsal root ganglion neurons (DRG). The number of filopodia was increased in the DRG neurons overexpressing FKBP133. In contrast, the overexpression of a mutant deleted the WH1 domain reduced the growth cone size and the number of filopodia. Furthermore, the neurons overexpressing FKBP133 became significantly resistant to Semaphorin-3A induced collapse response. These results suggest that FKBP133 modulates growth cone behavior with the WH1 domain. |
