Nucleophosmin is selectively deposited on mRNA during polyadenylation
- 9 April 2006
- journal article
- research article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 13 (5) , 429-435
- https://doi.org/10.1038/nsmb1080
Abstract
Nucleophosmin (NPM), an abundant, predominantly nucleolar protein that influences numerous cellular processes, was shown to specifically associate with the bodies of messenger RNAs as a result of the process of 3′-end formation. NPM deposition requires polyadenylation but not the 3′ cleavage event to occur on the transcript. Furthermore, the protein does not associate with RNAs bearing a preformed poly(A) tail or with mRNAs that have undergone cleavage but not polyadenylation. A region within 10 bases upstream of the AAUAAA element is required for NPM association, but deposition of the protein seems to be sequence independent. NPM association with poly(A)+ mRNAs was also demonstrated in vivo. NPM, therefore, represents a mark left on transcripts as a result of 3′-end processing and may have a role in one or more of a variety of post-transcriptional processes influenced by the polyadenylation event.Keywords
This publication has 62 references indexed in Scilit:
- Thr199 phosphorylation targets nucleophosmin to nuclear speckles and represses pre‐mRNA processingFEBS Letters, 2005
- Nucleophosmin/B23-binding peptide inhibits tumor growth and up-regulates transcriptional activity of p53Biochemical and Biophysical Research Communications, 2005
- Nucleophosmin/B23, a Nuclear PI(3,4,5)P3 Receptor, Mediates the Antiapoptotic Actions of NGF by Inhibiting CADMolecular Cell, 2005
- SRprises along a Messenger’s JourneyMolecular Cell, 2005
- Proteomic Analysis of theArabidopsisNucleolus Suggests Novel Nucleolar FunctionsMolecular Biology of the Cell, 2005
- Nuclear export of RNABiology of the Cell, 2004
- The nucleolus is involved in mRNA export from the nucleus in fission yeastJournal of Cell Science, 2004
- Directed Proteomic Analysis of the Human NucleolusCurrent Biology, 2002
- HnRNP L binds a cis-acting RNA sequence element that enables intron-dependent gene expression.Genes & Development, 1995
- Accurate cleavage and polyadenylation of exogenous RNA substrateCell, 1985