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doi:10.22028/D291-34887
Titel: | Critical Protein–Protein Interactions Determine the Biological Activity of Elk-1, a Master Regulator of Stimulus-Induced Gene Transcription |
VerfasserIn: | Thiel, Gerald Backes, Tobias M. Guethlein, Lisbeth A. Rössler, Oliver G. |
Sprache: | Englisch |
Titel: | Molecules |
Bandnummer: | 26 |
Heft: | 20 |
Verlag/Plattform: | MDPI |
Erscheinungsjahr: | 2021 |
Freie Schlagwörter: | c-Fos Egr-1 histone deacetylase MAP kinase mediator SRF SUMO |
DDC-Sachgruppe: | 610 Medizin, Gesundheit |
Dokumenttyp: | Journalartikel / Zeitschriftenartikel |
Abstract: | Elk-1 is a transcription factor that binds together with a dimer of the serum response factor (SRF) to the serum-response element (SRE), a genetic element that connects cellular stimulation with gene transcription. Elk-1 plays an important role in the regulation of cellular proliferation and apoptosis, thymocyte development, glucose homeostasis and brain function. The biological function of Elk-1 relies essentially on the interaction with other proteins. Elk-1 binds to SRF and generates a functional ternary complex that is required to activate SRE-mediated gene transcription. Elk-1 is kept in an inactive state under basal conditions via binding of a SUMO-histone deacetylase complex. Phosphorylation by extracellular signal-regulated protein kinase, c-Jun N-terminal protein kinase or p38 upregulates the transcriptional activity of Elk-1, mediated by binding to the mediator of RNA polymerase II transcription (Mediator) and the transcriptional coactivator p300. Strong and extended phosphorylation of Elk-1 attenuates Mediator and p300 recruitment and allows the binding of the mSin3A-histone deacetylase corepressor complex. The subsequent dephosphorylation of Elk-1, catalyzed by the protein phosphatase calcineurin, facilitates the re-SUMOylation of Elk1, transforming Elk-1 back to a transcriptionally inactive state. Thus, numerous protein–protein interactions control the activation cycle of Elk-1 and are essential for its biological function. |
DOI der Erstveröffentlichung: | 10.3390/molecules26206125 |
Link zu diesem Datensatz: | urn:nbn:de:bsz:291--ds-348877 hdl:20.500.11880/31915 http://dx.doi.org/10.22028/D291-34887 |
ISSN: | 1420-3049 |
Datum des Eintrags: | 27-Okt-2021 |
Fakultät: | M - Medizinische Fakultät |
Fachrichtung: | M - Medizinische Biochemie und Molekularbiologie |
Professur: | M - Prof. Dr. Gerald Thiel |
Sammlung: | SciDok - Der Wissenschaftsserver der Universität des Saarlandes |
Dateien zu diesem Datensatz:
Datei | Beschreibung | Größe | Format | |
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molecules-26-06125-v3.pdf | 3,33 MB | Adobe PDF | Öffnen/Anzeigen |
Diese Ressource wurde unter folgender Copyright-Bestimmung veröffentlicht: Lizenz von Creative Commons