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PLoS One. 2015 Apr 17;10(4):e0123912. doi: 10.1371/journal.pone.0123912. eCollection 2015.

The non-catalytic domains of Drosophila katanin regulate its abundance and microtubule-disassembly activity.

Author information

1
Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
2
Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America; Carolina Center for Genome Sciences, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America; Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.

Abstract

Microtubule severing is a biochemical reaction that generates an internal break in a microtubule and regulation of microtubule severing is critical for cellular processes such as ciliogenesis, morphogenesis, and meiosis and mitosis. Katanin is a conserved heterodimeric ATPase that severs and disassembles microtubules, but the molecular determinants for regulation of microtubule severing by katanin remain poorly defined. Here we show that the non-catalytic domains of Drosophila katanin regulate its abundance and activity in living cells. Our data indicate that the microtubule-interacting and trafficking (MIT) domain and adjacent linker region of the Drosophila katanin catalytic subunit Kat60 cooperate to regulate microtubule severing in two distinct ways. First, the MIT domain and linker region of Kat60 decrease its abundance by enhancing its proteasome-dependent degradation. The Drosophila katanin regulatory subunit Kat80, which is required to stabilize Kat60 in cells, conversely reduces the proteasome-dependent degradation of Kat60. Second, the MIT domain and linker region of Kat60 augment its microtubule-disassembly activity by enhancing its association with microtubules. On the basis of our data, we propose that the non-catalytic domains of Drosophila katanin serve as the principal sites of integration of regulatory inputs, thereby controlling its ability to sever and disassemble microtubules.

PMID:
25886649
PMCID:
PMC4401518
DOI:
10.1371/journal.pone.0123912
[Indexed for MEDLINE]
Free PMC Article

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