Results 11 to 20 of about 1,269 (164)

Cytoskeletal Interactions at the Nuclear Envelope Mediated by Nesprins [PDF]

International Journal of Cell Biology, 2012
Nesprin-1 is a giant tail-anchored nuclear envelope protein composed of an N-terminal F-actin binding domain, a long linker region formed by multiple spectrin repeats and a C-terminal transmembrane domain. Based on this structure, it connects the nucleus
Surayya Taranum, Ilknur Sur, Rolf Müller, Wenshu Lu, R. N. Rashmi, Martina Munck, Sascha Neumann, Iakowos Karakesisoglou, Angelika A. Noegel   +8 more
doaj   +5 more sources

Nesprin-2 Interacts with Condensin Component SMC2 [PDF]

International Journal of Cell Biology, 2017
The nuclear envelope proteins, Nesprins, have been primarily studied during interphase where they function in maintaining nuclear shape, size, and positioning. We analyze here the function of Nesprin-2 in chromatin interactions in interphase and dividing
Xin Xing, Carmen Mroß, Linlin Hao, Martina Munck, Alexandra Herzog, Clara Mohr, C. P. Unnikannan, Pranav Kelkar, Angelika A. Noegel, Ludwig Eichinger, Sascha Neumann   +10 more
doaj   +3 more sources

Nesprins: from the nuclear envelope and beyond [PDF]

Expert Reviews in Molecular Medicine, 2013
Nuclearenvelopespectrin-repeatproteins(Nesprins), are a novel family of nuclear and cytoskeletal proteins with rapidly expanding roles as intracellular scaffolds and linkers. Originally described as proteins that localise to the nuclear envelope (NE) and establish nuclear-cytoskeletal connections, nesprins have now been found to comprise a diverse ...
Dipen Rajgor, Catherine M. Shanahan
openalex   +3 more sources

Nesprin-1 role in DNA damage response [PDF]

Nucleus, 2014
Nuclear envelope (NE) proteins have fundamental roles in maintaining nuclear structure, cell signaling, chromatin organization, and gene regulation, and mutations in genes encoding NE components were identified as primary cause of a number of age associated diseases and cancer.
İlknur Sur‐Erdem, Sascha Neumann, Angelika A. Noegel   +2 more
openalex   +3 more sources

Nesprin‐1 and nesprin‐2 regulate endothelial cell shape and migration [PDF]

Cytoskeleton, 2014
Nesprins are large multi‐domain proteins that link the nuclear envelope to the cytoskeleton and nucleoskeleton. Here we show that nesprin‐1 and nesprin‐2 play important roles in regulating cell shape and migration in endothelial cells. Nesprin‐1 or nesprin‐2 depletion by RNAi increased endothelial cell spread area and the length of cellular protrusions,
Samantha J. King, Karolin Nowak, Narendra Suryavanshi, Ian Holt, Catherine M. Shanahan, Anne J. Ridley   +5 more
openalex   +4 more sources

Mechanosensing in Dendritic Cells. [PDF]

Immunol Rev
ABSTRACT Since their discovery, dendritic cells have been recognized for their unusual capacity to sense and respond to physical stimuli within their environment. However, it took nearly two decades—and the advent of mechanobiology—to elucidate the underlying mechanisms and functional implications of this mechanical hypersensitivity. In this review, we
Calmettes V, Quintanilla MA, Lacerda Mariano L, Piel M, Moreau HD, Lennon-Duménil AM.   +5 more
europepmc   +2 more sources

Drosophila Nesprin-1 Isoforms Differentially Contribute to Muscle Function [PDF]

Cells, 2021
Nesprin-1 is a large scaffold protein connecting nuclei to the actin cytoskeleton via its KASH and Calponin Homology domains, respectively. Nesprin-1 disconnection from nuclei results in altered muscle function and myonuclei mispositioning. Furthermore, Nesprin-1 mutations are associated with muscular pathologies such as Emery Dreifuss muscular ...
Alexandre N. Rey, Laurent Schaeffer, Bénédicte Durand, Véronique Morel   +3 more
openalex   +6 more sources

Nesprin interchain associations control nuclear size [PDF]

Cellular and Molecular Life Sciences, 2012
Nesprins-1/-2/-3/-4 are nuclear envelope proteins, which connect nuclei to the cytoskeleton. The largest nesprin-1/-2 isoforms (termed giant) tether F-actin through their N-terminal actin binding domain (ABD). Nesprin-3, however, lacks an ABD and associates instead to plectin, which binds intermediate filaments.
Wenshu, Lu, Maria, Schneider, Sascha, Neumann, Verena-Maren, Jaeger, Surayya, Taranum, Martina, Munck, Sarah, Cartwright, Christine, Richardson, James, Carthew, Kowoon, Noh, Martin, Goldberg, Angelika A, Noegel, Iakowos, Karakesisoglou   +12 more
openaire   +2 more sources

Mouse models of nesprin-related diseases [PDF]

Biochemical Society Transactions, 2018
Nesprins (nuclear envelope spectrin repeat proteins) are a family of multi-isomeric scaffolding proteins. Nesprins form the LInker of Nucleoskeleton-and-Cytoskeleton (LINC) complex with SUN (Sad1p/UNC84) domain-containing proteins at the nuclear envelope, in association with lamin A/C and emerin, linking the nucleoskeleton to the cytoskeleton. The LINC
Zhou, Can, Rao, Li, Warren, Derek T, Shanahan, Catherine M, Zhang, Qiuping   +4 more
openaire   +4 more sources

Drosophila Nesprin-1 controls glutamate receptor density at neuromuscular junctions

Cellular and Molecular Life Sciences, 2014
Nesprin-1 is a core component of a protein complex connecting nuclei to cytoskeleton termed LINC (linker of nucleoskeleton and cytoskeleton). Nesprin-1 is anchored to the nuclear envelope by its C-terminal KASH domain, the disruption of which has been associated with neuronal and neuromuscular pathologies, including autosomal recessive cerebellar ...
Véronique Morel, Simon Lepicard, Alexandre N. Rey, Marie‐Laure Parmentier, Laurent Schaeffer   +4 more
openalex   +4 more sources