Casado, P.; Prado, M. A; Zuazua-Villar, P.; Del Valle, Eva; Artime, N.; Cabal-Hierro, L.; Ruperez, P.; Burlingame, A. L.; Lazo, P. S. and Ramos, S.
Microtubule interfering agents and KSP inhibitors induce the phosphorylation of the nuclear protein p54(nrb), an event linked to G2/M arrest.
Journal of Proteomics, 71(6) pp. 592–600.
Full text available as:
Microtubule interfering agents (MIAs) are anti-tumor drugs that inhibit microtubule dynamics, while kinesin spindle protein (KSP) inhibitors are substances that block the formation of the bipolar spindle during mitosis. All these compounds cause G2/M arrest and cell death. Using 2D-PAGE followed by Nano-LC-ESI-Q-ToF analysis, we found that MIAs such as vincristine (Oncovin) or paclitaxel (Taxol) and KSP inhibitors such as S-tritil-l-cysteine induce the phosphorylation of the nuclear protein p54(nrb) in HeLa cells. Furthermore, we demonstrate that cisplatin (Platinol), an anti-tumor drug that does not cause M arrest, does not induce this modification. We show that the G2/M arrest induced by MIAs is required for p54(nrb) phosphorylation. Finally, we demonstrate that CDK activity is required for MIA-induced phosphorylation of p54(nrb).
|External Project Funding Details:
|Funded Project Name||Project ID||Funding Body|
|Not Set||Not Set||Fondo de Investigación de la Seguridad Social (FISS-05-PI-042664)|
|Not Set||Not Set||Ministerio de Educación y Ciencia (SAF2006-09686)|
|Not Set||Not Set||FICYT|
||Science > Life, Health and Chemical Sciences
|Interdisciplinary Research Centre:
||Biomedical Research Network (BRN)
Eva Del Valle Suarez
||21 May 2009 16:01
||10 Mar 2014 22:43
Actions (login may be required)