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A SUMOylation Motif in Aurora-A: Implications for Spindle Dynamics and Oncogenesis.

Abstract : Aurora-A is a serine/threonine kinase that plays critical roles in centrosome maturation, spindle dynamics, and chromosome orientation and it is frequently over-expressed in human cancers. In this work, we show that Aurora-A interacts with the SUMO-conjugating enzyme UBC9 and co-localizes with SUMO1 in mitotic cells. Aurora-A can be SUMOylated in vitro and in vivo. Mutation of the highly conserved SUMOylation residue lysine 249 significantly disrupts Aurora-A SUMOylation and mitotic defects characterized by defective and multipolar spindles ensue. The Aurora-A(K249R) mutant has normal kinase activity but displays altered dynamics at the mitotic spindle. In addition, ectopic expression of the Aurora-A(K249R) mutant results in a significant increase in susceptibility to malignant transformation induced by the Ras oncogene. These data suggest that modification by SUMO residues may control Aurora-A function at the spindle and that deficiency of SUMOylation of this kinase may have important implications for tumor development.
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Contributor : Laurent Jonchère <>
Submitted on : Tuesday, February 17, 2015 - 11:39:37 AM
Last modification on : Thursday, January 14, 2021 - 11:19:58 AM

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Ignacio Pérez de Castro, Cristina Aguirre-Portolés, Benedicte Martin, Gonzalo Fernández-Miranda, Andrea Klotzbucher, et al.. A SUMOylation Motif in Aurora-A: Implications for Spindle Dynamics and Oncogenesis.. Frontiers in Oncology, Frontiers, 2010, 1, pp.50. ⟨10.3389/fonc.2011.00050⟩. ⟨hal-01117519⟩



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