Most mammalian protein coding genes are subject to alternative cleavage and polyadenylation (APA), which can generate distinct mRNA 3′UTRs with differing regulatory potential. Although this process has been intensely studied in recent years, it remains unclear how and to what extent cleavage site selection is regulated under different physiological conditions. The cleavage factor Im (CFIm) complex is a core component of the mammalian cleavage machinery, and the observation that its depletion causes transcriptome-wide changes in cleavage site use makes it a key candidate regulator of APA. This review aims to summarize current knowledge of the CFIm complex, and explores the evidence surrounding its potential contribution to regulation of APA.
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August 2016
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A schematic representation of TGF-β and BMP9 signalling in endothelial cells via their serine/threonine type I and type II receptors, co-receptor endoglin and downstream Smad intracellular proteins. Taken from the article ‘Targeting tumour vasculature by inhibiting activing receptor-like kinase (ALK)1 function’ by de Vinuesa et al. in this issue (volume 44, issue 4, pages 1142-1149). - PDF Icon PDF LinkTable of Contents
Review Article|
August 15 2016
Cleavage factor Im (CFIm) as a regulator of alternative polyadenylation
Jessica G. Hardy;
Jessica G. Hardy
*Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, U.K.
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Chris J. Norbury
Chris J. Norbury
1
*Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, U.K.
1To whom correspondence should be addressed (email chris.norbury@path.ox.ac.uk).
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Biochem Soc Trans (2016) 44 (4): 1051–1057.
Article history
Received:
March 29 2016
Citation
Jessica G. Hardy, Chris J. Norbury; Cleavage factor Im (CFIm) as a regulator of alternative polyadenylation. Biochem Soc Trans 15 August 2016; 44 (4): 1051–1057. doi: https://doi.org/10.1042/BST20160078
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