Lipophilicity from the modified protein, thus enhancing its membrane association. In contrast to other lipid modifications, it is reversible and may accommodate regulation by extracellular signals (Tsutsumi et al., 2008; Chini Parenti, 2009). Cycles of de- and re-acylation of peripheral membrane proteins influence their membrane-association dynamics in each mammals and yeast. For instance, Ras is subjected to a dynamic acylation pathway that mediates trafficking among Golgi and plasma membrane, as well as the correct membrane-localized functioning of a subunits of most heterotrimeric G proteins is dependent on S-acylation (Roth et al., 2006; Greaves Chamberlain, 2007). Integral membrane proteinsNew Phytologist (2013) 200: 444?55 newphytologistsuch as GPCRs, ion channels and SNARE proteins are S-acylated influencing fidelity of processing and transport to certain membranes and membrane microdomains, or altering conformation such that their activity or interaction with other proteins is modified (Resh, 2006a,b). S-acylation of cysteines in transmembrane domains (TMDs), can market lateral diffusion into thicker microdomains rich in sphingolipid and cholesterol, or can tilt the TMD. Such modifications shield or expose membrane-proximal amino acids that happen to be targets for protein rotein interaction or posttranslational modifications (Greaves Chamberlain, 2007). S-acylation is catalysed by protein S-acyl transferases (PATs) in yeast (Lobo et al., 2002; Roth et al., 2002) and in mammals (Fukata et al., 2004; Huang et al., 2004; Keller et al., 2004). PATs are integral membrane proteins with four to six TMDs along with a cytoplasmic DHHC-containing Cysteine Wealthy Domain (DHHC-CRD) which is essential for catalytic activity (Montoro et al., 2011). S-acyl transferases are encoded by a seven member gene loved ones in Saccharomyces cerevisiae, 15 predicted genes in Caenorhabditis elegans, at least 23 predicted genes in Drosophila melanogaster, mammals (Tsutsumi et al., 2008) and 24 in Arabidopsis thaliana (Batisti, 2012). As well as the DHHC c?2013 The Authors New Phytologist ?2013 New Phytologist Trust That is an open access short article under the terms in the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, supplied the original work is appropriately cited.2619509-30-5 site New Phytologistdomain some S-acyl transferases also contain a PDZ-binding motif, other people an SH3 domain, while other members include many ankyrin repeats.Methyl 5-(bromomethyl)picolinate Chemscene In plants, understanding of S-acylation is restricted.PMID:23659187 A few proteins have been shown to become S-acylated and these are involved in Ca2+ signalling, movement of potassium ions, tension signalling and pathogenesis (Hemsley Grierson, 2008; Hemsley, 2009). A proteomic method identified 500 potentially palmitoylated proteins in Arabidopsis (Hemsley et al., 2013); however, so far, only one plant S-acyl transferase has been characterized, Arabidopsis TIP1. The transcriptional null mutant alleles exhibit defects in cell size handle, pollen tube, root hair growth and cell polarity (Hemsley et al., 2005). Lately, a survey in the genomics and localization from the 24 Arabidopsis PATs described the ubiquitous expression profiles of most PATs, and their complicated targeting patterns in cellular membrane compartments which are diverse from their counterparts in yeast and mammals (Batisti, 2012). c As part of an effort to ascertain the biological functions of Arabidopsis PATs we analysed two T-DNA insertion lines (Alonso et al., 2003) of At.