S‐acylation anchors remorin proteins to the plasma membrane but does not primarily determine their localization in membrane microdomains
| العنوان: | S‐acylation anchors remorin proteins to the plasma membrane but does not primarily determine their localization in membrane microdomains |
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| المؤلفون: | Sebastian S. A. Konrad, Thomas Ott, Jessica Folgmann, Veronika Thallmair, Iris K. Jarsch, Macarena Marín, Thomas F. Stratil, Claudia Popp |
| المصدر: | New Phytologist. 203:758-769 |
| بيانات النشر: | Wiley, 2014. |
| سنة النشر: | 2014 |
| مصطلحات موضوعية: | Physiology, Acylation, Molecular Sequence Data, Plant Science, Biology, Structure-Activity Relationship, Membrane Microdomains, Amino Acid Sequence, Cysteine, Protein–lipid interaction, Integral membrane protein, Plant Proteins, Binding Sites, FERM domain, Peripheral membrane protein, S-acylation, Membrane transport, Phosphoproteins, Cell biology, Protein Transport, Sterols, Membrane protein, Mutation, Translocase of the inner membrane, lipids (amino acids, peptides, and proteins), Carrier Proteins, Peptides, Subcellular Fractions |
| الوصف: | 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. |
| تدمد: | 1469-8137 0028-646X |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d198bddfcdf7b013093a9fb34af65027Test https://doi.org/10.1111/nph.12867Test |
| حقوق: | CLOSED |
| رقم الانضمام: | edsair.doi.dedup.....d198bddfcdf7b013093a9fb34af65027 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14698137 0028646X |
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