Open AccessAtomic force microscopy reveals distinct protofilament-scale structural dynamics in depolymerizing microtubule arrays
Author(s) -
Sithara S. Wijeratne,
Michelle F. Marchan,
Jason S. Tresback,
Radhika Subramanian
Publication year - 2022
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2115708119
Subject(s) - microtubule , kinesin , cytoskeleton , dynein , tubulin , biophysics , motor protein , biology , microtubule associated protein , microbiology and biotechnology , biochemistry , cell
Significance One cannot help but marvel at the precise organization of microtubule polymers in cellular structures such as the axoneme and the spindle. However, our understanding of the biochemical mechanisms that sculpt these arrays comes largely from in vitro experiments with a small number (one or two) of microtubules. This is somewhat akin to studying the architecture of multilane highways by studying one-lane streets. Here, we directly visualize depolymerizing microtubule arrays at individual microtubule and protofilament resolution using atomic force microscopy. Our results reveal differences in microtubule depolymerase activity and provide insights into how these differences in enzymatic activity on the nanometer scale can result in the differential remodeling of multimicrotubule arrays on the micron-length scale.