title: S-acylation anchors remorin proteins to the plasma membrane but does not primarily determine their localization in membrane microdomains.
abstract: 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.
authors.affiliation: Ludwig-Maximilians-University (LMU) Munich, Institute of Genetics, 82152, Martinsried, Germany.
authors.forename: Sebastian S A
authors.initials: SS
authors.lastname: Konrad
authors.forename: Claudia
authors.initials: C
authors.lastname: Popp
authors.forename: Thomas F
authors.initials: TF
authors.lastname: Stratil
authors.forename: Iris K
authors.initials: IK
authors.lastname: Jarsch
authors.forename: Veronika
authors.initials: V
authors.lastname: Thallmair
authors.forename: Jessica
authors.initials: J
authors.lastname: Folgmann
authors.forename: Macarena
authors.initials: M
authors.lastname: Marín
authors.forename: Thomas
authors.initials: T
authors.lastname: Ott
mesh_terms: D000215:Acylation; D000595:Amino Acid Sequence; D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D003545:Cysteine / Q000378:metabolism; D021962:Membrane Microdomains / Q000378:metabolism*; D008969:Molecular Sequence Data; D009154:Mutation; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D010750:Phosphoproteins / Q000737:chemistry / Q000378:metabolism*; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism*; D021381:Protein Transport; D013261:Sterols / Q000378:metabolism; D013329:Structure-Activity Relationship; D013347:Subcellular Fractions / Q000378:metabolism
chemical_list: D002352:Carrier Proteins; D010455:Peptides; D010750:Phosphoproteins; D010940:Plant Proteins; D013261:Sterols; C103794:remorin; D003545:Cysteine
keywords: S-acylation; membrane domain; palmitoylation; protein-protein interaction; remorin