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Dynamic Phosphorylation of miRNA Biogenesis Factor HYL1 by MPK3 Involving Nuclear–Cytoplasmic Shuttling and Protein Stability in Arabidopsis
MicroRNAs (miRNAs) are one of the prime regulators of gene expression. The recruitment of hyponastic leaves 1 (HYL1), a double-stranded RNA binding protein also termed as DRB1, to the microprocessor complex is crucial for accurate primary-miRNA (pri-miRNA) processing and the accumulation of mature m...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8998556/ https://www.ncbi.nlm.nih.gov/pubmed/35409147 http://dx.doi.org/10.3390/ijms23073787 |
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author | Bhagat, Prakash Kumar Verma, Deepanjali Singh, Kirti Badmi, Raghuram Sharma, Deepika Sinha, Alok Krishna |
author_facet | Bhagat, Prakash Kumar Verma, Deepanjali Singh, Kirti Badmi, Raghuram Sharma, Deepika Sinha, Alok Krishna |
author_sort | Bhagat, Prakash Kumar |
collection | PubMed |
description | MicroRNAs (miRNAs) are one of the prime regulators of gene expression. The recruitment of hyponastic leaves 1 (HYL1), a double-stranded RNA binding protein also termed as DRB1, to the microprocessor complex is crucial for accurate primary-miRNA (pri-miRNA) processing and the accumulation of mature miRNA in Arabidopsis thaliana. In the present study, we investigated the role of the MAP kinase-mediated phosphorylation of AtHYL1 and its sub-cellular activity. AtMPK3 specifically phosphorylates AtHYL1 at the evolutionarily conserved serine-42 present at the N-terminal regions and plays an important role in its nuclear–cytosolic shuttling. Additionally, we identified that AtHYL1 is cleaved by trypsin-like proteases into an N-terminal fragment, which renders its subcellular activities. We, for the first time, report that the dimerization of AtHYL1 not only takes place in the nucleus, but also in the cytosol, and the C-terminal of AtHYL1 has a role in regulating its stability, as well as its subcellular localization. AtHYL1 is hyper-phosphorylated in mpk3 mutants, leading to higher stability and reduced degradation. Our data show that AtMPK3 is a negative regulator of AtHYL1 protein stability and that the AtMPK3-induced phosphorylation of AtHYL1 leads to its protein degradation. |
format | Online Article Text |
id | pubmed-8998556 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-89985562022-04-12 Dynamic Phosphorylation of miRNA Biogenesis Factor HYL1 by MPK3 Involving Nuclear–Cytoplasmic Shuttling and Protein Stability in Arabidopsis Bhagat, Prakash Kumar Verma, Deepanjali Singh, Kirti Badmi, Raghuram Sharma, Deepika Sinha, Alok Krishna Int J Mol Sci Article MicroRNAs (miRNAs) are one of the prime regulators of gene expression. The recruitment of hyponastic leaves 1 (HYL1), a double-stranded RNA binding protein also termed as DRB1, to the microprocessor complex is crucial for accurate primary-miRNA (pri-miRNA) processing and the accumulation of mature miRNA in Arabidopsis thaliana. In the present study, we investigated the role of the MAP kinase-mediated phosphorylation of AtHYL1 and its sub-cellular activity. AtMPK3 specifically phosphorylates AtHYL1 at the evolutionarily conserved serine-42 present at the N-terminal regions and plays an important role in its nuclear–cytosolic shuttling. Additionally, we identified that AtHYL1 is cleaved by trypsin-like proteases into an N-terminal fragment, which renders its subcellular activities. We, for the first time, report that the dimerization of AtHYL1 not only takes place in the nucleus, but also in the cytosol, and the C-terminal of AtHYL1 has a role in regulating its stability, as well as its subcellular localization. AtHYL1 is hyper-phosphorylated in mpk3 mutants, leading to higher stability and reduced degradation. Our data show that AtMPK3 is a negative regulator of AtHYL1 protein stability and that the AtMPK3-induced phosphorylation of AtHYL1 leads to its protein degradation. MDPI 2022-03-30 /pmc/articles/PMC8998556/ /pubmed/35409147 http://dx.doi.org/10.3390/ijms23073787 Text en © 2022 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 | Article Bhagat, Prakash Kumar Verma, Deepanjali Singh, Kirti Badmi, Raghuram Sharma, Deepika Sinha, Alok Krishna Dynamic Phosphorylation of miRNA Biogenesis Factor HYL1 by MPK3 Involving Nuclear–Cytoplasmic Shuttling and Protein Stability in Arabidopsis |
title | Dynamic Phosphorylation of miRNA Biogenesis Factor HYL1 by MPK3 Involving Nuclear–Cytoplasmic Shuttling and Protein Stability in Arabidopsis |
title_full | Dynamic Phosphorylation of miRNA Biogenesis Factor HYL1 by MPK3 Involving Nuclear–Cytoplasmic Shuttling and Protein Stability in Arabidopsis |
title_fullStr | Dynamic Phosphorylation of miRNA Biogenesis Factor HYL1 by MPK3 Involving Nuclear–Cytoplasmic Shuttling and Protein Stability in Arabidopsis |
title_full_unstemmed | Dynamic Phosphorylation of miRNA Biogenesis Factor HYL1 by MPK3 Involving Nuclear–Cytoplasmic Shuttling and Protein Stability in Arabidopsis |
title_short | Dynamic Phosphorylation of miRNA Biogenesis Factor HYL1 by MPK3 Involving Nuclear–Cytoplasmic Shuttling and Protein Stability in Arabidopsis |
title_sort | dynamic phosphorylation of mirna biogenesis factor hyl1 by mpk3 involving nuclear–cytoplasmic shuttling and protein stability in arabidopsis |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8998556/ https://www.ncbi.nlm.nih.gov/pubmed/35409147 http://dx.doi.org/10.3390/ijms23073787 |
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