Fatscher, Tobias, Boehm, Volker ORCID: 0000-0001-7588-9842 and Gehring, Niels H. ORCID: 0000-0001-7792-1164 (2015). Mechanism, factors, and physiological role of nonsense-mediated mRNA decay. Cell. Mol. Life Sci., 72 (23). S. 4523 - 4545. BASEL: SPRINGER BASEL AG. ISSN 1420-9071

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Abstract

Nonsense-mediated mRNA decay (NMD) is a translation-dependent, multistep process that degrades irregular or faulty messenger RNAs (mRNAs). NMD mainly targets mRNAs with a truncated open reading frame (ORF) due to premature termination codons (PTCs). In addition, NMD also regulates the expression of different types of endogenous mRNA substrates. A multitude of factors are involved in the tight regulation of the NMD mechanism. In this review, we focus on the molecular mechanism of mammalian NMD. Based on the published data, we discuss the involvement of translation termination in NMD initiation. Furthermore, we provide a detailed overview of the core NMD machinery, as well as several peripheral NMD factors, and discuss their function. Finally, we present an overview of diseases associated with NMD factor mutations and summarize the current state of treatment for genetic disorders caused by nonsense mutations.

Item Type: Journal Article
Creators:
CreatorsEmailORCIDORCID Put Code
Fatscher, TobiasUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Boehm, VolkerUNSPECIFIEDorcid.org/0000-0001-7588-9842UNSPECIFIED
Gehring, Niels H.UNSPECIFIEDorcid.org/0000-0001-7792-1164UNSPECIFIED
URN: urn:nbn:de:hbz:38-386529
DOI: 10.1007/s00018-015-2017-9
Journal or Publication Title: Cell. Mol. Life Sci.
Volume: 72
Number: 23
Page Range: S. 4523 - 4545
Date: 2015
Publisher: SPRINGER BASEL AG
Place of Publication: BASEL
ISSN: 1420-9071
Language: English
Faculty: Faculty of Mathematics and Natural Sciences
Divisions: Faculty of Mathematics and Natural Sciences > Department of Biology > Institute for Genetics
Subjects: no entry
Uncontrolled Keywords:
KeywordsLanguage
EXON-JUNCTION COMPLEX; TRANSLATION INITIATION-FACTOR; HUMAN UPF1 HELICASE; RELEASE FACTOR ERF1; BETA-GLOBIN GENE; POLY(A)-BINDING PROTEIN; CRYSTAL-STRUCTURE; SACCHAROMYCES-CEREVISIAE; CAENORHABDITIS-ELEGANS; STRUCTURAL BASISMultiple languages
Biochemistry & Molecular Biology; Cell BiologyMultiple languages
Refereed: Yes
URI: http://kups.ub.uni-koeln.de/id/eprint/38652

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