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The kinase activity of human Rio1 is required for final steps of cytoplasmic maturation of 40S subunits
RIO proteins form a conserved family of atypical protein kinases. Humans possess three distinct RIO kinases—hRio1, hRio2, and hRio3, of which only hRio2 has been characterized with respect to its role in ribosomal biogenesis. Here we show that both hRio1 and hRio3, like hRio2, are associated with pr...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3248900/ https://www.ncbi.nlm.nih.gov/pubmed/22072790 http://dx.doi.org/10.1091/mbc.E11-07-0639 |
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author | Widmann, Barbara Wandrey, Franziska Badertscher, Lukas Wyler, Emanuel Pfannstiel, Jens Zemp, Ivo Kutay, Ulrike |
author_facet | Widmann, Barbara Wandrey, Franziska Badertscher, Lukas Wyler, Emanuel Pfannstiel, Jens Zemp, Ivo Kutay, Ulrike |
author_sort | Widmann, Barbara |
collection | PubMed |
description | RIO proteins form a conserved family of atypical protein kinases. Humans possess three distinct RIO kinases—hRio1, hRio2, and hRio3, of which only hRio2 has been characterized with respect to its role in ribosomal biogenesis. Here we show that both hRio1 and hRio3, like hRio2, are associated with precursors of 40S ribosomal subunits in human cells. Furthermore, we demonstrate that depletion of hRio1 by RNA interference affects the last step of 18S rRNA maturation and causes defects in the recycling of several trans-acting factors (hEnp1, hRio2, hLtv1, hDim2/PNO1, and hNob1) from pre-40S subunits in the cytoplasm. Although the effects of hRio1 and hRio2 depletion are similar, we show that the two kinases are not fully interchangeable. Moreover, rescue experiments with a kinase-dead mutant of hRio1 revealed that the kinase activity of hRio1 is essential for the recycling of the endonuclease hNob1 and its binding partner hDim2 from cytoplasmic pre-40S. Kinase-dead hRio1 is trapped on pre-40S particles containing hDim2 and hNob1 but devoid of hEnp1, hLtv1, and hRio2. These data reveal a role of hRio1 in the final stages of cytoplasmic pre-40S maturation. |
format | Online Article Text |
id | pubmed-3248900 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-32489002012-03-16 The kinase activity of human Rio1 is required for final steps of cytoplasmic maturation of 40S subunits Widmann, Barbara Wandrey, Franziska Badertscher, Lukas Wyler, Emanuel Pfannstiel, Jens Zemp, Ivo Kutay, Ulrike Mol Biol Cell Articles RIO proteins form a conserved family of atypical protein kinases. Humans possess three distinct RIO kinases—hRio1, hRio2, and hRio3, of which only hRio2 has been characterized with respect to its role in ribosomal biogenesis. Here we show that both hRio1 and hRio3, like hRio2, are associated with precursors of 40S ribosomal subunits in human cells. Furthermore, we demonstrate that depletion of hRio1 by RNA interference affects the last step of 18S rRNA maturation and causes defects in the recycling of several trans-acting factors (hEnp1, hRio2, hLtv1, hDim2/PNO1, and hNob1) from pre-40S subunits in the cytoplasm. Although the effects of hRio1 and hRio2 depletion are similar, we show that the two kinases are not fully interchangeable. Moreover, rescue experiments with a kinase-dead mutant of hRio1 revealed that the kinase activity of hRio1 is essential for the recycling of the endonuclease hNob1 and its binding partner hDim2 from cytoplasmic pre-40S. Kinase-dead hRio1 is trapped on pre-40S particles containing hDim2 and hNob1 but devoid of hEnp1, hLtv1, and hRio2. These data reveal a role of hRio1 in the final stages of cytoplasmic pre-40S maturation. The American Society for Cell Biology 2012-01-01 /pmc/articles/PMC3248900/ /pubmed/22072790 http://dx.doi.org/10.1091/mbc.E11-07-0639 Text en © 2012 Widmann et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Widmann, Barbara Wandrey, Franziska Badertscher, Lukas Wyler, Emanuel Pfannstiel, Jens Zemp, Ivo Kutay, Ulrike The kinase activity of human Rio1 is required for final steps of cytoplasmic maturation of 40S subunits |
title | The kinase activity of human Rio1 is required for final steps of cytoplasmic maturation of 40S subunits |
title_full | The kinase activity of human Rio1 is required for final steps of cytoplasmic maturation of 40S subunits |
title_fullStr | The kinase activity of human Rio1 is required for final steps of cytoplasmic maturation of 40S subunits |
title_full_unstemmed | The kinase activity of human Rio1 is required for final steps of cytoplasmic maturation of 40S subunits |
title_short | The kinase activity of human Rio1 is required for final steps of cytoplasmic maturation of 40S subunits |
title_sort | kinase activity of human rio1 is required for final steps of cytoplasmic maturation of 40s subunits |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3248900/ https://www.ncbi.nlm.nih.gov/pubmed/22072790 http://dx.doi.org/10.1091/mbc.E11-07-0639 |
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