Results 21 to 30 of about 1,269 (164)

Lamin A and the LINC complex act as potential tumor suppressors in Ewing Sarcoma

Cell Death and Disease, 2022
Lamin A, a main constituent of the nuclear lamina, is involved in mechanosignaling and cell migration through dynamic interactions with the LINC complex, formed by the nuclear envelope proteins SUN1, SUN2 and the nesprins.
Francesca Chiarini, Francesca Paganelli, Tommaso Balestra, Cristina Capanni, Antonietta Fazio, Maria Cristina Manara, Lorena Landuzzi, Stefania Petrini, Camilla Evangelisti, Pier-Luigi Lollini, Alberto M. Martelli, Giovanna Lattanzi, Katia Scotlandi   +12 more
doaj   +1 more source

Nesprin-1: novel regulator of striated muscle nuclear positioning and mechanotransduction. [PDF]

Biochem Soc Trans, 2023
Nesprins (nuclear envelope spectrin repeat proteins) are multi-isomeric scaffolding proteins. Giant nesprin-1 and -2 localise to the outer nuclear membrane, interact with SUN (Sad1p/UNC-84) domain-containing proteins at the inner nuclear membrane to form the LInker of Nucleoskeleton and Cytoskeleton (LINC) complex, which, in association with lamin A/C ...
De Silva S, Fan Z, Kang B, Shanahan CM, Zhang Q.   +4 more
europepmc   +3 more sources

Nesprin-2G tension fine-tunes Wnt/β-catenin signaling [PDF]

Journal of Cell Biology, 2020
How LINC complexes mediate nuclear mechanotransduction remains unclear. In this issue, Déjardin, Carollo, et al. (2020. J. Cell Biol.https://doi.org/10.1083/jcb.201908036) show that the LINC complex protein nesprin-2G is a mechanosensor of epithelial–mesenchymal transitions (EMTs), recruiting α-catenin to the nucleus to attenuate Wnt/β-catenin ...
Cara J. Gottardi, G.W. Gant Luxton
openaire   +4 more sources

Mechanical Responses of the Giant Nesprin-2 [PDF]

AbstractThe nesprin protein family serves as a critical physical bridge between the cytoskeleton–a fundamental structural scaffold and mechanotransduction hub of the cell, and the nucleus–an intriguing and emerging mechano-responsive element. Due to the external mechanical cues and the nucleo-cytoskeletal dynamics, the nesprins are physiologically ...
Fei Shang, Y. N. Zhang, Jiaqing Ye, Zhuwei Zhang, Xingyu Qi, Long‐Qing Chen, Miao Yu, Shimin Le   +7 more
openalex   +2 more sources

Large-scale modelling of the divergent spectrin repeats in nesprins: giant modular proteins.

PLoS ONE, 2013
Nesprin-1 and nesprin-2 are nuclear envelope (NE) proteins characterized by a common structure of an SR (spectrin repeat) rod domain and a C-terminal transmembrane KASH [Klarsicht-ANC-Syne-homology] domain and display N-terminal actin-binding CH ...
Flavia Autore, Mark Pfuhl, Xueping Quan, Aisling Williams, Roland G Roberts, Catherine M Shanahan, Franca Fraternali   +6 more
doaj   +1 more source

Identification and Validation of Putative Nesprin Variants [PDF]

, 2016
Nesprins are a family of multi-isomeric scaffolding proteins that were originally identified at the nuclear envelope (NE), where they bind to lamin A/C, emerin, and SUN-domain containing proteins, to form the LInker of Nucleoskeleton-and-Cytoskeleton (LINC) complex that connects the NE to the actin cytoskeleton. However, nesprin genes also give rise to
Autore, Flavia, Shanahan, Catherine Mary, Zhang, Qiuping   +2 more
openaire   +4 more sources

Nesprin-1 mutations in human and murine cardiomyopathy [PDF]

Journal of Molecular and Cellular Cardiology, 2010
Mutations in LMNA, the gene encoding the nuclear membrane proteins, lamins A and C, produce cardiac and muscle disease. In the heart, these autosomal dominant LMNA mutations lead to cardiomyopathy frequently associated with cardiac conduction system disease. Herein, we describe a patient with the R374H missense variant in nesprin-1alpha, a protein that
Megan J, Puckelwartz, Eric J, Kessler, Gene, Kim, Megan M, Dewitt, Yuan, Zhang, Judy U, Earley, Frederic F S, Depreux, James, Holaska, Stephanie K, Mewborn, Peter, Pytel, Elizabeth M, McNally   +10 more
openaire   +2 more sources

Nuclear envelopathies: a complex LINC between nuclear envelope and pathology

Orphanet Journal of Rare Diseases, 2017
Since the identification of the first disease causing mutation in the gene coding for emerin, a transmembrane protein of the inner nuclear membrane, hundreds of mutations and variants have been found in genes encoding for nuclear envelope components ...
Alexandre Janin, Delphine Bauer, Francesca Ratti, Gilles Millat, Alexandre Méjat   +4 more
doaj   +1 more source

Laminar Flow Protects Vascular Endothelial Tight Junctions and Barrier Function via Maintaining the Expression of Long Non-coding RNA MALAT1

Frontiers in Bioengineering and Biotechnology, 2020
Atherosclerotic plaque preferentially develops in arterial curvatures and branching regions, where endothelial cells constantly experience disturbed blood flow.
Fangfang Yang, Fangfang Yang, Fangfang Yang, Yunpeng Zhang, Yunpeng Zhang, Yunpeng Zhang, Juanjuan Zhu, Juanjuan Zhu, Juanjuan Zhu, Jin Wang, Jin Wang, Jin Wang, Zhitong Jiang, Zhitong Jiang, Zhitong Jiang, Chuanrong Zhao, Chuanrong Zhao, Chuanrong Zhao, Qianru Yang, Qianru Yang, Qianru Yang, Yu Huang, Weijuan Yao, Weijuan Yao, Weijuan Yao, Wei Pang, Wei Pang, Wei Pang, Lili Han, Lili Han, Lili Han, Jing Zhou, Jing Zhou, Jing Zhou   +33 more
doaj   +1 more source

Nesprin 1 is critical for nuclear positioning and anchorage [PDF]

Human Molecular Genetics, 2009
Nesprin 1 is an outer nuclear membrane protein that is thought to link the nucleus to the actin cytoskeleton. Recent data suggest that mutations in Nesprin 1 may also be involved in the pathogenesis of Emery-Dreifuss muscular dystrophy. To investigate the function of Nesprin 1 in vivo, we generated a mouse model in which all isoforms of Nesprin 1 ...
Zhang, Jianlin, Felder, Amanda, Liu, Yujie, Guo, Ling T., Lange, Stephan, Dalton, Nancy D., Gu, Yusu, Peterson, Kirk L., Mizisin, Andrew P., Shelton, G. Diane, Lieber, Richard L., Chen, Ju   +11 more
openaire   +2 more sources