In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen

Author:

Paul Danielle M.1,Mantell Judith2,Borucu Ufuk3ORCID,Coombs Jennifer2,Surridge Katherine J.2,Squire John M.14ORCID,Verkade Paul2ORCID,Dodding Mark P.2ORCID

Affiliation:

1. School of Physiology, Pharmacology and Neuroscience, Faculty of Life Sciences, University of Bristol, Bristol, United Kingdom

2. School of Biochemistry, Faculty of Life Sciences, University of Bristol, Bristol, United Kingdom

3. GW4 Facility for High-Resolution Electron Cryo-Microscopy, University of Bristol, Bristol, United Kingdom

4. Department of Metabolism, Digestion and Reproduction, Imperial College, London, United Kingdom

Abstract

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.

Funder

Biotechnology and Biosciences Research Council

Lister Research Prize Fellowship

British Heart Foundation

Alan Turing Institute

Academy of Medical Sciences

Wellcome Trust

Engineering and Physical Sciences Research Council

Bristol Centre for Functional Nanomaterials

Publisher

Rockefeller University Press

Subject

Cell Biology

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