Work

Plk1 and Aurora A regulate the depolymerase activity and the cellular localization of Kif2a

Year: 2009

Type: article

Abstract: The microtubule depolymerase Kif2a controls spindle assembly and dynamics and is essential for chromosome congression and segregation. Through a proteomic analysis, we identified Kif2a as a target for regulation by the Polo-like kinase Plk1. Plk1 interacts with Kif2a, but only in mitosis, in a manner dependent on its kinase activity. Plk1 phosphorylates Kif2a and enhances its depolymerase activity in vitro. Inhibition or depletion of Plk1 decreases microtubule-associated Kif2a signals and increases the spindle microtubule intensity in vivo. Interestingly, Aurora A also interacts with and phosphorylates Kif2a. Phosphorylation of Kif2a by Aurora A suppresses its depolymerase activity in vitro, and inhibition of Aurora A increases the microtubule-associated Kif2a signals and reduces the spindle microtubule intensity in vivo. Thus, Kif2a is regulated positively by Plk1 and negatively by Aurora A. We propose that this antagonistic regulation confers differential stability to microtubules in the spindle versus at the pole versus in the cytosol, and that this spatial differential stability is important for spindle assembly and function.

Source: Journal of Cell Science

DOI: 10.1242/jcs.044321

Authors: Chang-Young Jang, Judith A. Coppinger, Akiko Seki, John R. Yates, Guowei Fang

Institutions: Stanford University, Scripps Research Institute, Genentech

Language: English

Topic: Microtubule and mitosis dynamics

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Heart, Lung, and Blood Institute, National Institute of General Medical Sciences, National Center for Research Resources

Awards: Proteomic Profiling of CFTR Protein Interaction, Mechanism of the Spindle Assembly Checkpoint Control, Comprehensive Biology: Exploiting the Yeast Genome, G4499998736