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

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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 approximate to 10-30 pN forces to these nesprin linkages yielded structural transitions, with a base transition size of 5-6nm, 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.
Publisher
TAYLOR & FRANCIS INC
Issue Date
2017-06
Language
English
Article Type
Article
Keywords

ENDOTHELIAL-CELLS; SIGNAL-TRANSDUCTION; ACTIN CYTOSKELETON; MEMBRANE PROTEIN; SPECTRIN DOMAINS; IN-VITRO; FORCE; MECHANOTRANSDUCTION; CHROMATIN; ENVELOPE

Citation

NUCLEUS, v.8, no.5, pp.534 - 547

ISSN
1949-1034
DOI
10.1080/19491034.2017.1322237
URI
http://hdl.handle.net/10203/238846
Appears in Collection
ME-Journal Papers(저널논문)
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