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The RSA complex targets Protein Phosphatase 2A to centrosomes and regulates mitotic spindle assembly in C. elegans

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Schlaitz, A.-L., Srayko, M., Dammermann, A., Quintin, S., Wielsch, N., MacLeod, I., et al. (2007). The RSA complex targets Protein Phosphatase 2A to centrosomes and regulates mitotic spindle assembly in C. elegans. Cell, 128(1), 115-127. doi:10.1016/j.cell.2006.10.050.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002C-E7B9-5
Abstract
Microtubule behavior changes during the cell cycle and during spindle assembly. However it remains unclear how these changes are regulated and coordinated. We describe a complex that targets the Protein Phosphatase 2A holoenzyme (PP2A) to centrosomes in C. elegans embryos. This complex includes RSA-1, a targeting subunit for PP2A, and RSA-2, a protein that binds and recruits RSA-1 to centrosomes. In contrast to the multiple functions of the PP2A catalytic subunit, RSA-1 and RSA-2 are specifically required for microtubule outgrowth from centrosomes and for spindle assembly. The centrosomally localized RSA-PP2A complex mediates these functions in part by regulating two critical mitotic effectors: the microtubule destabilizer KLP-7 and the C. elegans regulator of spindle assembly TPXL-1. Therefore, by recruiting the PP2A catalytic subunit to centrosomes, the RSA complex regulates a subset of PP2A functions in order to coordinate microtubule outgrowth from centrosomes and microtubule stability in the forming mitotic spindle.