Interfering with the connection between the nucleus and the cytoskeleton affects nuclear rotation, mechanotransduction and myogenesis

Brosig, Michaela; Ferralli, Jacqueline; Gelman, Laurent; Chiquet, Matthias; Chiquet-Ehrismann, Ruth (2010). Interfering with the connection between the nucleus and the cytoskeleton affects nuclear rotation, mechanotransduction and myogenesis. International journal of biochemistry & cell biology, 42(10), pp. 1717-28. Amsterdam: Elsevier 10.1016/j.biocel.2010.07.001

Full text not available from this repository. (Request a copy)

Mechanical stress controls a broad range of cellular functions. The cytoskeleton is physically connected to the extracellular matrix via integrin receptors, and to the nuclear lamina by the LINC complex that spans both nuclear membranes. We asked here how disruption of this direct link from the cytoskeleton to nuclear chromatin affects mechanotransduction. Fibroblasts grown on flexible silicone membranes reacted to cyclic stretch by nuclear rotation. This rotation was abolished by inhibition of actomyosin contraction as well as by overexpression of dominant-negative versions of nesprin or sun proteins that form the LINC complex. In an in vitro model of muscle differentiation, cyclic strain inhibits differentiation and induces proliferation of C2C12 myoblasts. Interference with the LINC complex in these cells abrogated their stretch-induced proliferation, while stretch increased p38 MAPK and NFkappaB phosphorylation and the transcript levels of myogenic transcription factors MyoD and myogenin. We found that the physical link from the cytoskeleton to the nuclear lamina is crucial for correct mechanotransduction, and that disruption of the LINC complex perturbs the mechanical control of cell differentiation.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > School of Dental Medicine > Department of Orthodontics

UniBE Contributor:

Chiquet, Matthias

ISSN:

1357-2725

Publisher:

Elsevier

Language:

English

Submitter:

Eveline Carmen Schuler

Date Deposited:

04 Oct 2013 14:08

Last Modified:

25 Jan 2017 12:16

Publisher DOI:

10.1016/j.biocel.2010.07.001

PubMed ID:

20621196

Web of Science ID:

000282350200021

URI:

https://boris.unibe.ch/id/eprint/454 (FactScience: 199344)

Actions (login required)

Edit item Edit item
Provide Feedback