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The nesprin-cytoskeleton interface probed directly on single nuclei is a mechanically rich system

Authors
 Daniel A. Balikov  ;  Sonia K. Brady  ;  Ung Hyun Ko  ;  Jennifer H. Shin  ;  Jose M. de Pereda  ;  Arnoud Sonnenberg  ;  Hak-Joon Sung  ;  Matthew J. Lang 
Citation
 NUCLEUS, Vol.8(5) : 534-547, 2017 
Journal Title
NUCLEUS
ISSN
 1949-1034 
Issue Date
2017
MeSH
Biomechanical Phenomena ; Cell Nucleus/metabolism ; Cytoskeleton/metabolism ; Humans ; Mechanical Phenomena ; Mesenchymal Stromal Cells/cytology ; Nuclear Proteins/metabolism ; Single-Cell Analysis
Keywords
biomechanics ; cytoskeleton ; nesprin ; nucleus ; single molecule
Abstract
The cytoskeleton provides structure and plays an important role in cellular function such as migration, resisting compression forces, and transport. The cytoskeleton also reacts to physical cues such as fluid shear stress or extracellular matrix remodeling by reorganizing filament associations, most commonly focal adhesions and cell-cell cadherin junctions. These mechanical stimuli can result in genome-level changes, and the physical connection of the cytoskeleton to the nucleus provides an optimal conduit for signal transduction by interfacing with nuclear envelope proteins, called nesprins, within the LINC (linker of the nucleus to the cytoskeleton) complex. Using single-molecule on single nuclei assays, we report that the interactions between the nucleus and the cytoskeleton, thought to be nesprin-cytoskeleton interactions, are highly sensitive to force magnitude and direction depending on whether cells are historically interfaced with the matrix or with cell aggregates. Application of ∼10-30 pN forces to these nesprin linkages yielded structural transitions, with a base transition size of 5-6 nm, which are speculated to be associated with partial unfoldings of the spectrin domains of the nesprins and/or structural changes of histones within the nucleus.
DOI
10.1080/19491034.2017.1322237
Appears in Collections:
1. College of Medicine (의과대학) > BioMedical Science Institute (의생명과학부) > 1. Journal Papers
Yonsei Authors
Sung, Hak-Joon(성학준) ORCID logo https://orcid.org/0000-0003-2312-2484
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/161404
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