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- W1979648895 abstract "Microtubules are polar, long, hollow, and stiff cytoskeletal polymers made of α/β tubulin heterodimers. Their dynamic properties provide the framework for central cellular processes, ranging from cell motility and intracellular transport to mitosis and meiosis. A still growing number of proteins interact with microtubules (MAPs) to tightly and finely regulate their assembly, stability, and disassembly. The microtubule-severing enzymes contribute to the dynamic reorganization of the microtubule network. Severing enzymes are members of the AAA+ (ATPases Associated with various cellular Activities) family of ATPases. The latest addition to this family is fidgetin, which is involved in mammalian development, maintenance of the centrosome, and normal astral microtubule array. Yet, we do not have quantitative biophysical data about the activity of fidgetin in vitro. Fidgetin at low concentration acts as a depolymerizing factor removing tubulin dimers preferentially from the minus end of the microtubules. At high concentration fidgetin cuts all along the lattice of taxol-microtubules. We also found that fidgetin preferentially depolymerizes and severs GMPCPP microtubules over Taxol-stabilized microtubules. Our results indicate that fidgetin is a microtubule-severing enzyme with new and specific biophysical abilities, with the ability to detect fine changes on the MT lattice." @default.
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- W1979648895 date "2013-01-01" @default.
- W1979648895 modified "2023-09-28" @default.
- W1979648895 title "Biophysical Studies and Atomic Force Microscopy Bring to Light Particular Activities of the Microtubule Severing ATPase Enzyme Fidgetin" @default.
- W1979648895 doi "https://doi.org/10.1016/j.bpj.2012.11.817" @default.
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