In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen
Author(s) -
Danielle M. Paul,
Judith Mantell,
Ufuk Borucu,
Jennifer Coombs,
Katherine J. Surridge,
John M. Squire,
Paul Verkade,
Mark P. Dodding
Publication year - 2020
Publication title -
the journal of cell biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.414
H-Index - 380
eISSN - 1540-8140
pISSN - 0021-9525
DOI - 10.1083/jcb.201911154
Subject(s) - microtubule , cryo electron tomography , cytoskeleton , microbiology and biotechnology , electron tomography , actin , lumen (anatomy) , in situ , microtubule nucleation , biophysics , biology , cell , chemistry , nanotechnology , tomography , materials science , physics , biochemistry , centrosome , cell cycle , optics , scanning transmission electron microscopy , organic chemistry , transmission electron microscopy
Microtubules and filamentous (F-) actin engage in complex interactions to drive many cellular processes from subcellular organization to cell division and migration. This is thought to be largely controlled by proteins that interface between the two structurally distinct cytoskeletal components. Here, we use cryo-electron tomography to demonstrate that the microtubule lumen can be occupied by extended segments of F-actin in small molecule-induced, microtubule-based, cellular projections. We uncover an unexpected versatility in cytoskeletal form that may prompt a significant development of our current models of cellular architecture and offer a new experimental approach for the in situ study of microtubule structure and contents.
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