Microtubule severing by the katanin complex is activated by PPFR-1-dependent MEI-1 dephosphorylation. - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Journal of Cell Biology Année : 2013

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

Résumé

Katanin is an evolutionarily conserved microtubule (MT)-severing complex implicated in multiple aspects of MT dynamics. In Caenorhabditis elegans, the katanin homologue MEI-1 is required for meiosis, but must be inactivated before mitosis. Here we show that PPFR-1, a regulatory subunit of a trimeric protein phosphatase 4 complex, enhanced katanin MT-severing activity during C. elegans meiosis. Loss of ppfr-1, similarly to the inactivation of MT severing, caused a specific defect in meiosis II spindle disassembly. We show that a fraction of PPFR-1 was degraded after meiosis, contributing to katanin inactivation. PPFR-1 interacted with MEL-26, the substrate recognition subunit of the CUL-3 RING E3 ligase (CRL3(MEL-26)), which also targeted MEI-1 for post-meiotic degradation. Reversible protein phosphorylation of MEI-1 may ensure temporal activation of the katanin complex during meiosis, whereas CRL3(MEL-26)-mediated degradation of both MEI-1 and its activator PPFR-1 ensure efficient katanin inactivation in the transition to mitosis.

Dates et versions

hal-00880219 , version 1 (05-11-2013)

Identifiants

Citer

José-Eduardo Gomes, Nicolas Tavernier, Bénédicte Richaudeau, Etienne Formstecher, Thomas Boulin, et al.. Microtubule severing by the katanin complex is activated by PPFR-1-dependent MEI-1 dephosphorylation.. Journal of Cell Biology, 2013, 202 (3), pp.431-9. ⟨10.1083/jcb.201304174⟩. ⟨hal-00880219⟩
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