IBYME   02675
INSTITUTO DE BIOLOGIA Y MEDICINA EXPERIMENTAL
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
LIMK1/2 PARTICIPATES IN THE MECHANISMS ASSOCIATED TO SPERM MOTILITY BY AN INDEPENDENT ACTIN POLIMERIZATION PATHWAY
Autor/es:
ROMAROWSKI A ; LA SPINA F; BATTISTONE MA; CUASNICU PS; BUFFONE M
Lugar:
Chascomus
Reunión:
Jornada; 15ta Jornadas Multidisciplinarias de la Sociedad Argentina de Biología; 2013
Resumen:
LIMK plays a central role in the signaling pathway of the small GTPases Rho, Rac and cdc42. Its activation has been associated with different cellular events and mediated by the dynamic of the actin cytoskeleton through phosphorylation of cofilin. In this work, we investigated the role of LIMK in mouse sperm. By western-blot we detected that LIMK is phosphorylated (LIMK-P) in Thr508 during capacitation. This phosphorylation is downstream of PKA and would be independent of the Rho and Rac signaling pathway. By immunofluorescence, we observed that LIMK-P is localized mainly in the sperm flagella and is associated with the Triton X-100 insoluble fraction. Inhibition with specific inhibitor of LIMK-P (BMS-3) results in a dose-dependent manner decrease in progressive motility. The inhibition of LIMK-P does not decrease actin polymerization, suggesting that its mechanism of action is independent of the dynamics of the cytoskeleton in opposition of what is observed in other cell systems. In conclusion, LIMK phosphorylation downstream the activation of PKA is important for mouse sperm motility.