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Differential basal-to-apical accessibility of lamin A/C epitopes in the nuclear lamina regulated by changes in cytoskeletal tension

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Differential basal-to-apical accessibility of lamin A/C epitopes in the nuclear lamina regulated by changes in cytoskeletal tension. / Ihalainen, Teemu O.; Aires, Lina; Herzog, Florian A.; Schwartlander, Ruth; Moeller, Jens; Vogel, Viola.

In: Nature Materials, Vol. 14, No. 12, 01.12.2015, p. 1252-1261.

Research output: Contribution to journalArticleScientificpeer-review

Harvard

Ihalainen, TO, Aires, L, Herzog, FA, Schwartlander, R, Moeller, J & Vogel, V 2015, 'Differential basal-to-apical accessibility of lamin A/C epitopes in the nuclear lamina regulated by changes in cytoskeletal tension', Nature Materials, vol. 14, no. 12, pp. 1252-1261. https://doi.org/10.1038/nmat4389

APA

Ihalainen, T. O., Aires, L., Herzog, F. A., Schwartlander, R., Moeller, J., & Vogel, V. (2015). Differential basal-to-apical accessibility of lamin A/C epitopes in the nuclear lamina regulated by changes in cytoskeletal tension. Nature Materials, 14(12), 1252-1261. https://doi.org/10.1038/nmat4389

Vancouver

Ihalainen TO, Aires L, Herzog FA, Schwartlander R, Moeller J, Vogel V. Differential basal-to-apical accessibility of lamin A/C epitopes in the nuclear lamina regulated by changes in cytoskeletal tension. Nature Materials. 2015 Dec 1;14(12):1252-1261. https://doi.org/10.1038/nmat4389

Author

Ihalainen, Teemu O. ; Aires, Lina ; Herzog, Florian A. ; Schwartlander, Ruth ; Moeller, Jens ; Vogel, Viola. / Differential basal-to-apical accessibility of lamin A/C epitopes in the nuclear lamina regulated by changes in cytoskeletal tension. In: Nature Materials. 2015 ; Vol. 14, No. 12. pp. 1252-1261.

Bibtex - Download

@article{5dfa8a925a994d06951139c91955c523,
title = "Differential basal-to-apical accessibility of lamin A/C epitopes in the nuclear lamina regulated by changes in cytoskeletal tension",
abstract = "Nuclear lamins play central roles at the intersection between cytoplasmic signalling and nuclear events. Here, we show that at least two N- and C-terminal lamin epitopes are not accessible at the basal side of the nuclear envelope under environmental conditions known to upregulate cell contractility. The conformational epitope on the Ig-domain of A-type lamins is more buried in the basal than apical nuclear envelope of human mesenchymal stem cells undergoing osteogenesis (but not adipogenesis), and in fibroblasts adhering to rigid (but not soft) polyacrylamide hydrogels. This structural polarization of the lamina is promoted by compressive forces, emerges during cell spreading, and requires lamin A/C multimerization, intact nucleoskeleton-cytoskeleton linkages (LINC), and apical-actin stress-fibre assembly. Notably, the identified Ig-epitope overlaps with emerin, DNA and histone binding sites, and comprises various laminopathy mutation sites. Our findings should help decipher how the physical properties of cellular microenvironments regulate nuclear events.",
author = "Ihalainen, {Teemu O.} and Lina Aires and Herzog, {Florian A.} and Ruth Schwartlander and Jens Moeller and Viola Vogel",
year = "2015",
month = "12",
day = "1",
doi = "10.1038/nmat4389",
language = "English",
volume = "14",
pages = "1252--1261",
journal = "Nature Materials",
issn = "1476-1122",
publisher = "Nature Publishing Group",
number = "12",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Differential basal-to-apical accessibility of lamin A/C epitopes in the nuclear lamina regulated by changes in cytoskeletal tension

AU - Ihalainen, Teemu O.

AU - Aires, Lina

AU - Herzog, Florian A.

AU - Schwartlander, Ruth

AU - Moeller, Jens

AU - Vogel, Viola

PY - 2015/12/1

Y1 - 2015/12/1

N2 - Nuclear lamins play central roles at the intersection between cytoplasmic signalling and nuclear events. Here, we show that at least two N- and C-terminal lamin epitopes are not accessible at the basal side of the nuclear envelope under environmental conditions known to upregulate cell contractility. The conformational epitope on the Ig-domain of A-type lamins is more buried in the basal than apical nuclear envelope of human mesenchymal stem cells undergoing osteogenesis (but not adipogenesis), and in fibroblasts adhering to rigid (but not soft) polyacrylamide hydrogels. This structural polarization of the lamina is promoted by compressive forces, emerges during cell spreading, and requires lamin A/C multimerization, intact nucleoskeleton-cytoskeleton linkages (LINC), and apical-actin stress-fibre assembly. Notably, the identified Ig-epitope overlaps with emerin, DNA and histone binding sites, and comprises various laminopathy mutation sites. Our findings should help decipher how the physical properties of cellular microenvironments regulate nuclear events.

AB - Nuclear lamins play central roles at the intersection between cytoplasmic signalling and nuclear events. Here, we show that at least two N- and C-terminal lamin epitopes are not accessible at the basal side of the nuclear envelope under environmental conditions known to upregulate cell contractility. The conformational epitope on the Ig-domain of A-type lamins is more buried in the basal than apical nuclear envelope of human mesenchymal stem cells undergoing osteogenesis (but not adipogenesis), and in fibroblasts adhering to rigid (but not soft) polyacrylamide hydrogels. This structural polarization of the lamina is promoted by compressive forces, emerges during cell spreading, and requires lamin A/C multimerization, intact nucleoskeleton-cytoskeleton linkages (LINC), and apical-actin stress-fibre assembly. Notably, the identified Ig-epitope overlaps with emerin, DNA and histone binding sites, and comprises various laminopathy mutation sites. Our findings should help decipher how the physical properties of cellular microenvironments regulate nuclear events.

UR - http://www.scopus.com/inward/record.url?scp=84947870719&partnerID=8YFLogxK

U2 - 10.1038/nmat4389

DO - 10.1038/nmat4389

M3 - Article

VL - 14

SP - 1252

EP - 1261

JO - Nature Materials

JF - Nature Materials

SN - 1476-1122

IS - 12

ER -