TU Darmstadt / ULB / TUbiblio

Hypoxia reduces MAX expression in endothelial cells by unproductive splicing

Kemmerer, Katrin and Weigand, Julia E. (2014):
Hypoxia reduces MAX expression in endothelial cells by unproductive splicing.
In: FEBS letters, 588 (24), pp. 4784-4790. Wiley, ISSN 1873-3468,
DOI: 10.1016/j.febslet.2014.11.011,
[Article]

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.

Item Type: Article
Erschienen: 2014
Creators: Kemmerer, Katrin and Weigand, Julia E.
Title: Hypoxia reduces MAX expression in endothelial cells by unproductive splicing
Language: English
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.

Journal or Publication Title: FEBS letters
Journal volume: 588
Number: 24
Publisher: Wiley
Divisions: 10 Department of Biology
10 Department of Biology > RNA Biochemistry
Date Deposited: 05 Mar 2021 07:31
DOI: 10.1016/j.febslet.2014.11.011
Official URL: https://febs.onlinelibrary.wiley.com/doi/10.1016/j.febslet.2...
Identification Number: pmid:25451222
Export:
Suche nach Titel in: TUfind oder in Google
Send an inquiry Send an inquiry

Options (only for editors)
Show editorial Details Show editorial Details