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Invited review: Microtubule severing enzymes couple atpase activity with tubulin GTPase spring loading
Author(s) -
Bailey Megan E.,
Jiang Nan,
Dima Ruxandra I.,
Ross Jennifer L.
Publication year - 2016
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22842
Subject(s) - microtubule , gtpase , tubulin , atpase , chemistry , enzyme , microbiology and biotechnology , gtp' , biophysics , dynamics (music) , biochemistry , biology , physics , acoustics
Microtubules are amazing filaments made of GTPase enzymes that store energy used for their own self‐destruction to cause a stochastically driven dynamics called dynamic instability. Dynamic instability can be reproduced in vitro with purified tubulin, but the dynamics do not mimic that observed in cells. This is because stabilizers and destabilizers act to alter microtubule dynamics. One interesting and understudied class of destabilizers consists of the microtubule‐severing enzymes from the ATPases Associated with various cellular Activities (AAA+) family of ATP‐enzymes. Here we review current knowledge about GTP‐driven microtubule dynamics and how that couples to ATP‐driven destabilization by severing enzymes. We present a list of challenges regarding the mechanism of severing, which require development of experimental and modeling approaches to shed light as to how severing enzymes can act to regulate microtubule dynamics in cells. © 2016 Wiley Periodicals, Inc. Biopolymers 105: 547–556, 2016.