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The C. elegans RSA complex localizes protein phosphatase 2A to centrosomes and regulates mitotic spindle assembly

Academic Article
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Overview

authors

  • Schlaitz, A. L.
  • Srayko, M.
  • Dammermann, A.
  • Quintin, S.
  • Wielsch, N.
  • MacLeod, I.
  • de Robillard, Q.
  • Zinke, A.
  • Yates III, John
  • Muller-Reichert, T.
  • Shevchenko, A.
  • Oegema, K.
  • Hyman, A. A.

publication date

  • January 2007

journal

  • Cell  Journal

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 Regulator of Spindle Assembly 1 (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. By regulating a subset of PP2A functions at the centrosome, the RSA complex could therefore provide a means of coordinating microtubule outgrowth from centrosomes and kinetochore microtubule stability during mitotic spindle assembly.

subject areas

  • Animals
  • Caenorhabditis elegans
  • Caenorhabditis elegans Proteins
  • Carrier Proteins
  • Catalysis
  • Centrosome
  • Dimerization
  • Embryo, Nonmammalian
  • Kinesin
  • Microtubules
  • Multiprotein Complexes
  • Phosphoprotein Phosphatases
  • Protein Binding
  • Protein Phosphatase 2
  • Protein Subunits
  • Protein Transport
  • Spindle Apparatus
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Identity

PubMed Central ID

  • PMC2987564

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/j.cell.2006.10.050

PubMed ID

  • 17218259
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Additional Document Info

start page

  • 115

end page

  • 127

volume

  • 128

issue

  • 1

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