Plant PP2A: A Versatile Enzyme with Key Physiological Functions
Protein phosphatase 2A (PP2A) is a highly conserved heterotrimeric enzyme complex present in all eukaryotic cells, consisting of a scaffolding A subunit, a catalytic C subunit, and a regulatory B subunit. The A and C subunits form the core enzyme, which interacts with the B subunit to determine the...
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MDPI AG
2025-03-01
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| Series: | Kinases and Phosphatases |
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| Online Access: | https://www.mdpi.com/2813-3757/3/1/5 |
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| author | Juan I. Cortelezzi Martina Zubillaga Victoria R. Scardino María N. Muñiz García Daniela A. Capiati |
| author_facet | Juan I. Cortelezzi Martina Zubillaga Victoria R. Scardino María N. Muñiz García Daniela A. Capiati |
| author_sort | Juan I. Cortelezzi |
| collection | DOAJ |
| description | Protein phosphatase 2A (PP2A) is a highly conserved heterotrimeric enzyme complex present in all eukaryotic cells, consisting of a scaffolding A subunit, a catalytic C subunit, and a regulatory B subunit. The A and C subunits form the core enzyme, which interacts with the B subunit to determine the substrate specificity, subcellular localization, and enzymatic activity of the holoenzyme. The <i>Arabidopsis thaliana</i> genome encodes five C subunits, three A subunits, and 17 B subunits, enabling the formation of diverse holoenzymes with extensive functional versatility. Genetic evidence highlights the essential role of PP2A in regulating various physiological processes in plants, including responses to abiotic and biotic stresses and developmental programs. Notably, PP2A can act as both a positive and negative regulator within the same pathway, while individual subunits often participate in multiple processes. This functional diversity arises from the structural flexibility of PP2A. This review examines the structural diversity of plant PP2A and its regulatory roles across diverse physiological contexts. |
| format | Article |
| id | doaj-art-c14a3c6752c24db2a8a0e4305053e51f |
| institution | Kabale University |
| issn | 2813-3757 |
| language | English |
| publishDate | 2025-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Kinases and Phosphatases |
| spelling | doaj-art-c14a3c6752c24db2a8a0e4305053e51f2025-08-20T03:43:31ZengMDPI AGKinases and Phosphatases2813-37572025-03-0131510.3390/kinasesphosphatases3010005Plant PP2A: A Versatile Enzyme with Key Physiological FunctionsJuan I. Cortelezzi0Martina Zubillaga1Victoria R. Scardino2María N. Muñiz García3Daniela A. Capiati4Instituto de Investigaciones en Ingeniería Genética y Biología Molecular “Dr. Héctor Torres” (INGEBI), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Vuelta de Obligado 2490, Cuidad de Buenos Aires C1428ADN, ArgentinaInstituto de Investigaciones en Ingeniería Genética y Biología Molecular “Dr. Héctor Torres” (INGEBI), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Vuelta de Obligado 2490, Cuidad de Buenos Aires C1428ADN, ArgentinaInstituto de Investigaciones en Ingeniería Genética y Biología Molecular “Dr. Héctor Torres” (INGEBI), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Vuelta de Obligado 2490, Cuidad de Buenos Aires C1428ADN, ArgentinaInstituto de Investigaciones en Ingeniería Genética y Biología Molecular “Dr. Héctor Torres” (INGEBI), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Vuelta de Obligado 2490, Cuidad de Buenos Aires C1428ADN, ArgentinaInstituto de Investigaciones en Ingeniería Genética y Biología Molecular “Dr. Héctor Torres” (INGEBI), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Vuelta de Obligado 2490, Cuidad de Buenos Aires C1428ADN, ArgentinaProtein phosphatase 2A (PP2A) is a highly conserved heterotrimeric enzyme complex present in all eukaryotic cells, consisting of a scaffolding A subunit, a catalytic C subunit, and a regulatory B subunit. The A and C subunits form the core enzyme, which interacts with the B subunit to determine the substrate specificity, subcellular localization, and enzymatic activity of the holoenzyme. The <i>Arabidopsis thaliana</i> genome encodes five C subunits, three A subunits, and 17 B subunits, enabling the formation of diverse holoenzymes with extensive functional versatility. Genetic evidence highlights the essential role of PP2A in regulating various physiological processes in plants, including responses to abiotic and biotic stresses and developmental programs. Notably, PP2A can act as both a positive and negative regulator within the same pathway, while individual subunits often participate in multiple processes. This functional diversity arises from the structural flexibility of PP2A. This review examines the structural diversity of plant PP2A and its regulatory roles across diverse physiological contexts.https://www.mdpi.com/2813-3757/3/1/5abiotic stressbiotic stressdevelopmentphosphataseplant PP2A |
| spellingShingle | Juan I. Cortelezzi Martina Zubillaga Victoria R. Scardino María N. Muñiz García Daniela A. Capiati Plant PP2A: A Versatile Enzyme with Key Physiological Functions Kinases and Phosphatases abiotic stress biotic stress development phosphatase plant PP2A |
| title | Plant PP2A: A Versatile Enzyme with Key Physiological Functions |
| title_full | Plant PP2A: A Versatile Enzyme with Key Physiological Functions |
| title_fullStr | Plant PP2A: A Versatile Enzyme with Key Physiological Functions |
| title_full_unstemmed | Plant PP2A: A Versatile Enzyme with Key Physiological Functions |
| title_short | Plant PP2A: A Versatile Enzyme with Key Physiological Functions |
| title_sort | plant pp2a a versatile enzyme with key physiological functions |
| topic | abiotic stress biotic stress development phosphatase plant PP2A |
| url | https://www.mdpi.com/2813-3757/3/1/5 |
| work_keys_str_mv | AT juanicortelezzi plantpp2aaversatileenzymewithkeyphysiologicalfunctions AT martinazubillaga plantpp2aaversatileenzymewithkeyphysiologicalfunctions AT victoriarscardino plantpp2aaversatileenzymewithkeyphysiologicalfunctions AT marianmunizgarcia plantpp2aaversatileenzymewithkeyphysiologicalfunctions AT danielaacapiati plantpp2aaversatileenzymewithkeyphysiologicalfunctions |