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231224s2014 xx |||||o 00| ||eng c |
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|a 10.1111/nph.12867
|2 doi
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|a pubmed24n0796.xml
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|a (DE-627)NLM238882519
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|a (NLM)24897938
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Konrad, Sebastian S A
|e verfasserin
|4 aut
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|a S-acylation anchors remorin proteins to the plasma membrane but does not primarily determine their localization in membrane microdomains
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|c 2014
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 30.03.2015
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|a Date Revised 30.09.2020
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|a published: Print-Electronic
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|a GENBANK: AEX20500
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|a Citation Status MEDLINE
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|a © 2014 The Authors. New Phytologist © 2014 New Phytologist Trust.
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|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
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a S-acylation
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|a membrane domain
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|a palmitoylation
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|a protein-protein interaction
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|a remorin
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|a Carrier Proteins
|2 NLM
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|a Peptides
|2 NLM
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|a Phosphoproteins
|2 NLM
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|a Plant Proteins
|2 NLM
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|a Sterols
|2 NLM
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|a remorin
|2 NLM
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|a Cysteine
|2 NLM
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|a K848JZ4886
|2 NLM
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1 |
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|a Popp, Claudia
|e verfasserin
|4 aut
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|a Stratil, Thomas F
|e verfasserin
|4 aut
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|a Jarsch, Iris K
|e verfasserin
|4 aut
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|a Thallmair, Veronika
|e verfasserin
|4 aut
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|a Folgmann, Jessica
|e verfasserin
|4 aut
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|a Marín, Macarena
|e verfasserin
|4 aut
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|a Ott, Thomas
|e verfasserin
|4 aut
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|i Enthalten in
|t The New phytologist
|d 1979
|g 203(2014), 3 vom: 05. Aug., Seite 758-69
|w (DE-627)NLM09818248X
|x 1469-8137
|7 nnns
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|g volume:203
|g year:2014
|g number:3
|g day:05
|g month:08
|g pages:758-69
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|u http://dx.doi.org/10.1111/nph.12867
|3 Volltext
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|a GBV_ILN_350
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|a AR
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|d 203
|j 2014
|e 3
|b 05
|c 08
|h 758-69
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