p180 promotes the ribosome-independent localization of a subset of mRNA to the endoplasmic reticulum.

In metazoans, the majority of mRNAs coding for secreted and membrane-bound proteins are translated on the surface of the endoplasmic reticulum (ER). Although the targeting of these transcripts to the surface of the ER can be mediated by the translation of a signal sequence and their maintenance is m...

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Autores principales:	Xianying A Cui, Hui Zhang, Alexander F Palazzo
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/8d61723bd83a45158f12e9c7c31a7e9f
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spelling	oai:doaj.org-article:8d61723bd83a45158f12e9c7c31a7e9f2021-11-18T05:36:38Zp180 promotes the ribosome-independent localization of a subset of mRNA to the endoplasmic reticulum.1544-91731545-788510.1371/journal.pbio.1001336https://doaj.org/article/8d61723bd83a45158f12e9c7c31a7e9f2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22679391/?tool=EBIhttps://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885In metazoans, the majority of mRNAs coding for secreted and membrane-bound proteins are translated on the surface of the endoplasmic reticulum (ER). Although the targeting of these transcripts to the surface of the ER can be mediated by the translation of a signal sequence and their maintenance is mediated by interactions between the ribosome and the translocon, it is becoming increasingly clear that additional ER-localization pathways exist. Here we demonstrate that many of these mRNAs can be targeted to, and remain associated with, the ER independently of ribosomes and translation. Using a mass spectrometry analysis of proteins that associate with ER-bound polysomes, we identified putative mRNA receptors that may mediate this alternative mechanism, including p180, an abundant, positively charged membrane-bound protein. We demonstrate that p180 over-expression can enhance the association of generic mRNAs with the ER. We then show that p180 contains a lysine-rich region that can directly interact with RNA in vitro. Finally, we demonstrate that p180 is required for the efficient ER-anchoring of bulk poly(A) and of certain transcripts, such as placental alkaline phosphatase and calreticulin, to the ER. In summary, we provide, to our knowledge, the first mechanistic details for an alternative pathway to target and maintain mRNA at the ER. It is likely that this alternative pathway not only enhances the fidelity of protein sorting, but also localizes mRNAs to various subdomains of the ER and thus contributes to cellular organization.Xianying A CuiHui ZhangAlexander F PalazzoPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 10, Iss 5, p e1001336 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Xianying A Cui Hui Zhang Alexander F Palazzo p180 promotes the ribosome-independent localization of a subset of mRNA to the endoplasmic reticulum.
description	In metazoans, the majority of mRNAs coding for secreted and membrane-bound proteins are translated on the surface of the endoplasmic reticulum (ER). Although the targeting of these transcripts to the surface of the ER can be mediated by the translation of a signal sequence and their maintenance is mediated by interactions between the ribosome and the translocon, it is becoming increasingly clear that additional ER-localization pathways exist. Here we demonstrate that many of these mRNAs can be targeted to, and remain associated with, the ER independently of ribosomes and translation. Using a mass spectrometry analysis of proteins that associate with ER-bound polysomes, we identified putative mRNA receptors that may mediate this alternative mechanism, including p180, an abundant, positively charged membrane-bound protein. We demonstrate that p180 over-expression can enhance the association of generic mRNAs with the ER. We then show that p180 contains a lysine-rich region that can directly interact with RNA in vitro. Finally, we demonstrate that p180 is required for the efficient ER-anchoring of bulk poly(A) and of certain transcripts, such as placental alkaline phosphatase and calreticulin, to the ER. In summary, we provide, to our knowledge, the first mechanistic details for an alternative pathway to target and maintain mRNA at the ER. It is likely that this alternative pathway not only enhances the fidelity of protein sorting, but also localizes mRNAs to various subdomains of the ER and thus contributes to cellular organization.
format	article
author	Xianying A Cui Hui Zhang Alexander F Palazzo
author_facet	Xianying A Cui Hui Zhang Alexander F Palazzo
author_sort	Xianying A Cui
title	p180 promotes the ribosome-independent localization of a subset of mRNA to the endoplasmic reticulum.
title_short	p180 promotes the ribosome-independent localization of a subset of mRNA to the endoplasmic reticulum.
title_full	p180 promotes the ribosome-independent localization of a subset of mRNA to the endoplasmic reticulum.
title_fullStr	p180 promotes the ribosome-independent localization of a subset of mRNA to the endoplasmic reticulum.
title_full_unstemmed	p180 promotes the ribosome-independent localization of a subset of mRNA to the endoplasmic reticulum.
title_sort	p180 promotes the ribosome-independent localization of a subset of mrna to the endoplasmic reticulum.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/8d61723bd83a45158f12e9c7c31a7e9f
work_keys_str_mv	AT xianyingacui p180promotestheribosomeindependentlocalizationofasubsetofmrnatotheendoplasmicreticulum AT huizhang p180promotestheribosomeindependentlocalizationofasubsetofmrnatotheendoplasmicreticulum AT alexanderfpalazzo p180promotestheribosomeindependentlocalizationofasubsetofmrnatotheendoplasmicreticulum
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p180 promotes the ribosome-independent localization of a subset of mRNA to the endoplasmic reticulum.

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