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Regulation of membrane protein structure and function by their lipid nano-environment

Nature reviews. Molecular cell biology, 2023-02, Vol.24 (2), p.107-122 [Peer Reviewed Journal]

2022. Springer Nature Limited. ;Springer Nature Limited 2022. corrected publication 2022. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. ;ISSN: 1471-0072 ;EISSN: 1471-0080 ;DOI: 10.1038/s41580-022-00524-4 ;PMID: 36056103

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  • Title:
    Regulation of membrane protein structure and function by their lipid nano-environment
  • Author: Levental, Ilya ; Lyman, Ed
  • Subjects: Animals ; Cell Membrane - metabolism ; Integral membrane proteins ; Lipids ; Mammals ; Mammals - metabolism ; Membrane Proteins - metabolism ; Membranes ; Metabolism ; Microenvironments ; Modulation ; Physicochemical properties ; Protein interaction ; Protein structure ; Proteins ; Proteome - metabolism ; Proteomes ; Signaling ; Structure-function relationships
  • Is Part Of: Nature reviews. Molecular cell biology, 2023-02, Vol.24 (2), p.107-122
  • Description: Transmembrane proteins comprise ~30% of the mammalian proteome, mediating metabolism, signalling, transport and many other functions required for cellular life. The microenvironment of integral membrane proteins (IMPs) is intrinsically different from that of cytoplasmic proteins, with IMPs solvated by a compositionally and biophysically complex lipid matrix. These solvating lipids affect protein structure and function in a variety of ways, from stereospecific, high-affinity protein-lipid interactions to modulation by bulk membrane properties. Specific examples of functional modulation of IMPs by their solvating membranes have been reported for various transporters, channels and signal receptors; however, generalizable mechanistic principles governing IMP regulation by lipid environments are neither widely appreciated nor completely understood. Here, we review recent insights into the inter-relationships between complex lipidomes of mammalian membranes, the membrane physicochemical properties resulting from such lipid collectives, and the regulation of IMPs by either or both. The recent proliferation of high-resolution methods to study such lipid-protein interactions has led to generalizable insights, which we synthesize into a general framework termed the 'functional paralipidome' to understand the mutual regulation between membrane proteins and their surrounding lipid microenvironments.
  • Publisher: England: Nature Publishing Group
  • Language: English
  • Identifier: ISSN: 1471-0072
    EISSN: 1471-0080
    DOI: 10.1038/s41580-022-00524-4
    PMID: 36056103
  • Source: MEDLINE
    ProQuest Databases
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