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Hypoxia reduces MAX expression in endothelial cells by unproductive splicing

Kemmerer, Katrin ; Weigand, Julia E. (2014)
Hypoxia reduces MAX expression in endothelial cells by unproductive splicing.
In: FEBS letters, 588 (24)
doi: 10.1016/j.febslet.2014.11.011
Artikel, Bibliographie

Kurzbeschreibung (Abstract)

The MYC-MAX-MXD network is involved in the regulation of cell differentiation and proliferation. Hypoxia affects the expression levels of several members of this network, but changes specific to MAX expression have so far not been shown. We found that in endothelial cells, hypoxia induces alternative splicing of MAX, thereby increasing the expression of two MAX isoforms that differ from the wild type in their 3' end. Isoform C is degraded by nonsense-mediated decay and isoform E encodes a highly unstable protein. The instability of isoform E is conferred by 36 isoform-specific amino acids, which have the capacity to destabilize heterologous proteins. Both splicing events are therefore unproductive and serve the purpose to downregulate the wild type protein.

Typ des Eintrags: Artikel
Erschienen: 2014
Autor(en): Kemmerer, Katrin ; Weigand, Julia E.
Art des Eintrags: Bibliographie
Titel: Hypoxia reduces MAX expression in endothelial cells by unproductive splicing
Sprache: Englisch
Publikationsjahr: 15 November 2014
Verlag: Wiley
Titel der Zeitschrift, Zeitung oder Schriftenreihe: FEBS letters
Jahrgang/Volume einer Zeitschrift: 588
(Heft-)Nummer: 24
DOI: 10.1016/j.febslet.2014.11.011
URL / URN: https://febs.onlinelibrary.wiley.com/doi/10.1016/j.febslet.2...
Kurzbeschreibung (Abstract):

The MYC-MAX-MXD network is involved in the regulation of cell differentiation and proliferation. Hypoxia affects the expression levels of several members of this network, but changes specific to MAX expression have so far not been shown. We found that in endothelial cells, hypoxia induces alternative splicing of MAX, thereby increasing the expression of two MAX isoforms that differ from the wild type in their 3' end. Isoform C is degraded by nonsense-mediated decay and isoform E encodes a highly unstable protein. The instability of isoform E is conferred by 36 isoform-specific amino acids, which have the capacity to destabilize heterologous proteins. Both splicing events are therefore unproductive and serve the purpose to downregulate the wild type protein.

ID-Nummer: pmid:25451222
Fachbereich(e)/-gebiet(e): 10 Fachbereich Biologie
10 Fachbereich Biologie > RNA Biochemie
Hinterlegungsdatum: 05 Mär 2021 07:31
Letzte Änderung: 05 Mär 2021 07:31
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