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Microtubule severing by the katanin complex is activated by PPFR-1-dependent MEI-1 dephosphorylation

José-Eduardo Gomes1, Nicolas Tavernier, Bénédicte Richaudeau

  • 1Institut Jacques Monod, Centre National de la Recherche Scientifique, UMR 7592, University of Paris Diderot, F-75205 Paris, France.

The Journal of Cell Biology
|August 7, 2013
PubMed

Insights

The protein PPFR-1 activates katanin during meiosis in C. elegans. Its degradation, along with MEI-1, by the CRL3(MEL-26) ligase ensures timely inactivation of katanin for mitosis.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Developmental Biology

Background:

  • Katanin is a conserved microtubule-severing complex crucial for microtubule dynamics.
  • In C. elegans, the katanin homolog MEI-1 is essential for meiosis but must be inactivated for mitosis.

Purpose of the Study:

  • To investigate the role of PPFR-1 in regulating katanin activity during C. elegans meiosis.
  • To elucidate the mechanisms controlling katanin inactivation after meiosis.

Main Methods:

  • Investigated PPFR-1 function in C. elegans meiosis.
  • Analyzed MEI-1 and PPFR-1 protein levels and interactions.
  • Utilized genetic analysis of loss-of-function mutants for ppfr-1 and mel-26.

Main Results:

  • PPFR-1 enhances katanin's microtubule-severing activity during meiosis.
  • Loss of ppfr-1 causes defects in meiosis II spindle disassembly.
  • PPFR-1 and MEI-1 are degraded by the CRL3(MEL-26) E3 ligase complex after meiosis.
  • PPFR-1 interacts with MEL-26, targeting both itself and MEI-1 for degradation.

Conclusions:

  • PPFR-1 acts as a meiotic activator for katanin.
  • CRL3(MEL-26)-mediated degradation of MEI-1 and PPFR-1 ensures katanin inactivation for mitotic transition.
  • Temporal regulation of katanin activity involves reversible phosphorylation and targeted protein degradation.

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