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.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 203(2014), 3 vom: 05. Aug., Seite 758-69
1. Verfasser: Konrad, Sebastian S A (VerfasserIn)
Weitere Verfasser: Popp, Claudia, Stratil, Thomas F, Jarsch, Iris K, Thallmair, Veronika, Folgmann, Jessica, Marín, Macarena, Ott, Thomas
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... Plant Proteins Sterols Cysteine K848JZ4886
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245 1 0 |a S-acylation anchors remorin proteins to the plasma membrane but does not primarily determine their localization in membrane microdomains 
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520 |a 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 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a S-acylation 
650 4 |a membrane domain 
650 4 |a palmitoylation 
650 4 |a protein-protein interaction 
650 4 |a remorin 
650 7 |a Carrier Proteins  |2 NLM 
650 7 |a Peptides  |2 NLM 
650 7 |a Phosphoproteins  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Sterols  |2 NLM 
650 7 |a remorin  |2 NLM 
650 7 |a Cysteine  |2 NLM 
650 7 |a K848JZ4886  |2 NLM 
700 1 |a Popp, Claudia  |e verfasserin  |4 aut 
700 1 |a Stratil, Thomas F  |e verfasserin  |4 aut 
700 1 |a Jarsch, Iris K  |e verfasserin  |4 aut 
700 1 |a Thallmair, Veronika  |e verfasserin  |4 aut 
700 1 |a Folgmann, Jessica  |e verfasserin  |4 aut 
700 1 |a Marín, Macarena  |e verfasserin  |4 aut 
700 1 |a Ott, Thomas  |e verfasserin  |4 aut 
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773 1 8 |g volume:203  |g year:2014  |g number:3  |g day:05  |g month:08  |g pages:758-69 
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