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10.1126/sciadv.1700532 http://scihub22266oqcxt.onion/10.1126/sciadv.1700532 C5580885!5580885 !28879236     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28879236 &cmd=llinks): Failed to open stream: HTTP request failed! 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Cardiolipin mediates membrane and channel interactions of the mitochondrial TIM23 protein import complex receptor Tim50 |pdf=|usr=}}{{28879236 }} gab.com Text Cardiolipin mediates membrane and channel interactions of the mitochondrial TIM23 protein import complex receptor Tim50 JO: Sci Adv http://www.kidney.de/pget.php?&tw=1&pmid=28879236 #FOAvip The phospholipid cardiolipin mediates the functional interactions of proteins that reside within energy-conserving biological membranes. However, the molecular basis by which this lipid performs this essential cellular role is not well understood. We address this role of cardiolipin using the multisubunit mitochondrial TIM23 protein transport complex as a model system. The early stages of protein import by this complex require specific interactions between the polypeptide substrate receptor, Tim50, and the membrane-bound channel-forming subunit, Tim23. Using analyses performed in vivo, in isolated mitochondria, and in reductionist nanoscale model membrane systems, we show that the soluble receptor domain of Tim50 interacts with membranes and with specific sites on the Tim23 channel in a manner that is directly modulated by cardiolipin. To obtain structural insights into the nature of these interactions, we obtained the first small-angle x-ray scattering-based structure of the soluble Tim50 receptor in its entirety. Using these structural insights, molecular dynamics simulations combined with a range of biophysical measurements confirmed the role of cardiolipin in driving the association of the Tim50 receptor with lipid bilayers with concomitant structural changes, highlighting the role of key structural elements in mediating this interaction. Together, these results show that cardiolipin is required to mediate specific receptor-channel associations in the TIM23 complex. Our results support a new working model for the dynamic structural changes that occur within the complex during transport. More broadly, this work strongly advances our understanding of how cardiolipin mediates interactions among membrane-associated proteins. Twit Text FOAVip Cardiolipin mediates membrane and channel interactions of the mitochondrial TIM23 protein import complex receptor Tim50 ????Sci Adv http://www.kidney.de/pget.php?&tw=1&pmid=28879236 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28879236 #FOAvip English Wikipedia <ref>{{Cite pmid|28879236 }}</ref> Cardiolipin mediates membrane and channel interactions of the mitochondrial TIM23 protein import complex receptor Tim50 #MMPMID28879236 Malhotra K ; Modak A ; Nangia S ; Daman TH ; Gunsel U ; Robinson VL ; Mokranjac D ; May ER ; Alder NN Sci Adv 2017[Sep]; 3 (9 ): e1700532 PMID28879236 show ga The phospholipid cardiolipin mediates the functional interactions of proteins that reside within energy-conserving biological membranes. However, the molecular basis by which this lipid performs this essential cellular role is not well understood. We address this role of cardiolipin using the multisubunit mitochondrial TIM23 protein transport complex as a model system. The early stages of protein import by this complex require specific interactions between the polypeptide substrate receptor, Tim50, and the membrane-bound channel-forming subunit, Tim23. Using analyses performed in vivo, in isolated mitochondria, and in reductionist nanoscale model membrane systems, we show that the soluble receptor domain of Tim50 interacts with membranes and with specific sites on the Tim23 channel in a manner that is directly modulated by cardiolipin. To obtain structural insights into the nature of these interactions, we obtained the first small-angle x-ray scattering-based structure of the soluble Tim50 receptor in its entirety. Using these structural insights, molecular dynamics simulations combined with a range of biophysical measurements confirmed the role of cardiolipin in driving the association of the Tim50 receptor with lipid bilayers with concomitant structural changes, highlighting the role of key structural elements in mediating this interaction. Together, these results show that cardiolipin is required to mediate specific receptor-channel associations in the TIM23 complex. Our results support a new working model for the dynamic structural changes that occur within the complex during transport. More broadly, this work strongly advances our understanding of how cardiolipin mediates interactions among membrane-associated proteins. |Biological Transport [MESH] |Cardiolipins/chemistry/*metabolism [MESH] |Cell Membrane/chemistry/*metabolism [MESH] |Gene Expression [MESH] |Lipid Bilayers [MESH] |Mitochondria/*metabolism [MESH] |Mitochondrial Membrane Transport Proteins/chemistry/genetics/*metabolism [MESH] |Models, Biological [MESH] |Models, Molecular [MESH] |Protein Binding [MESH] |Protein Conformation [MESH] |Proteolysis [MESH] |Recombinant Proteins [MESH]Cardiolipin mediates membrane and channel interactions of the mitochon(epmc).pdf DeepDyve Pubget Overpricing