Structural basis for disassembly of katanin heterododecamers

The reorganization of microtubules in mitosis, meiosis, and development requires the microtubule-severing activity of katanin. Katanin is a heterodimer composed of an TPase ssociated with diverse cellular ctivities (AAA) subunit and a regulatory subunit. Microtubule severing requires ATP hydrolysis...

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Vydané v:The Journal of biological chemistry Ročník 293; číslo 27; s. 10590
Hlavní autori: Nithianantham, Stanley, McNally, Francis J, Al-Bassam, Jawdat
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: United States 06.07.2018
Predmet:
Adenosine Triphosphatases - chemistry
Adenosine Triphosphatases - metabolism
Animals
Caenorhabditis elegans - enzymology
Caenorhabditis elegans Proteins - chemistry
Caenorhabditis elegans Proteins - metabolism
Crystallography, X-Ray
Humans
Katanin - chemistry
Katanin - metabolism
Meiosis
Microtubules
Protein Conformation
Protein Multimerization
Spindle Apparatus
X-ray crystallography
microtubule
microtubule-associated protein (MAP)
tubulin
meiosis
mitosis
ISSN:1083-351X, 1083-351X
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Shrnutí:The reorganization of microtubules in mitosis, meiosis, and development requires the microtubule-severing activity of katanin. Katanin is a heterodimer composed of an TPase ssociated with diverse cellular ctivities (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.
Bibliografia:ObjectType-Article-1
SourceType-Scholarly Journals-1
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content type line 23
ISSN:1083-351X
1083-351X
DOI:10.1074/jbc.RA117.001215