Lamin A/C-dependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope - sprookjes - yvandenbroek - TriplyDB

Lamin A/C-dependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope

Lamin A/C-dependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope

http://www.wikidata.org/entity/Q24531346

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A novel role for the nuclear membrane protein emerin in association of the centrosome to the outer nuclear membrane The inner nuclear membrane protein emerin regulates beta-catenin activity by restricting its accumulation in the nucleus Coupling of the nucleus and cytoplasm: role of the LINC complex Cytoskeletal interactions at the nuclear envelope mediated by nesprins Structural requirements for the assembly of LINC complexes and their function in cellular mechanical stiffness LINC complex alterations in DMD and EDMD/CMT fibroblasts Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes Nesprin-3 regulates endothelial cell morphology, perinuclear cytoskeletal architecture, and flow-induced polarization Nuclear actin extends, with no contraction in sight.Multiple roles for emerin: implications for Emery-Dreifuss muscular dystrophy Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin Under Pressure: Mechanical Stress Management in the Nucleus The Nesprin family member ANC-1 regulates synapse formation and axon termination by functioning in a pathway with RPM-1 and β-Catenin In silico synchronization reveals regulators of nuclear ruptures in lamin A/C deficient model cells.Cytoskeletal tension induces the polarized architecture of the nucleus.Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells Nesprin-2 interacts with meckelin and mediates ciliogenesis via remodelling of the actin cytoskeleton KDP-1 is a nuclear envelope KASH protein required for cell-cycle progression Lamin A variants that cause striated muscle disease are defective in anchoring transmembrane actin-associated nuclear lines for nuclear movement.The role of Lamin A in cytoskeleton organization in colorectal cancer cells: a proteomic investigation.Novel nesprin-1 mutations associated with dilated cardiomyopathy cause nuclear envelope disruption and defects in myogenesis.Interactions between nuclei and the cytoskeleton are mediated by SUN-KASH nuclear-envelope bridges.Attenuated hypertrophic response to pressure overload in a lamin A/C haploinsufficiency mouse Actomyosin tension exerted on the nucleus through nesprin-1 connections influences endothelial cell adhesion, migration, and cyclic strain-induced reorientation.Nesprin-2 interacts with {alpha}-catenin and regulates Wnt signaling at the nuclear envelope.The differential formation of the LINC-mediated perinuclear actin cap in pluripotent and somatic cells.UNC-83 IS a KASH protein required for nuclear migration and is recruited to the outer nuclear membrane by a physical interaction with the SUN protein UNC-84 Direct actin binding to A- and B-type lamin tails and actin filament bundling by the lamin A tail.Mapping of protein- and chromatin-interactions at the nuclear lamina Identification of differential protein interactors of lamin A and progerin Large-scale modelling of the divergent spectrin repeats in nesprins: giant modular proteins Structural protein 4.1R is integrally involved in nuclear envelope protein localization, centrosome-nucleus association and transcriptional signaling.Mutations in LMNA modulate the lamin A--Nesprin-2 interaction and cause LINC complex alterations Targeted ablation of nesprin 1 and nesprin 2 from murine myocardium results in cardiomyopathy, altered nuclear morphology and inhibition of the biomechanical gene response.The nuclear envelope: form and reformation.Nesprins: tissue-specific expression of epsilon and other short isoforms.Making the LINC: SUN and KASH protein interactions.Nesprins, but not sun proteins, switch isoforms at the nuclear envelope during muscle development.Nesprin-2-dependent ERK1/2 compartmentalisation regulates the DNA damage response in vascular smooth muscle cell ageing The nuclear envelope protein Nesprin-2 has roles in cell proliferation and differentiation during wound healing.

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Lamin A/C-dependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope

http://www.wikidata.org/entity/Q24531346

description

2005 nî lūn-bûn

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2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2005 թվականի հուլիսին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

Lamin A/C-dependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope

@ast

Lamin A/C-dependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope

@en

Lamin A/C-dependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope

@en-gb

Lamin A/C-dependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope

@nl

type

label

Lamin A/C-dependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope

@ast

Lamin A/C-dependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope

@en

Lamin A/C-dependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope

@en-gb

Lamin A/C-dependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope

@nl

prefLabel

Lamin A/C-dependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope

@ast

Lamin A/C-dependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope

@en

Lamin A/C-dependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope

@en-gb

Lamin A/C-dependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope

@nl

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MBC.E04-11-1009

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Molecular Biology of the Cell

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Lamin A/C-dependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope

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Angelika A Noegel

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Christopher Hutchison

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Hafida Zaim

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Iakowos Karakesisoglou

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Manfred Wehnert

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Martina Munck

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Thorsten Libotte

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Ursula Sauder

http://www.w3.org/2001/XMLSchema#string

V C Padmakumar

http://www.w3.org/2001/XMLSchema#string

Wenshu Lu

http://www.w3.org/2001/XMLSchema#string

P2860

UNC-84 localizes to the nuclear envelope and is required for nuclear migration and anchoring during C. elegans development

Syne-1, a dystrophin- and Klarsicht-related protein associated with synaptic nuclei at the neuromuscular junction

Nesprins: a novel family of spectrin-repeat-containing proteins that localize to the nuclear membrane in multiple tissues

Myne-1, a spectrin repeat transmembrane protein of the myocyte inner nuclear membrane, interacts with lamin A/C

Nesprin-2 is a multi-isomeric protein that binds lamin and emerin at the nuclear envelope and forms a subcellular network in skeletal muscle

NUANCE, a giant protein connecting the nucleus and actin cytoskeleton

Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane

Nesprin-1alpha self-associates and binds directly to emerin and lamin A in vitro

The nesprins are giant actin-binding proteins, orthologous to Drosophila melanogaster muscle protein MSP-300

In vivo and in vitro interaction between human transcription factor MOK2 and nuclear lamin A/C.

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819994

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10.1091/MBC.E04-11-1009

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7

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Birthe Fahrenkrog

Maria Victoria Schneider

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