Enhanced HP1α homodimer interaction <i>via</i> force-induced salt bridge formation: implications for chromatin crosslinking and phase separation-Reference-Cited by-同舟云学术

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Enhanced HP1α homodimer interaction via force-induced salt bridge formation: implications for chromatin crosslinking and phase separation

Published:2024 Issue:1 Volume:1 Page:78-93
ISSN:2976-8683
Container-title:RSC Mechanochemistry
language:en
Short-container-title:RSC Mechanochem.

Author:

Tsukamoto Shingo¹^ORCID,Khavani Mohammad¹^ORCID,Domkam Nya¹^ORCID,Mofrad Mohammad R. K.¹²^ORCID

Affiliation:

1. Molecular Cell Biomechanics Laboratory, Departments of Bioengineering and Mechanical Engineering, University of California, Berkeley, CA 94720, USA

2. Molecular Biophysics and Integrative Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA

Abstract

Unlocking chromatin dyanamics: force-driven salt bridges may spearhead compaction and phase transition.

Funder

Japan Student Services Organization

National Science Foundation

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/MR/D3MR00011G

Reference55 articles.

1. Nuclear Shape, Mechanics, and Mechanotransduction

2. The nucleus feels the force, LINCed in or not!

3. Compressive forces driven by lateral actin fibers are a key to the nuclear deformation under uniaxial cell-substrate stretching

4. Mechanotransduction at a distance: mechanically coupling the extracellular matrix with the nucleus

5. Mechanical Regulation of Transcription: Recent Advances

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