Abstract
Microtubule length regulation is required for proper spindle length and positioning, cilia formation, and axonal outgrowth. For correct microtubule organization to occur, microtubule associated proteins (MAPs) bind to microtubules and control the dynamics. Despite much work on stabilizing MAPs affecting microtubule dynamics, few studies have investigate the role of destabilizing MAPs on microtubules. Katanin, a known destabilizing MAP and the first-discovered microtubule severing enzyme, is a AAA+ enzyme that oligomerizes into hexamers and uses ATP hydrolysis to sever microtubules. We seek to measure the effects of katanin severing on microtubule dynamic instability in vitro, away from compounding cellular factors. We will use Total Internal Reflection Fluorescence (TIRF) microscopy on fluorescent microtubules and purified MBP-katanin to reveal that katanin is unable to sever dynamic microtubules, and instead modulates microtubules by changing the rates of growth and depolymerization. Our experiments also indicate that katanin does not modify the catastrophe rate of microtubules. Further work is required to disclose how katanin may work with stabilizing MAPs to control microtubule length.
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