Juxta-membrane S-acylation of plant receptor-like kinases is likely fortuitous and does not necessarily impact upon function.

ABSTRACT: S-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 comm

SUBMITTER: Hurst CH 

PROVIDER: S-EPMC6731221 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature