Structural basis for disassembly of katanin heterododecamers.

The Journal of Biological Chemistry
Stanley NithiananthamJawdat Al-Bassam

Abstract

The reorganization of microtubules in mitosis, meiosis, and development requires the microtubule-severing activity of katanin. Katanin is a heterodimer composed of an ATPase associated with diverse cellular activities (AAA) subunit and a regulatory subunit. Microtubule severing requires ATP hydrolysis by katanin's conserved AAA ATPase domains. Whereas other AAA ATPases form stable hexamers, we show that katanin forms only a monomer or dimers of heterodimers in solution. Katanin oligomers consistent with hexamers of heterodimers or heterododecamers were only observed for an ATP hydrolysis-deficient mutant in the presence of ATP. X-ray structures of katanin's AAA ATPase in monomeric nucleotide-free and pseudo-oligomeric ADP-bound states revealed conformational changes in the AAA subdomains that explained the structural basis for the instability of the katanin heterododecamer. We propose that the rapid dissociation of katanin AAA oligomers may lead to an autoinhibited state that prevents inappropriate microtubule severing or that cyclical disassembly into heterodimers may critically contribute to the microtubule-severing mechanism.

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Citations

Oct 31, 2018·The Journal of Cell Biology·Francis J McNally, Antonina Roll-Mecak
Apr 25, 2019·Molecular Biology of the Cell·Graham M Burkart, Ram Dixit
Mar 15, 2020·Cytoskeleton·Rohith A VarikotiRuxandra I Dima
Nov 19, 2019·Developmental Cell·Elena A ZehrAntonina Roll-Mecak
Nov 14, 2020·Trends in Cell Biology·Yin-Wei Kuo, Jonathon Howard
Aug 21, 2021·Frontiers in Cell and Developmental Biology·Nicole A LynnJorge Z Torres

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