Ubiquitylation of ABA Receptors and Protein Phosphatase 2C Coreceptors to Modulate ABA Signaling and Stress Response
Post-translational modifications play a fundamental role in regulating protein function and stability. In particular, protein ubiquitylation is a multifaceted modification involved in numerous aspects of plant biology. Landmark studies connected the ATP-dependent ubiquitylation of substrates to thei...
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MDPI AG
2021-07-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/22/13/7103 |
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| author | Alberto Coego Jose Julian Jorge Lozano-Juste Gaston A. Pizzio Abdulwahed F. Alrefaei Pedro L. Rodriguez |
| author_facet | Alberto Coego Jose Julian Jorge Lozano-Juste Gaston A. Pizzio Abdulwahed F. Alrefaei Pedro L. Rodriguez |
| author_sort | Alberto Coego |
| collection | DOAJ |
| description | Post-translational modifications play a fundamental role in regulating protein function and stability. In particular, protein ubiquitylation is a multifaceted modification involved in numerous aspects of plant biology. Landmark studies connected the ATP-dependent ubiquitylation of substrates to their degradation by the 26S proteasome; however, nonproteolytic functions of the ubiquitin (Ub) code are also crucial to regulate protein interactions, activity, and localization. Regarding proteolytic functions of Ub, Lys-48-linked branched chains are the most common chain type for proteasomal degradation, whereas promotion of endocytosis and vacuolar degradation is triggered through monoubiquitylation or Lys63-linked chains introduced in integral or peripheral plasma membrane proteins. Hormone signaling relies on regulated protein turnover, and specifically the half-life of ABA signaling components is regulated both through the ubiquitin-26S proteasome system and the endocytic/vacuolar degradation pathway. E3 Ub ligases have been reported that target different ABA signaling core components, i.e., ABA receptors, PP2Cs, SnRK2s, and ABFs/ABI5 transcription factors. In this review, we focused specifically on the ubiquitylation of ABA receptors and PP2C coreceptors, as well as other post-translational modifications of ABA receptors (nitration and phosphorylation) that result in their ubiquitination and degradation. |
| first_indexed | 2024-03-10T09:51:44Z |
| format | Article |
| id | doaj.art-5eccda2ce673420ebd2424d0e53d52b1 |
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| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T09:51:44Z |
| publishDate | 2021-07-01 |
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| series | International Journal of Molecular Sciences |
| spelling | doaj.art-5eccda2ce673420ebd2424d0e53d52b12023-11-22T02:40:12ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-07-012213710310.3390/ijms22137103Ubiquitylation of ABA Receptors and Protein Phosphatase 2C Coreceptors to Modulate ABA Signaling and Stress ResponseAlberto Coego0Jose Julian1Jorge Lozano-Juste2Gaston A. Pizzio3Abdulwahed F. Alrefaei4Pedro L. Rodriguez5Instituto de Biología Molecular y Celular de Plantas, Consejo Superior de Investigaciones Científicas-Universidad Politécnica de Valencia, ES-46022 Valencia, SpainInstituto de Biología Molecular y Celular de Plantas, Consejo Superior de Investigaciones Científicas-Universidad Politécnica de Valencia, ES-46022 Valencia, SpainInstituto de Biología Molecular y Celular de Plantas, Consejo Superior de Investigaciones Científicas-Universidad Politécnica de Valencia, ES-46022 Valencia, SpainInstituto de Biología Molecular y Celular de Plantas, Consejo Superior de Investigaciones Científicas-Universidad Politécnica de Valencia, ES-46022 Valencia, SpainZoology Department, College of Science, King Saud University, Riyadh 11451, Saudi ArabiaInstituto de Biología Molecular y Celular de Plantas, Consejo Superior de Investigaciones Científicas-Universidad Politécnica de Valencia, ES-46022 Valencia, SpainPost-translational modifications play a fundamental role in regulating protein function and stability. In particular, protein ubiquitylation is a multifaceted modification involved in numerous aspects of plant biology. Landmark studies connected the ATP-dependent ubiquitylation of substrates to their degradation by the 26S proteasome; however, nonproteolytic functions of the ubiquitin (Ub) code are also crucial to regulate protein interactions, activity, and localization. Regarding proteolytic functions of Ub, Lys-48-linked branched chains are the most common chain type for proteasomal degradation, whereas promotion of endocytosis and vacuolar degradation is triggered through monoubiquitylation or Lys63-linked chains introduced in integral or peripheral plasma membrane proteins. Hormone signaling relies on regulated protein turnover, and specifically the half-life of ABA signaling components is regulated both through the ubiquitin-26S proteasome system and the endocytic/vacuolar degradation pathway. E3 Ub ligases have been reported that target different ABA signaling core components, i.e., ABA receptors, PP2Cs, SnRK2s, and ABFs/ABI5 transcription factors. In this review, we focused specifically on the ubiquitylation of ABA receptors and PP2C coreceptors, as well as other post-translational modifications of ABA receptors (nitration and phosphorylation) that result in their ubiquitination and degradation.https://www.mdpi.com/1422-0067/22/13/7103abscisic acidABA receptorclade A PP2CE3 ubiquitin ligasesPYR/PYL/RCARRBR E3 ligase |
| spellingShingle | Alberto Coego Jose Julian Jorge Lozano-Juste Gaston A. Pizzio Abdulwahed F. Alrefaei Pedro L. Rodriguez Ubiquitylation of ABA Receptors and Protein Phosphatase 2C Coreceptors to Modulate ABA Signaling and Stress Response International Journal of Molecular Sciences abscisic acid ABA receptor clade A PP2C E3 ubiquitin ligases PYR/PYL/RCAR RBR E3 ligase |
| title | Ubiquitylation of ABA Receptors and Protein Phosphatase 2C Coreceptors to Modulate ABA Signaling and Stress Response |
| title_full | Ubiquitylation of ABA Receptors and Protein Phosphatase 2C Coreceptors to Modulate ABA Signaling and Stress Response |
| title_fullStr | Ubiquitylation of ABA Receptors and Protein Phosphatase 2C Coreceptors to Modulate ABA Signaling and Stress Response |
| title_full_unstemmed | Ubiquitylation of ABA Receptors and Protein Phosphatase 2C Coreceptors to Modulate ABA Signaling and Stress Response |
| title_short | Ubiquitylation of ABA Receptors and Protein Phosphatase 2C Coreceptors to Modulate ABA Signaling and Stress Response |
| title_sort | ubiquitylation of aba receptors and protein phosphatase 2c coreceptors to modulate aba signaling and stress response |
| topic | abscisic acid ABA receptor clade A PP2C E3 ubiquitin ligases PYR/PYL/RCAR RBR E3 ligase |
| url | https://www.mdpi.com/1422-0067/22/13/7103 |
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