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The role of hydrophobic matching on transmembrane helix packing in cells

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The role of hydrophobic matching on transmembrane helix packing in cells

dc.contributor.author	Grau, Brayan
dc.contributor.author	Javanainen, Matti
dc.contributor.author	García Murria, María Jesús
dc.contributor.author	Kulig, Waldemar
dc.contributor.author	Vattulainen, Ilpo
dc.contributor.author	Mingarro Muñoz, Ismael
dc.contributor.author	Martínez Gil, Luis
dc.date.accessioned	2018-03-06T14:32:36Z
dc.date.available	2018-03-06T14:32:36Z
dc.date.issued	2017
dc.identifier.citation	Grau, Brayan Javanainen, Matti García Murria, María Jesús Kulig, Waldemar Vattulainen, Ilpo Mingarro Muñoz, Ismael Martínez Gil, Luis 2017 The role of hydrophobic matching on transmembrane helix packing in cells Cell Stress 1 2 90 106
dc.identifier.uri	http://hdl.handle.net/10550/65272
dc.description.abstract	Folding and packing of membrane proteins are highly influenced by the lipidic component of the membrane. Here, we explore how the hydrophobic mismatch (the difference between the hydrophobic span of a transmembrane protein region and the hydrophobic thickness of the lipid membrane around the protein) influences transmembrane helix packing in a cellular environment. Using a ToxRED assay in Escherichia coli and a Bimolecular Fluorescent Complementation approach in human-derived cells complemented by atomistic molecular dynamics simulations we analyzed the dimerization of Glycophorin A derived transmembrane segments. We concluded that, biological membranes can accommodate transmembrane homo-dimers with a wide range of hydrophobic lengths. Hydrophobic mismatch and its effects on dimerization are found to be considerably weaker than those previously observed in model membranes, or under in vitro conditions, indicating that biological membranes (particularly eukaryotic membranes) can adapt to structural deformations through compensatory mechanisms that emerge from their complex structure and composition to alleviate membrane stress. Results based on atomistic simulations support this view, as they revealed that Glycophorin A dimers remain stable, despite of poor hydrophobic match, using mechanisms based on dimer tilting or local membrane thickness perturbations. Furthermore, hetero-dimers with large length disparity between their monomers are also tolerated in cells, and the conclusions that one can draw are essentially similar to those found with homo-dimers. However, large differences between transmembrane helices length hinder the monomer/dimer equilibrium, confirming that, the hydrophobic mismatch has, nonetheless, biologically relevant effects on helix packing in vivo.
dc.language.iso	eng
dc.relation.ispartof	Cell Stress, 2017, vol. 1, num. 2, p. 90-106
dc.subject	Proteïnes de membrana
dc.subject	Cèl·lules
dc.title	The role of hydrophobic matching on transmembrane helix packing in cells
dc.type	journal article	es_ES
dc.date.updated	2018-03-06T14:32:37Z
dc.identifier.doi	10.15698/cst2017.11.111
dc.identifier.idgrec	121224
dc.rights.accessRights	open access	es_ES