Cargando…
The mutual interaction of glycolytic enzymes and RNA in post-transcriptional regulation
About three decades ago, researchers suggested that metabolic enzymes participate in cellular processes that are unrelated to their catalytic activity, and the term “moonlighting functions” was proposed. Recently developed advanced technologies in the field of RNA interactome capture now unveil the...
Autores principales: | , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory Press
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9745834/ https://www.ncbi.nlm.nih.gov/pubmed/35973722 http://dx.doi.org/10.1261/rna.079210.122 |
_version_ | 1784849235034767360 |
---|---|
author | Wegener, Melanie Dietz, Karl-Josef |
author_facet | Wegener, Melanie Dietz, Karl-Josef |
author_sort | Wegener, Melanie |
collection | PubMed |
description | About three decades ago, researchers suggested that metabolic enzymes participate in cellular processes that are unrelated to their catalytic activity, and the term “moonlighting functions” was proposed. Recently developed advanced technologies in the field of RNA interactome capture now unveil the unexpected RNA binding activity of many metabolic enzymes, as exemplified here for the enzymes of glycolysis. Although for most of these proteins a precise binding mechanism, binding conditions, and physiological relevance of the binding events still await in-depth clarification, several well explored examples demonstrate that metabolic enzymes hold crucial functions in post-transcriptional regulation of protein synthesis. This widely conserved RNA-binding function of glycolytic enzymes plays major roles in controlling cell activities. The best explored examples are glyceraldehyde 3-phosphate dehydrogenase, enolase, phosphoglycerate kinase, and pyruvate kinase. This review summarizes current knowledge about the RNA-binding activity of the ten core enzymes of glycolysis in plant, yeast, and animal cells, its regulation and physiological relevance. Apparently, a tight bidirectional regulation connects core metabolism and RNA biology, forcing us to rethink long established functional singularities. |
format | Online Article Text |
id | pubmed-9745834 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Cold Spring Harbor Laboratory Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-97458342023-01-04 The mutual interaction of glycolytic enzymes and RNA in post-transcriptional regulation Wegener, Melanie Dietz, Karl-Josef RNA Review About three decades ago, researchers suggested that metabolic enzymes participate in cellular processes that are unrelated to their catalytic activity, and the term “moonlighting functions” was proposed. Recently developed advanced technologies in the field of RNA interactome capture now unveil the unexpected RNA binding activity of many metabolic enzymes, as exemplified here for the enzymes of glycolysis. Although for most of these proteins a precise binding mechanism, binding conditions, and physiological relevance of the binding events still await in-depth clarification, several well explored examples demonstrate that metabolic enzymes hold crucial functions in post-transcriptional regulation of protein synthesis. This widely conserved RNA-binding function of glycolytic enzymes plays major roles in controlling cell activities. The best explored examples are glyceraldehyde 3-phosphate dehydrogenase, enolase, phosphoglycerate kinase, and pyruvate kinase. This review summarizes current knowledge about the RNA-binding activity of the ten core enzymes of glycolysis in plant, yeast, and animal cells, its regulation and physiological relevance. Apparently, a tight bidirectional regulation connects core metabolism and RNA biology, forcing us to rethink long established functional singularities. Cold Spring Harbor Laboratory Press 2022-11 /pmc/articles/PMC9745834/ /pubmed/35973722 http://dx.doi.org/10.1261/rna.079210.122 Text en © 2022 Wegener and Dietz; Published by Cold Spring Harbor Laboratory Press for the RNA Society https://creativecommons.org/licenses/by-nc/4.0/This article, published in RNA, is available undera Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) . |
spellingShingle | Review Wegener, Melanie Dietz, Karl-Josef The mutual interaction of glycolytic enzymes and RNA in post-transcriptional regulation |
title | The mutual interaction of glycolytic enzymes and RNA in post-transcriptional regulation |
title_full | The mutual interaction of glycolytic enzymes and RNA in post-transcriptional regulation |
title_fullStr | The mutual interaction of glycolytic enzymes and RNA in post-transcriptional regulation |
title_full_unstemmed | The mutual interaction of glycolytic enzymes and RNA in post-transcriptional regulation |
title_short | The mutual interaction of glycolytic enzymes and RNA in post-transcriptional regulation |
title_sort | mutual interaction of glycolytic enzymes and rna in post-transcriptional regulation |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9745834/ https://www.ncbi.nlm.nih.gov/pubmed/35973722 http://dx.doi.org/10.1261/rna.079210.122 |
work_keys_str_mv | AT wegenermelanie themutualinteractionofglycolyticenzymesandrnainposttranscriptionalregulation AT dietzkarljosef themutualinteractionofglycolyticenzymesandrnainposttranscriptionalregulation AT wegenermelanie mutualinteractionofglycolyticenzymesandrnainposttranscriptionalregulation AT dietzkarljosef mutualinteractionofglycolyticenzymesandrnainposttranscriptionalregulation |