Results 31 to 40 of about 4,186 (177)

A-type lamins anchor emerin at the inner nuclear membrane via two independent binding sites. [PDF]

open access: yesJ Biol Chem
Lamins form a dense meshwork at the inner surface of the inner nuclear membrane (INM), where they interact with other nuclear envelope proteins such as emerin.
Odell J, Nedza K, Lammerding J.
europepmc   +2 more sources

Emerin intermolecular links to emerin and BAF

open access: yesJournal of Cell Science, 2014
Emerin is a conserved nuclear membrane LEM-domain protein that binds lamins and BAF (barrier-to-integration factor; BANF1) as a component of nuclear lamina structure. We report an advance in understanding the molecular basis of emerin function: inter-molecular emerin-emerin association.
Jason M, Berk   +6 more
openaire   +3 more sources

Emerin Is Required for Proper Nucleus Reassembly after Mitosis: Implications for New Pathogenetic Mechanisms for Laminopathies Detected in EDMD1 Patients

open access: yesCells, 2019
Emerin is an essential LEM (LAP2, Emerin, MAN1) domain protein in metazoans and an integral membrane protein associated with inner and outer nuclear membranes.
Magda Dubińska-Magiera   +5 more
doaj   +1 more source

An Emerin LEM-Domain Mutation Impairs Cell Response to Mechanical Stress

open access: yesCells, 2019
Emerin is a nuclear envelope protein that contributes to genome organization and cell mechanics. Through its N-terminal LAP2-emerin-MAN1 (LEM)-domain, emerin interacts with the DNA-binding protein barrier-to-autointegration (BAF).
Nada Essawy   +9 more
doaj   +1 more source

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

open access: yesPLoS Biology, 2004
X-linked Emery-Dreifuss muscular dystrophy is caused by loss of emerin, a LEM-domain protein of the nuclear inner membrane. To better understand emerin function, we used affinity chromatography to purify emerin-binding proteins from nuclear extracts of ...
James M Holaska   +2 more
doaj   +1 more source

MAPK signaling pathways and HDAC3 activity are disrupted during differentiation of emerin-null myogenic progenitor cells

open access: yesDisease Models & Mechanisms, 2017
Mutations in the gene encoding emerin cause Emery–Dreifuss muscular dystrophy (EDMD). Emerin is an integral inner nuclear membrane protein and a component of the nuclear lamina. EDMD is characterized by skeletal muscle wasting, cardiac conduction defects
Carol M. Collins   +2 more
doaj   +1 more source

Comparative Interactome Analysis of Emerin, MAN1 and LEM2 Reveals a Unique Role for LEM2 in Nucleotide Excision Repair

open access: yesCells, 2020
LAP2-Emerin-MAN1 (LEM) domain-containing proteins represent an abundant group of inner nuclear membrane proteins involved in diverse nuclear functions, but their functional redundancies remain unclear.
Bernhard Moser   +4 more
doaj   +1 more source

Negative correlation between the nuclear size and nuclear Lamina component Lamin A in intraductal papillary mucinous neoplasms of the pancreas

open access: yesPathology and Oncology Research, 2022
Background: The nuclear laminar protein Lamin A and inner nuclear membrane protein Emerin plays important role in sustaining nuclear structure. However, They have not investigated the significance of these proteins for development of pancreatic ...
Tamaki Hiroe   +8 more
doaj   +1 more source

Emerin anchors Msx1 and its protein partners at the nuclear periphery to inhibit myogenesis

open access: yesCell & Bioscience, 2019
Background Previous studies have shown that in myogenic precursors, the homeoprotein Msx1 and its protein partners, histone methyltransferases and repressive histone marks, tend to be enriched on target myogenic regulatory genes at the nuclear periphery.
Zhangjing Ma   +8 more
doaj   +1 more source

Probing the Environment of Emerin by Enhanced Ascorbate Peroxidase 2 (APEX2)-Mediated Proximity Labeling

open access: yesCells, 2020
Emerin is one of the best characterized proteins of the inner nuclear membrane, but can also occur at the level of the endoplasmic reticulum. We now use enhanced ascorbate peroxidase 2 (APEX2) to probe the environment of emerin.
Marret Müller   +4 more
doaj   +1 more source

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