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dc.creatorNechama, Morris
dc.creatorPeng, Yong
dc.creatorBell, Osnat
dc.creatorBriata, Paola
dc.creatorGherzi, Roberto
dc.creatorSchoenberg, Daniel R.
dc.creatorNaveh-Many, Tally
dc.identifier.citationMorris 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,
dc.description.abstractBackground: 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.en_US
dc.publisherBioMed Centralen_US
dc.titleKSRP-PMR1-exosome association determines parathyroid hormone mRNA levels and stability in transfected cellsen_US
dc.rights.ccAttribution 3.0 Unporteden_US

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Attribution 3.0 Unported
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