Abstract
In both eukaryotic and prokaryotic cells, it has been recently established that mRNAs encoding secreted and membrane proteins can be localized to the surface of membranes via both translation-dependent and RNA element-mediated mechanisms. Previously, we showed that the placental alkaline phosphatase (ALPP) mRNA can be localized to the ER membrane independently of translation, and this localization is mediated by p180, an mRNA receptor present in the ER. In this article, we aimed to identify the cis-acting RNA element in ALPP. Using chimera constructs containing fragments of the ALPP mRNA, we demonstrate that the ER-localizing RNA element is present within the 3' end of the open reading frame and codes for a transmembrane domain. In addition, we show that this region requires p180 for efficient ER anchoring. Taken together, we provide the first insight into the nature of cis-acting ER-localizing RNA elements responsible for localizing mRNAs on the ER in mammalian cells.
Highlights
Certain mRNAs are anchored to the endoplasmic reticulum (ER) by p180
The cells were fixed, and AF1 mRNA was detected by Fluorescent in Situ Hybridization (FISH) using probes directed to the alkaline phosphatase (ALPP) ORF, whereas AF2 was detected using probes that hybridize to the ftz ORF
We have identified a region of ALPP that contains an RNA element that promotes ER localization
Summary
Results: The placental alkaline phosphatase mRNA requires its transmembrane domain coding region to be anchored by p180. Conclusion: Translational-independent ER targeting of mRNA by p180 can be mediated by regions of the ORF that encode hydrophobic peptides. Significance: Translational-independent targeting of mRNA to membranes may be mediated by a mechanism conserved between prokaryotes and eukaryotes. We showed that the placental alkaline phosphatase (ALPP) mRNA can be localized to the ER membrane independently of translation, and this localization is mediated by p180, an mRNA receptor present in the ER. Using chimera constructs containing fragments of the ALPP mRNA, we demonstrate that the ER-localizing RNA element is present within the 3 end of the open reading frame and codes for a transmembrane domain. We provide the first insight into the nature of cis-acting ER-localizing RNA elements responsible for localizing mRNAs on the ER in mammalian cells
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