S-acylation anchors remorin proteins to the plasma membrane but does not primarily determine their localization in membrane microdomains
© 2014 The Authors. New Phytologist © 2014 New Phytologist Trust.
| Veröffentlicht in: | The New phytologist. - 1979. - 203(2014), 3 vom: 05. Aug., Seite 758-69 |
|---|---|
| 1. Verfasser: | |
| Weitere Verfasser: | , , , , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2014
|
| Zugriff auf das übergeordnete Werk: | The New phytologist |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't S-acylation membrane domain palmitoylation protein-protein interaction remorin Carrier Proteins Peptides Phosphoproteins mehr... |
| Zusammenfassung: | © 2014 The Authors. New Phytologist © 2014 New Phytologist Trust. 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 |
|---|---|
| Beschreibung: | Date Completed 30.03.2015 Date Revised 30.09.2020 published: Print-Electronic GENBANK: AEX20500 Citation Status MEDLINE |
| ISSN: | 1469-8137 |
| DOI: | 10.1111/nph.12867 |