Show simple item record

Files in this item


Item metadata

dc.contributor.authorHurst, Charlotte H.
dc.contributor.authorWright, Kathryn M.
dc.contributor.authorTurnbull, Dionne
dc.contributor.authorLeslie, Kerry
dc.contributor.authorJones, Susan
dc.contributor.authorHemsley, Piers A.
dc.identifier.citationHurst , C H , Wright , K M , Turnbull , D , Leslie , K , Jones , S & Hemsley , P A 2019 , ' Juxta-membrane S-acylation of plant receptor-like kinases is likely fortuitous and does not necessarily impact upon function ' , Scientific Reports , vol. 9 , 12818 .
dc.identifier.otherPURE: 261267721
dc.identifier.otherPURE UUID: 07d43d85-1c28-4d5b-8f5d-65380e86e849
dc.identifier.otherScopus: 85071896242
dc.identifier.otherPubMed: 31492958
dc.identifier.otherWOS: 000484656700006
dc.descriptionThis work was funded by UK Biotechnology and Biological Sciences Research Council Grants BB/M024911/1 and BB/M010996/1 to P.A.H.en
dc.description.abstractS-acylation is a common post-translational modification of membrane protein cysteine residues with many regulatory roles. S-acylation adjacent to transmembrane domains has been described in the literature as affecting diverse protein properties including turnover, trafficking and microdomain partitioning. However, all of these data are derived from mammalian and yeast systems. Here we examine the role of S-acylation adjacent to the transmembrane domain of the plant pathogen perceiving receptor-like kinase FLS2. Surprisingly, S-acylation of FLS2 adjacent to the transmembrane domain is not required for either FLS2 trafficking or signalling function. Expanding this analysis to the wider plant receptor-like kinase family we find that S-acylation adjacent to receptor-like kinase domains is common, affecting ~25% of Arabidopsis receptor-like kinases, but poorly conserved between orthologues through evolution. This suggests that S-acylation of receptor-like kinases at this site is likely the result of chance mutation leading to cysteine occurrence. As transmembrane domains followed by cysteine residues are common motifs for S-acylation to occur, and many S-acyl transferases appear to have lax substrate specificity, we propose that many receptor-like kinases are fortuitously S-acylated once chance mutation has introduced a cysteine at this site. Interestingly some receptor-like kinases show conservation of S-acylation sites between orthologues suggesting that S-acylation has come to play a role and has been positively selected for during evolution. The most notable example of this is in the ERECTA-like family where S-acylation of ERECTA adjacent to the transmembrane domain occurs in all ERECTA orthologues but not in the parental ERECTA-like clade. This suggests that ERECTA S-acylation occurred when ERECTA emerged during the evolution of angiosperms and may have contributed to the neo-functionalisation of ERECTA from ERECTA-like proteins.
dc.relation.ispartofScientific Reportsen
dc.rightsCopyright © The Author(s) 2019. Open Access. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit
dc.subjectQH301 Biologyen
dc.subjectSB Plant cultureen
dc.titleJuxta-membrane S-acylation of plant receptor-like kinases is likely fortuitous and does not necessarily impact upon functionen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.description.statusPeer revieweden

This item appears in the following Collection(s)

Show simple item record