Differential Role of Threonine and Tyrosine Phosphorylation in the Activation and Activity of the Yeast MAPK Slt2

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dc.contributor.authorGonzález Rubio, Gema
dc.contributor.authorSellers Moya, Ángela
dc.contributor.authorMartín Brieva, Humberto
dc.contributor.authorMolina Martín, María
dc.date.accessioned2023-06-17T08:25:05Z
dc.date.available2023-06-17T08:25:05Z
dc.date.issued2021-01-23
dc.description.abstractThe Mitogen-Activated Protein Kinase (MAPK) Slt2 is central to signaling through the yeast Cell Wall Integrity (CWI) pathway. MAPKs are regulated by phosphorylation at both the threonine and tyrosine of the conserved TXY motif within the activation loop (T190/Y192 in Slt2). Since phosphorylation at both sites results in the full activation of MAPKs, signaling through MAPK pathways is monitored with antibodies that detect dually phosphorylated forms. However, most of these antibodies also recognize monophosphorylated species, whose relative abundance and functionality are diverse. By using different phosphospecific antibodies and phosphate-affinity (Phostag) analysis on distinct Slt2 mutants, we determined that Y192- and T190-monophosphorylated species coexist with biphosphorylated Slt2, although most of the Slt2 pool remains unphosphorylated following stress. Among the monophosphorylated forms, only T190 exhibited biological activity. Upon stimulation, Slt2 is first phosphorylated at Y192, mainly by the MAPKK Mkk1, and this phosphorylation is important for the subsequent T190 phosphorylation. Similarly, dephosphorylation of Slt2 by the Dual Specificity Phosphatase (DSP) Msg5 is ordered, with dephosphorylation of T190 depending on previous Y192 dephosphorylation. Whereas Y192 phosphorylation enhances the Slt2 catalytic activity, T190 is essential for this activity. The conserved T195 residue is also critical for Slt2 functionality. Mutations that abolish the activity of Slt2 result in a high increase in inactive Y192- monophosphorylated Slt2. The coexistence of different Slt2 phosphoforms with diverse biological significance highlights the importance of the precise detection of the Slt2 phosphorylation status.
dc.description.departmentDepto. de Microbiología y Parasitología
dc.description.facultyFac. de Farmacia
dc.description.refereedTRUE
dc.description.sponsorshipMinisterio de Economía y Competitividad (MINECO)
dc.description.sponsorshipMinisterio de Ciencia e Innovación (MICINN)
dc.description.sponsorshipComunidad de Madrid/ FEDER
dc.description.statuspub
dc.eprint.idhttps://eprints.ucm.es/id/eprint/71620
dc.identifier.doi10.3390/ijms22031110
dc.identifier.issn1422-0067
dc.identifier.officialurlhttps://doi.org/10.3390/ijms22031110
dc.identifier.urihttps://hdl.handle.net/20.500.14352/7041
dc.issue.number3
dc.journal.titleInternational Journal of Molecular Sciences
dc.language.isoeng
dc.page.initial1110
dc.publisherMDPI
dc.relation.projectIDBIO2016-75030-P
dc.relation.projectIDPID2019- 105342GB-I00
dc.relation.projectIDInGEMICS-CM (S2017/BMD-3691)
dc.rightsAtribución 3.0 España
dc.rights.accessRightsopen access
dc.rights.urihttps://creativecommons.org/licenses/by/3.0/es/
dc.subject.keywordcell wall integrity
dc.subject.keywordMAPKs
dc.subject.keywordsignaling
dc.subject.keywordSlt2
dc.subject.keywordMsg5
dc.subject.keywordphosphorylation
dc.subject.keywordmonophosphorylation
dc.subject.keywordPhos-tag
dc.subject.ucmBioquímica (Farmacia)
dc.subject.ucmMicrobiología (Farmacia)
dc.subject.unesco3302.03 Microbiología Industrial
dc.titleDifferential Role of Threonine and Tyrosine Phosphorylation in the Activation and Activity of the Yeast MAPK Slt2
dc.typejournal article
dc.volume.number22
dspace.entity.typePublication
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relation.isAuthorOfPublicationdf46f90d-579d-48d9-8a2f-f299a317eba2
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relation.isAuthorOfPublication.latestForDiscoveryd9e92796-62d5-4566-8a17-e2357c7ec32a
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