Breaking News


Emerin protein function and structure

images emerin protein function and structure

Jacque and Stevenson concluded that HIV-1 cDNA, upon entering the nucleus, must interact with emerin to contact chromatin, and they suggested that molecules that prevent this interaction might promote abortive HIV-1 infection of a cell. DNA sequence-dependent compartmentalization and silencing of chromatin at the nuclear lamina. As a child, he had been limited in his participation in athletics in school. The arrangement of F-actin filaments impacts cell morphology, contractility and cell mechanics [ 84 ]. Single nuclei were cropped and subjected to 3D surface rendering followed by radial distance measurements of chromosome territories [ 8687 ]. Yorifuji, H.

  • Emerin, LEM domain (IPR) < InterPro < EMBLEBI

  • Emerin is a protein that in humans is encoded by the EMD gene, also known as the STA gene. Contents. 1 Structure; 2 Function; 3 Clinical significance; 4 Interactions; 5 References; 6 Further reading; 7 External links.

    Emerin. Gene Reviewed-Annotation score: Experimental evidence at protein leveli Legend: HelixTurnBeta strandPDB Structure known for this area. Emerin and several other LEM-domain proteins (e.g.
    Genome Res.

    Haraguchi et al.

    Emerin, LEM domain (IPR) < InterPro < EMBLEBI

    Mouse B-type lamins are required for proper organogenesis but not by embryonic stem cells. Emerin modulates spatial organization of chromosome territories in cells on softer matrices.

    Ye Q, Worman HJ. Mutations in Emery-Dreifuss muscular dystrophy and their effects on emerin protein expression.

    images emerin protein function and structure
    An emerin mutant defective in BAF binding in vitro failed to localize at the core in vivo and subsequently failed to localize at the reformed nuclear envelope.

    images emerin protein function and structure

    A myosin I isoform in the nucleus. Nuclear Lamin-a scales with tissue stiffness and enhances matrix-directed differentiation.

    Topological domains in mammalian genomes identified by analysis of chromatin interactions.


    Mutations in emerin cause X-linked recessive Emery—Dreifuss muscular dystrophywhich is characterized by early contractures in the Achilles tendons, elbows and post-cervical muscles; muscle weakness proximal in the upper limbs and distal in lower limbs; along with cardiac conduction defects that range from sinus bradycardiaPR prolongation to complete heart block.

    The Nuclear Lamina and Its Functions in the Nucleus The emerin protein conservation in evolution, its ubiquitous expression, and its requirement for.

    The structural hypothesis is based on the idea that lamin, along with other NE proteins. INM proteins bind to lamins to form a proteinaceous network called the nuclear lamina that is required for nuclear structure and function.


    These emerin‐regulated cellular functions include regulating genomic architecture, maintaining nuclear structure and regulating gene.
    Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

    Characterization of the Drosophila melanogaster genome at the nuclear lamina. GWAS Central. Ellis, J.

    X-linked recessive.

    Video: Emerin protein function and structure Protein Functions - Functions of protein - Science Land

    Emerin has been shown to interact with:. Stochastic genome-nuclear lamina interactions: modulating roles of Lamin a and BAF.

    images emerin protein function and structure
    The molecular architecture of lamins in somatic cells.

    images emerin protein function and structure

    Ellis et al. Cartegni, L. Bank EM, Gruenbaum Y.

    Video: Emerin protein function and structure NUCLEAR LAMINA

    Using protein pull-down and coimmunoprecipitation assays, Libotte et al.

    2 thoughts on “Emerin protein function and structure

    1. Nuclear myosin 1 contributes to a chromatin landscape compatible with RNA polymerase II transcription activation. A-type lamins bind both hetero- and euchromatin, the latter being regulated by lamina-associated polypeptide 2 alpha.