Výsledky vyhledávání - "Livija, Zlopasa"

Nucleo-cytoplasmic shuttling of the endonuclease ankyrin repeats and LEM domain-containing protein 1 (Ankle1) is mediated by canonical nuclear export- and nuclear import signals

Autor: Livija, Zlopasa, Andreas, Brachner, Roland, Foisner

Publikováno v: BMC Cell Biology

Background Ankyrin repeats and LEM domain containing protein 1 (Ankle1) belongs to the LEM protein family, whose members share a chromatin-interacting LEM motif. Unlike most other LEM proteins, Ankle1 is not an integral protein of the inner nuclear m

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ebb8647a44db2cd00ba0fc8160f65bc9
https://pubmed.ncbi.nlm.nih.gov/27245214

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Additional file 3: Figure S3. of Nucleo-cytoplasmic shuttling of the endonuclease ankyrin repeats and LEM domain-containing protein 1 (Ankle1) is mediated by canonical nuclear export- and nuclear import signals

Autor: Livija Zlopasa, Brachner, Andreas, Foisner, Roland

Ankle1 does not accumulate on condensed chromosomes during mitosis. U2OS cells stably expressing GFP-Ankle1mut were fixed, stained with DAPI and imaged using a LSM700 confocal microscope. Representative images of at least five cells per mitotic phase

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Additional file 1: Figure S1. of Nucleo-cytoplasmic shuttling of the endonuclease ankyrin repeats and LEM domain-containing protein 1 (Ankle1) is mediated by canonical nuclear export- and nuclear import signals

Autor: Livija Zlopasa, Brachner, Andreas, Foisner, Roland

Catalytically dead Ankle1 mutant shuttles like wild-type Ankle1 but does not induce DNA damage response. (A) U2OS cells stably expressing GFP-Ankle1mut (GIY-YIG to GIY-AAA) were imaged using confocal microscopy without or after 3 h leptomycin B treat

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Additional file 2: Figure S2. of Nucleo-cytoplasmic shuttling of the endonuclease ankyrin repeats and LEM domain-containing protein 1 (Ankle1) is mediated by canonical nuclear export- and nuclear import signals

Autor: Livija Zlopasa, Brachner, Andreas, Foisner, Roland

DNA damage response is active in U2OS cells stably overexpressing GFP-Ankle1mut. Cells were fixed and stained for γH2A.X either untreated or after overnight treatment with bleomycin (1 μg/mL), mitomycin C (0.5 μg/mL) or hydroxyurea (100 μM) and i

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The endonuclease Ankle1 requires its LEM and GIY-YIG motifs for DNA cleavage in vivo

Autor: Roland Foisner, Juliane Braun, Siegfried Knasmüller, Medini Manohar Ghodgaonkar, Josef Jiricny, Veronika Ehrlich, Dennis Castor, Andreas Brachner, Livija Zlopasa, Josef Gotzmann

Publikováno v: Journal of cell science

The LEM domain (for lamina-associated polypeptide, emerin, MAN1 domain) defines a group of nuclear proteins that bind chromatin through interaction of the LEM motif with the conserved DNA crosslinking protein, barrier-to-autointegration factor (BAF).

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7de998f7e894b394ecb0f085e746a3e3
https://pubmed.ncbi.nlm.nih.gov/22399800

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