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Roles of Plant Glycine-Rich RNA-Binding Proteins in Development and Stress Responses
In recent years, much progress has been made in elucidating the functional roles of plant glycine-rich RNA-binding proteins (GR-RBPs) during development and stress responses. Canonical GR-RBPs contain an RNA recognition motif (RRM) or a cold-shock domain (CSD) at the N-terminus and a glycine-rich do...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8198583/ https://www.ncbi.nlm.nih.gov/pubmed/34072567 http://dx.doi.org/10.3390/ijms22115849 |
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author | Ma, Liqun Cheng, Ke Li, Jinyan Deng, Zhiqi Zhang, Chunjiao Zhu, Hongliang |
author_facet | Ma, Liqun Cheng, Ke Li, Jinyan Deng, Zhiqi Zhang, Chunjiao Zhu, Hongliang |
author_sort | Ma, Liqun |
collection | PubMed |
description | In recent years, much progress has been made in elucidating the functional roles of plant glycine-rich RNA-binding proteins (GR-RBPs) during development and stress responses. Canonical GR-RBPs contain an RNA recognition motif (RRM) or a cold-shock domain (CSD) at the N-terminus and a glycine-rich domain at the C-terminus, which have been associated with several different RNA processes, such as alternative splicing, mRNA export and RNA editing. However, many aspects of GR-RBP function, the targeting of their RNAs, interacting proteins and the consequences of the RNA target process are not well understood. Here, we discuss recent findings in the field, newly defined roles for GR-RBPs and the actions of GR-RBPs on target RNA metabolism. |
format | Online Article Text |
id | pubmed-8198583 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-81985832021-06-14 Roles of Plant Glycine-Rich RNA-Binding Proteins in Development and Stress Responses Ma, Liqun Cheng, Ke Li, Jinyan Deng, Zhiqi Zhang, Chunjiao Zhu, Hongliang Int J Mol Sci Review In recent years, much progress has been made in elucidating the functional roles of plant glycine-rich RNA-binding proteins (GR-RBPs) during development and stress responses. Canonical GR-RBPs contain an RNA recognition motif (RRM) or a cold-shock domain (CSD) at the N-terminus and a glycine-rich domain at the C-terminus, which have been associated with several different RNA processes, such as alternative splicing, mRNA export and RNA editing. However, many aspects of GR-RBP function, the targeting of their RNAs, interacting proteins and the consequences of the RNA target process are not well understood. Here, we discuss recent findings in the field, newly defined roles for GR-RBPs and the actions of GR-RBPs on target RNA metabolism. MDPI 2021-05-29 /pmc/articles/PMC8198583/ /pubmed/34072567 http://dx.doi.org/10.3390/ijms22115849 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Ma, Liqun Cheng, Ke Li, Jinyan Deng, Zhiqi Zhang, Chunjiao Zhu, Hongliang Roles of Plant Glycine-Rich RNA-Binding Proteins in Development and Stress Responses |
title | Roles of Plant Glycine-Rich RNA-Binding Proteins in Development and Stress Responses |
title_full | Roles of Plant Glycine-Rich RNA-Binding Proteins in Development and Stress Responses |
title_fullStr | Roles of Plant Glycine-Rich RNA-Binding Proteins in Development and Stress Responses |
title_full_unstemmed | Roles of Plant Glycine-Rich RNA-Binding Proteins in Development and Stress Responses |
title_short | Roles of Plant Glycine-Rich RNA-Binding Proteins in Development and Stress Responses |
title_sort | roles of plant glycine-rich rna-binding proteins in development and stress responses |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8198583/ https://www.ncbi.nlm.nih.gov/pubmed/34072567 http://dx.doi.org/10.3390/ijms22115849 |
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