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 PMID:38329452  

Microtubule-binding domains in Katanin p80 subunit are essential for severing activity in C. elegans.

Eva Beaumale | Lucie Van Hove | Lionel Pintard | Nicolas Joly
The Journal of cell biology | 2024

Microtubule-severing enzymes (MSEs), such as Katanin, Spastin, and Fidgetin play essential roles in cell division and neurogenesis. They damage the microtubule (MT) lattice, which can either destroy or amplify the MT cytoskeleton, depending on the cellular context. However, little is known about how they interact with their substrates. We have identified the microtubule-binding domains (MTBD) required for Katanin function in C. elegans. Katanin is a heterohexamer of dimers containing a catalytic subunit p60 and a regulatory subunit p80, both of which are essential for female meiotic spindle assembly. Here, we report that p80-like(MEI-2) dictates Katanin binding to MTs via two MTBDs composed of basic patches. Substituting these patches reduces Katanin binding to MTs, compromising its function in female meiotic-spindle assembly. Structural alignments of p80-like(MEI-2) with p80s from different species revealed that the MTBDs are evolutionarily conserved, even if the specific amino acids involved vary. Our findings highlight the critical importance of the regulatory subunit (p80) in providing MT binding to the Katanin complex.

Pubmed ID: 38329452

Antibodies used in this publication

None found

Associated grants

  • Agency: NIH HHS, United States
    Id: P40 OD010440
  • Agency: ODCDC CDC HHS, United States
    Id: P40 OD010440

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MetaMorph Microscopy Automation and Image Analysis Software (tool)

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RRID:SCR_005375

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RRID:SCR_014212

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RRID:SCR_007341

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