S‐acylation anchors remorin proteins to the plasma membrane but does not primarily determine their localization in membrane microdomains

Abstract

Summary Remorins are well‐established marker proteins for plasma membrane microdomains. They specifically localize to the inner membrane leaflet despite an overall hydrophilic amino acid composition. Here, we determined amino acids and post‐translational lipidations that are required for membrane association of remorin proteins. We used a combination of cell biological and biochemical approaches to localize remorin proteins and truncated variants of those in living cells and determined S‐acylation on defined residues in these proteins. S‐acylation of cysteine residues in a C‐terminal hydrophobic core contributes to membrane association of most remorin proteins. While S‐acylation patterns differ between members of this multi‐gene family, initial membrane association is mediated by protein–protein or protein–lipid interactions. However, S‐acylation is not a key determinant for the localization of remorins in membrane microdomains. Although remorins bind via a conserved mechanism to the plasma membrane, other membrane‐resident proteins may be involved in the recruitment of remorins into membrane domains. S‐acylation probably occurs after an initial targeting of the proteins to the plasma membrane and locks remorins in this compartment. As S‐acylation is a reversible post‐translational modification, stimulus‐dependent intracellular trafficking of these proteins can be envisioned.

Plant immune and growth receptors share common signalling components but localise to distinct plasma membrane nanodomains

“…The study of Jarsch et al (2014), which described various different localisation patterns for the REM protein family in plant PMs, revealed that the clusters of these PM-associated proteins also hardly undergo lateral movements. Since REMs bind to the inner leaflet of PMs (Konrad et al, 2014) and therefore cannot directly interact with the extracellular cell wall, a restrictive influence of the cortical cytoskeleton on the lateral PM mobility should not be excluded.…”

Male–female communication triggers calcium signatures during fertilization in Arabidopsis

“…A C-terminal 109 nucleotide sequence of MtSYMREM1 (ref. 66), covering the C-terminal remorin anchor, was amplified from pDONR207-MtSYMREM1 with the primers FV03 (5′-GGG GAATTC TGGGGAAGAAATCCTCAAGGTAGAG-3′) and FV04 (5′-CCCC GGATCC CTAACTGAAAAACCTTAAACCGCTG-3′). The resulting PCR product was cloned into pENTR-tagRFP-T using the introduced EcoRI and BamHI restriction sites (underlined) to obtain pENTR-tagRFP-T-REM.…”

Progress toward Understanding Protein S-acylation: Prospective in Plants

“…Although, individual knockout mutant of LIP1 and LIP2 did not have any defects the double mutant can cause sterility due to loss of pollen tube guidance (Liu et al, 2013). S-acylation of remorin proteins, a group of well-known plasma membrane marker proteins, contribute to their subcellular localization (Konrad et al, 2014). Very recently, Kumar and his coworkers confirmed that a number of the catalytic subunits of cellulose synthase complex (CSC) in Arabidopsis are S-acylated.…”