Translational symphony in (hnRNP) C major for APP

Stringent post-transcriptional regulation of the amyloid precursor protein (APP) is critical for maintaining proper neurological function. In this issue, Lee et al . identify two RNA-binding proteins, FMRP and hnRNP C, that have opposite effects on APP translation via competing interactions, surpris...

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Veröffentlicht in:	Nature structural & molecular biology 2010-06, Vol.17 (6), p.675-676
Hauptverfasser:	Lee, Jerome E, Wilusz, Jeffrey
Format:	Artikel
Sprache:	eng
Schlagworte:	631/208/200 631/337/574 Amyloid beta-protein Amyloid beta-Protein Precursor - chemistry Amyloid beta-Protein Precursor - genetics Amyloid beta-Protein Precursor - metabolism Binding sites Biochemistry Biological Microscopy Biomedical and Life Sciences Fragile X Mental Retardation Protein - metabolism Genetic aspects Genetic regulation Heterogeneous-Nuclear Ribonucleoprotein Group C - metabolism Humans Life Sciences Membrane Biology Messenger RNA Models, Biological Molecular biology Neurology news-and-views Open Reading Frames Physiological aspects Protein Biosynthesis Protein Structure Proteins Ribonucleic acid Ribonucleoproteins RNA RNA, Messenger - genetics RNA, Messenger - metabolism Signal Transduction Trans-Activators - metabolism
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Beschreibung
Zusammenfassung:	Stringent post-transcriptional regulation of the amyloid precursor protein (APP) is critical for maintaining proper neurological function. In this issue, Lee et al . identify two RNA-binding proteins, FMRP and hnRNP C, that have opposite effects on APP translation via competing interactions, surprisingly, with the mRNA coding region.
ISSN:	1545-9993 1545-9985
DOI:	10.1038/nsmb0610-675