APRF1 Interactome Reveals HSP90 as a New Player in the Complex That Epigenetically Regulates Flowering Time in <i>Arabidopsis thaliana</i>
WD40 repeat proteins (WDRs) are present in all eukaryotes and include members that are implicated in numerous cellular activities. They act as scaffold proteins and thus as molecular “hubs” for protein–protein interactions, which mediate the assembly of multifunctional complexes that regulate key de...
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MDPI AG
2024-01-01
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author | Ioannis Isaioglou Varvara Podia Athanassios D. Velentzas Georgios Kapolas Despoina Beris Michael Karampelias Panagiota Konstantinia Plitsi Dimitris Chatzopoulos Despina Samakovli Andreas Roussis Jasmeen Merzaban Dimitra Milioni Dimitrios J. Stravopodis Kosmas Haralampidis |
author_facet | Ioannis Isaioglou Varvara Podia Athanassios D. Velentzas Georgios Kapolas Despoina Beris Michael Karampelias Panagiota Konstantinia Plitsi Dimitris Chatzopoulos Despina Samakovli Andreas Roussis Jasmeen Merzaban Dimitra Milioni Dimitrios J. Stravopodis Kosmas Haralampidis |
author_sort | Ioannis Isaioglou |
collection | DOAJ |
description | WD40 repeat proteins (WDRs) are present in all eukaryotes and include members that are implicated in numerous cellular activities. They act as scaffold proteins and thus as molecular “hubs” for protein–protein interactions, which mediate the assembly of multifunctional complexes that regulate key developmental processes in <i>Arabidopsis thaliana</i>, such as flowering time, hormonal signaling, and stress responses. Despite their importance, many aspects of their putative functions have not been elucidated yet. Here, we show that the late-flowering phenotype of the <i>anthesis promoting factor 1</i> (<i>aprf1</i>) mutants is temperature-dependent and can be suppressed when plants are grown under mild heat stress conditions. To gain further insight into the mechanism of APRF1 function, we employed a co-immunoprecipitation (Co-IP) approach to identify its interaction partners. We provide the first interactome of APRF1, which includes proteins that are localized in several subcellular compartments and are implicated in diverse cellular functions. The dual nucleocytoplasmic localization of ARRF1, which was validated through the interaction of APRF1 with HEAT SHOCK PROTEIN 1 (HSP90.1) in the nucleus and with HSP90.2 in the cytoplasm, indicates a dynamic and versatile involvement of APRF1 in multiple biological processes. The specific interaction of APRF1 with the chaperon HSP90.1 in the nucleus expands our knowledge regarding the epigenetic regulation of flowering time in <i>A. thaliana</i> and further suggests the existence of a delicate thermoregulated mechanism during anthesis. |
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spelling | doaj.art-204ff146d1dc45c1b8ef3ca3a664c4dc2024-01-29T13:59:34ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672024-01-01252131310.3390/ijms25021313APRF1 Interactome Reveals HSP90 as a New Player in the Complex That Epigenetically Regulates Flowering Time in <i>Arabidopsis thaliana</i>Ioannis Isaioglou0Varvara Podia1Athanassios D. Velentzas2Georgios Kapolas3Despoina Beris4Michael Karampelias5Panagiota Konstantinia Plitsi6Dimitris Chatzopoulos7Despina Samakovli8Andreas Roussis9Jasmeen Merzaban10Dimitra Milioni11Dimitrios J. Stravopodis12Kosmas Haralampidis13Section of Botany, Biology Department, National and Kapodistrian University of Athens, 15772 Athens, GreeceSection of Botany, Biology Department, National and Kapodistrian University of Athens, 15772 Athens, GreeceSection of Cell Biology & Biophysics, Biology Department, National and Kapodistrian University of Athens, 15772 Athens, GreeceSection of Botany, Biology Department, National and Kapodistrian University of Athens, 15772 Athens, GreeceSection of Botany, Biology Department, National and Kapodistrian University of Athens, 15772 Athens, GreeceBioscience Program, Biological and Environmental Science and Engineering Division, King Abdullah University of Science and Technology (KAUST), Thuwal 23955, Saudi ArabiaDepartment of Agricultural Biotechnology, Agricultural