| First Author | Shinmura K | Year | 2005 |
| Journal | FEBS Lett | Volume | 579 |
| Issue | 29 | Pages | 6621-34 |
| PubMed ID | 16297385 | Mgi Jnum | J:103773 |
| Mgi Id | MGI:3610707 | Doi | 10.1016/j.febslet.2005.10.057 |
| Citation | Shinmura K, et al. (2005) Characterization of centrosomal association of nucleophosmin/B23 linked to Crm1 activity. FEBS Lett 579(29):6621-34 |
| abstractText | Nucleophosmin (NPM)/B23 is a multifunctional protein, involving in a wide variety of basic cellular processes, including ribosome assembly, DNA duplication, nucleocytoplasmic trafficking, and centrosome duplication. It has previously been shown that NPM/B23 localizes to centrosomes, and dissociate from centrosomes upon phosphorylation by Cdk2/cyclin E. However, detail characterization of centrosomal association of NPM/B23 has been hampered by the lack of appropriate antibodies that efficiently detects centrosomally localized NPM/B23, as well as by apparent loss of natural behavior of NPM/B23 when tagged with fluorescent proteins. Here, by the use of newly generated anti-NPM/B23 antibody, we conducted a careful analysis of centrosomal localization of NPM/B23. We found that NPM/B23 localizes between the paired centrioles of unduplicated centrosomes, suggesting the role of NPM/B23 in the centriole pairing. Upon initiation of centrosome duplication, some NPM/B23 proteins remain at mother centrioles of the parental centriole pairs. We further found that inhibition of Crm1 nuclear export receptor results in both accumulation of cyclin E at centrosomes and efficient dissociation of NPM/B23 from centrosomes. |
