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KSRP-PMR1-exosome association determines parathyroid hormone mRNA levels and stability in transfected cells

Please use this identifier to cite or link to this item: http://hdl.handle.net/1811/47428

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Title: KSRP-PMR1-exosome association determines parathyroid hormone mRNA levels and stability in transfected cells
Creators: Nechama, Morris; Peng, Yong; Bell, Osnat; Briata, Paola; Gherzi, Roberto; Schoenberg, Daniel R.; Naveh-Many, Tally
Issue Date: 2009-09-23
Publisher: BioMed Central
Citation: Morris Nechama et al, "KSRP-PMR1-exosome association determines parathyroid hormone mRNA levels and stability in transfected cells," BMC Cell Biology 10 (2009), doi:10.1186/1471-2121-10-70,http://www.biomedcentral.com/1471-2121/10/70
DOI: 10.1186/1471-2121-10-70
Abstract: Background: Parathyroid hormone (PTH) gene expression is regulated post-transcriptionally through the binding of the trans-acting proteins AU rich binding factor 1 (AUF1), Upstream of N-ras (Unr) and KH-type splicing regulatory protein (KSRP) to an AU rich element (ARE) in PTH mRNA 3'-UTR. AUF1 and Unr stabilize PTH mRNA while KSRP, recruiting the exoribonucleolytic complex exosome, promotes PTH mRNA decay. Results: PTH mRNA is cleaved by the endoribonuclease polysomal ribonuclease 1 (PMR1) in an ARE-dependent manner. Moreover, PMR1 co-immunoprecipitates with PTH mRNA, the exosome and KSRP. Knock-down of either exosome components or KSRP by siRNAs prevents PMR1-mediated cleavage of PTH mRNA. Conclusion: PTH mRNA is a target for the endonuclease PMR1. The PMR1 mediated decrease in PTH mRNA levels involves the PTH mRNA 3'-UTR ARE, KSRP and the exosome. This represents an unanticipated mechanism by which the decay of an ARE-containing mRNA is facilitated by KSRP and is dependent on both the exosome and an endoribonuclease.
ISSN: 1471-2121
URI: http://hdl.handle.net/1811/47428
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Attribution 3.0 Unported