University of Athens, Iera Odos 75, 11855 Athens, GreeceSection of Cell Biology & Biophysics, Biology Department, National and Kapodistrian University of Athens, 15772 Athens, GreeceSection of Botany, Biology Department, National and Kapodistrian University of Athens, 15772 Athens, GreeceSection of Botany, Biology Department, National and Kapodistrian University of Athens, 15772 Athens, GreeceBioscience Program, Biological and Environmental Science and Engineering Division, King Abdullah University of Science and Technology (KAUST), Thuwal 23955, Saudi ArabiaDepartment of Agricultural Biotechnology, Agricultural University of Athens, Iera Odos 75, 11855 Athens, GreeceSection of Cell Biology & Biophysics, Biology Department, National and Kapodistrian University of Athens, 15772 Athens, GreeceSection of Botany, Biology Department, National and Kapodistrian University of Athens, 15772 Athens, GreeceWD40 repeat proteins (WDRs) are present in all eukaryotes and include members that are implicated in numerous cellular activities. They act as scaffold proteins and thus as molecular “hubs” for protein–protein interactions, which mediate the assembly of multifunctional complexes that regulate key developmental processes in <i>Arabidopsis thaliana</i>, such as flowering time, hormonal signaling, and stress responses. Despite their importance, many aspects of their putative functions have not been elucidated yet. Here, we show that the late-flowering phenotype of the <i>anthesis promoting factor 1</i> (<i>aprf1</i>) mutants is temperature-dependent and can be suppressed when plants are grown under mild heat stress conditions. To gain further insight into the mechanism of APRF1 function, we employed a co-immunoprecipitation (Co-IP) approach to identify its interaction partners. We provide the first interactome of APRF1, which includes proteins that are localized in several subcellular compartments and are implicated in diverse cellular functions. The dual nucleocytoplasmic localization of ARRF1, which was validated through the interaction of APRF1 with HEAT SHOCK PROTEIN 1 (HSP90.1) in the nucleus and with HSP90.2 in the cytoplasm, indicates a dynamic and versatile involvement of APRF1 in multiple biological processes. The specific interaction of APRF1 with the chaperon HSP90.1 in the nucleus expands our knowledge regarding the epigenetic regulation of flowering time in <i>A. thaliana</i> and further suggests the existence of a delicate thermoregulated mechanism during anthesis.https://www.mdpi.com/1422-0067/25/2/1313ArabidopsisfloweringWD40WDRsCo-IPAPRF1 |
spellingShingle | Ioannis Isaioglou Varvara Podia Athanassios D. Velentzas Georgios Kapolas Despoina Beris Michael Karampelias Panagiota Konstantinia Plitsi Dimitris Chatzopoulos Despina Samakovli Andreas Roussis Jasmeen Merzaban Dimitra Milioni Dimitrios J. Stravopodis Kosmas Haralampidis APRF1 Interactome Reveals HSP90 as a New Player in the Complex That Epigenetically Regulates Flowering Time in <i>Arabidopsis thaliana</i> International Journal of Molecular Sciences Arabidopsis flowering WD40 WDRs Co-IP APRF1 |
title | APRF1 Interactome Reveals HSP90 as a New Player in the Complex That Epigenetically Regulates Flowering Time in <i>Arabidopsis thaliana</i> |
title_full | APRF1 Interactome Reveals HSP90 as a New Player in the Complex That Epigenetically Regulates Flowering Time in <i>Arabidopsis thaliana</i> |
title_fullStr | APRF1 Interactome Reveals HSP90 as a New Player in the Complex That Epigenetically Regulates Flowering Time in <i>Arabidopsis thaliana</i> |
title_full_unstemmed | APRF1 Interactome Reveals HSP90 as a New Player in the Complex That Epigenetically Regulates Flowering Time in <i>Arabidopsis thaliana</i> |
title_short | APRF1 Interactome Reveals HSP90 as a New Player in the Complex That Epigenetically Regulates Flowering Time in <i>Arabidopsis thaliana</i> |
title_sort | aprf1 interactome reveals hsp90 as a new player in the complex that epigenetically regulates flowering time in i arabidopsis thaliana i |
topic | Arabidopsis flowering WD40 WDRs Co-IP APRF1 |
url | https://www.mdpi.com/1422-0067/25/2/1313 |
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