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The emerging roles of ribosomal histidyl hydroxylases in cell biology, physiology and disease
Hydroxylation is a novel protein modification catalyzed by a family of oxygenases that depend on fundamental nutrients and metabolites for activity. Protein hydroxylases have been implicated in a variety of key cellular processes that play important roles in both normal homeostasis and pathogenesis....
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer International Publishing
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6182338/ https://www.ncbi.nlm.nih.gov/pubmed/30151692 http://dx.doi.org/10.1007/s00018-018-2903-z |
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author | Bundred, James R. Hendrix, Eline Coleman, Mathew L. |
author_facet | Bundred, James R. Hendrix, Eline Coleman, Mathew L. |
author_sort | Bundred, James R. |
collection | PubMed |
description | Hydroxylation is a novel protein modification catalyzed by a family of oxygenases that depend on fundamental nutrients and metabolites for activity. Protein hydroxylases have been implicated in a variety of key cellular processes that play important roles in both normal homeostasis and pathogenesis. Here, in this review, we summarize the current literature on a highly conserved sub-family of oxygenases that catalyze protein histidyl hydroxylation. We discuss the evidence supporting the biochemical assignment of these emerging enzymes as ribosomal protein hydroxylases, and provide an overview of their role in immunology, bone development, and cancer. |
format | Online Article Text |
id | pubmed-6182338 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Springer International Publishing |
record_format | MEDLINE/PubMed |
spelling | pubmed-61823382018-10-22 The emerging roles of ribosomal histidyl hydroxylases in cell biology, physiology and disease Bundred, James R. Hendrix, Eline Coleman, Mathew L. Cell Mol Life Sci Review Hydroxylation is a novel protein modification catalyzed by a family of oxygenases that depend on fundamental nutrients and metabolites for activity. Protein hydroxylases have been implicated in a variety of key cellular processes that play important roles in both normal homeostasis and pathogenesis. Here, in this review, we summarize the current literature on a highly conserved sub-family of oxygenases that catalyze protein histidyl hydroxylation. We discuss the evidence supporting the biochemical assignment of these emerging enzymes as ribosomal protein hydroxylases, and provide an overview of their role in immunology, bone development, and cancer. Springer International Publishing 2018-08-27 2018 /pmc/articles/PMC6182338/ /pubmed/30151692 http://dx.doi.org/10.1007/s00018-018-2903-z Text en © The Author(s) 2018 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Review Bundred, James R. Hendrix, Eline Coleman, Mathew L. The emerging roles of ribosomal histidyl hydroxylases in cell biology, physiology and disease |
title | The emerging roles of ribosomal histidyl hydroxylases in cell biology, physiology and disease |
title_full | The emerging roles of ribosomal histidyl hydroxylases in cell biology, physiology and disease |
title_fullStr | The emerging roles of ribosomal histidyl hydroxylases in cell biology, physiology and disease |
title_full_unstemmed | The emerging roles of ribosomal histidyl hydroxylases in cell biology, physiology and disease |
title_short | The emerging roles of ribosomal histidyl hydroxylases in cell biology, physiology and disease |
title_sort | emerging roles of ribosomal histidyl hydroxylases in cell biology, physiology and disease |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6182338/ https://www.ncbi.nlm.nih.gov/pubmed/30151692 http://dx.doi.org/10.1007/s00018-018-2903-z |
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