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  Three-dimensional organization of the cytoskeleton: A cryo-electron tomography perspective

Chakraborty, S., Jasnin, M., & Baumeister, W. (2020). Three-dimensional organization of the cytoskeleton: A cryo-electron tomography perspective. Protein Science, 29, 1302-1320. doi:10.1002/pro.3858.

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 Creators:
Chakraborty, Saikat1, Author              
Jasnin, Marion1, Author              
Baumeister, Wolfgang1, Author              
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Free keywords: BRANCHED ACTIN-FILAMENTS; ALPHA-BETA-TUBULIN; INTERMEDIATE-FILAMENTS; ELECTRON-MICROSCOPY; ARP2/3 COMPLEX; MOLECULAR ARCHITECTURE; LISTERIA-MONOCYTOGENES; PROTOFILAMENT NUMBERS; DYNAMIC INSTABILITY; EUKARYOTIC CELLSBiochemistry & Molecular Biology; actin filaments; cryo-electron tomography; in situ architecture; intermediate filaments; microtubules;
 Abstract: Traditionally, structures of cytoskeletal components have been studied ex situ, that is, with biochemically purified materials. There are compelling reasons to develop approaches to study them in situ in their native functional context. In recent years, cryo-electron tomography emerged as a powerful method for visualizing the molecular organization of unperturbed cellular landscapes with the potential to attain near-atomic resolution. Here, we review recent works on the cytoskeleton using cryo-electron tomography, demonstrating the power of in situ studies. We also highlight the potential of this method in addressing important questions pertinent to the field of cytoskeletal biomechanics.

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Language(s): eng - English
 Dates: 2020-032020
 Publication Status: Published in print
 Pages: 19
 Publishing info: -
 Table of Contents: Corrigendum
Volume 29, Issue 10, Protein Science, pages: 2132-2133
First Published online: September 14, 2020
 Rev. Type: -
 Identifiers: ISI: 000562383200005
DOI: 10.1002/pro.3858
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Project name : HFSP. Grant Number: RGP0035/2016
Grant ID : RGP0035
Funding program : Human Frontier Science Program
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Title: Protein Science
Source Genre: Journal
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Publ. Info: New York, N.Y. : Cambridge University Press
Pages: - Volume / Issue: 29 Sequence Number: - Start / End Page: 1302 - 1320 Identifier: ISSN: 0961-8368
CoNE: https://pure.mpg.de/cone/journals/resource/954925342760