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ABA inhibits myristoylation and induces shuttling of the RGLG1 E3 ligase to promote nuclear degradation of PP2CA

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ABA inhibits myristoylation and induces shuttling of the RGLG1 E3 ligase to promote nuclear degradation of PP2CA

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dc.contributor.author Belda Palazón, Borja es_ES
dc.contributor.author Julian, Jose es_ES
dc.contributor.author Coego, Alberto es_ES
dc.contributor.author Wu, Qian es_ES
dc.contributor.author Zhang, Xu es_ES
dc.contributor.author Batistic, Oliver es_ES
dc.contributor.author Alquraishi, Saleh A. es_ES
dc.contributor.author Kudla, Joerg es_ES
dc.contributor.author An, Chengcai es_ES
dc.contributor.author Rodríguez Egea, Pedro Luís es_ES
dc.date.accessioned 2021-02-03T04:33:41Z
dc.date.available 2021-02-03T04:33:41Z
dc.date.issued 2019-06 es_ES
dc.identifier.issn 0960-7412 es_ES
dc.identifier.uri http://hdl.handle.net/10251/160599
dc.description.abstract [EN] Hormone- and stress-induced shuttling of signaling or regulatory proteins is an important cellular mechanism to modulate hormone signaling and cope with abiotic stress. Hormone-induced ubiquitination plays a crucial role to determine half-life of key negative regulators of hormone signaling. For ABA signaling, degradation of clade A PP2Cs, such as PP2CA or ABI1, is a complementary mechanism to PYR/PYL/RCAR-mediated inhibition of PP2C activity. ABA promotes the degradation of PP2CA through the RGLG1 E3 ligase, although it is not known how ABA enhances the interaction of RGLG1 with PP2CA given they are predominantly found in plasma membrane and nucleus, respectively. We demonstrate that ABA modifies the subcellular localization of RGLG1 and promotes nuclear interaction with PP2CA. We found RGLG1 is myristoylated in vivo, which facilitates its attachment to plasma membrane. ABA inhibits myristoylation of RGLG1 through downregulation of Nmyristoyltransferase1 (NMT1) and promotes nuclear translocation of RGLG1 in a cycloheximide-insensitive manner. Enhanced nuclear recruitment of the E3 ligase was also promoted by increasing PP2CA protein levels and the formation of RGLG1-receptor-phosphatase complexes. We show that RGLG1Gly2Ala -mutated in the Nterminal myristoylation site- shows constitutive nuclear localization and causes enhanced response to ABA and salt/osmotic stress. RGLG1/5 can interact with certain monomeric ABA receptors, which facilitates the formation of nuclear complexes such as RGLG1-PP2CA-PYL8. In summary, we provide evidence that an E3 ligase can dynamically re-localize in response to both ABA and increased levels of its target, which reveals a mechanism to explain how ABA enhances RGLG1-PP2CA interaction and hence PP2CA degradation. es_ES
dc.description.sponsorship Work in P.L.R.'s laboratory was supported by the Ministerio de Ciencia e Innovacion, Fondo Europeo de Desarrollo Regional and Consejo Superior de Investigaciones Cientificas through grants BIO2014-52537-R and BIO2017-82503-R. This work was also funded by grants from the Deutsche Forschungsgemeinschaft (DFG) Ku931/4-1 to J. K., and BA4742/1-2 to O.B. B.B. was funded by Programa VALi+ d GVA APOSTD/2017/039. J.J. was supported by an FPI contract from MINECO es_ES
dc.language Inglés es_ES
dc.publisher Blackwell Publishing es_ES
dc.relation.ispartof The Plant Journal es_ES
dc.rights Reserva de todos los derechos es_ES
dc.subject ABA signaling es_ES
dc.subject RGLG1 es_ES
dc.subject E3 ligase es_ES
dc.subject PP2C es_ES
dc.subject Ubiquitination es_ES
dc.subject Myristoylation es_ES
dc.subject Shuttling es_ES
dc.subject Arabidopsis thaliana es_ES
dc.subject.classification BIOQUIMICA Y BIOLOGIA MOLECULAR es_ES
dc.title ABA inhibits myristoylation and induces shuttling of the RGLG1 E3 ligase to promote nuclear degradation of PP2CA es_ES
dc.type Artículo es_ES
dc.identifier.doi 10.1111/tpj.14274 es_ES
dc.relation.projectID info:eu-repo/grantAgreement/MINECO//BIO2014-52537-R/ES/REGULACION DE LA SEÑALIZACION DEL ABA MEDIANTE MECHANISMOS QUE AFECTAN LOCALIZACION SUBCELULAR, VIDA MEDIA Y ACTIVIDAD DE RECEPTORES PARA REFORZAR TOLERANCIA VEGETAL A SEQUIA/ es_ES
dc.relation.projectID info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BIO2017-82503-R/ES/REGULACION DE LA SEÑALIZACION DEL ABA Y TOLERANCIA A SEQUIA MEDIANTE E3 UBIQUITIN LIGASAS QUE REGULAN EL RECAMBIO DE RECEPTORES Y FOSFATASAS 2C/ es_ES
dc.relation.projectID info:eu-repo/grantAgreement/GVA//APOSTD%2F2017%2F039/ es_ES
dc.relation.projectID info:eu-repo/grantAgreement/DFG//Ku931%2F4-1/ es_ES
dc.relation.projectID info:eu-repo/grantAgreement/DFG//BA4742%2F1-2/ es_ES
dc.rights.accessRights Abierto es_ES
dc.contributor.affiliation Universitat Politècnica de València. Instituto Universitario Mixto de Biología Molecular y Celular de Plantas - Institut Universitari Mixt de Biologia Molecular i Cel·lular de Plantes es_ES
dc.description.bibliographicCitation Belda Palazón, B.; Julian, J.; Coego, A.; Wu, Q.; Zhang, X.; Batistic, O.; Alquraishi, SA.... (2019). ABA inhibits myristoylation and induces shuttling of the RGLG1 E3 ligase to promote nuclear degradation of PP2CA. The Plant Journal. 98(5):813-825. https://doi.org/10.1111/tpj.14274 es_ES
dc.description.accrualMethod S es_ES
dc.relation.publisherversion https://doi.org/10.1111/tpj.14274 es_ES
dc.description.upvformatpinicio 813 es_ES
dc.description.upvformatpfin 825 es_ES
dc.type.version info:eu-repo/semantics/publishedVersion es_ES
dc.description.volume 98 es_ES
dc.description.issue 5 es_ES
dc.identifier.pmid 30730075 es_ES
dc.relation.pasarela S\377948 es_ES
dc.contributor.funder Ministerio de Economía y Competitividad es_ES
dc.contributor.funder Generalitat Valenciana es_ES
dc.contributor.funder Deutsche Forschungsgemeinschaft es_ES
dc.contributor.funder European Regional Development Fund es_ES
dc.contributor.funder Consejo Superior de Investigaciones Científicas es_ES
dc.contributor.funder Agencia Estatal de Investigación es_ES
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