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10.1038/ncomms9728 http://scihub22266oqcxt.onion/10.1038/ncomms9728 C4632190!4632190!26522943     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2015 ; 6 (ä): ä Nephropedia Template TP {{tp|p=26522943|t=2015. Transmembrane protein sorting driven by membrane curvature |pdf=|usr=}}{{26522943}} gab.com Text Transmembrane protein sorting driven by membrane curvature JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=26522943 #FOAvip The intricate structure of prokaryotic and eukaryotic cells depends on the ability to target proteins to specific cellular locations. In most cases, we have a poor understanding of the underlying mechanisms. A typical example is the assembly of bacterial chemoreceptors at cell poles. Here we show that the classical chemoreceptor TlpA of Bacillus subtilis does not localize according to the consensus stochastic nucleation mechanism but accumulates at strongly curved membrane areas generated during cell division. This preference was confirmed by accumulation at non-septal curved membranes. Localization appears to be an intrinsic property of the protein complex and does not rely on chemoreceptor clustering, as was previously shown for Escherichia coli. By constructing specific amino-acid substitutions, we demonstrate that the preference for strongly curved membranes arises from the curved shape of chemoreceptor trimer of dimers. These findings demonstrate that the intrinsic shape of transmembrane proteins can determine their cellular localization. Twit Text FOAVip Transmembrane protein sorting driven by membrane curvature ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=26522943 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26522943 #FOAvip English Wikipedia <ref>{{Cite pmid|26522943}}</ref> Transmembrane protein sorting driven by membrane curvature #MMPMID26522943 Strahl H; Ronneau S; González BS; Klutsch D; Schaffner-Barbero C; Hamoen LW Nat Commun 2015[]; 6 (ä): ä PMID26522943show ga The intricate structure of prokaryotic and eukaryotic cells depends on the ability to target proteins to specific cellular locations. In most cases, we have a poor understanding of the underlying mechanisms. A typical example is the assembly of bacterial chemoreceptors at cell poles. Here we show that the classical chemoreceptor TlpA of Bacillus subtilis does not localize according to the consensus stochastic nucleation mechanism but accumulates at strongly curved membrane areas generated during cell division. This preference was confirmed by accumulation at non-septal curved membranes. Localization appears to be an intrinsic property of the protein complex and does not rely on chemoreceptor clustering, as was previously shown for Escherichia coli. By constructing specific amino-acid substitutions, we demonstrate that the preference for strongly curved membranes arises from the curved shape of chemoreceptor trimer of dimers. These findings demonstrate that the intrinsic shape of transmembrane proteins can determine their cellular localization. äTransmembrane protein sorting driven by membrane curvature (epmc).pdf DeepDyve Pubget Overpricing