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Bacterial AsmA-Like Proteins: Bridging the Gap in Intermembrane Phospholipid Transport
In eukaryotic cells, nonvesicular lipid transport between organelles is mediated by lipid-transfer proteins. Recently, a new class of these lipid transporters has been described to facilitate the bulk of inter-organelle lipid transport at contact sites by forming bridge-like structures with a hydrop...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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SAGE Publications
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10345924/ https://www.ncbi.nlm.nih.gov/pubmed/37455811 http://dx.doi.org/10.1177/25152564231185931 |
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author | Kumar, Sujeet Ruiz, Natividad |
author_facet | Kumar, Sujeet Ruiz, Natividad |
author_sort | Kumar, Sujeet |
collection | PubMed |
description | In eukaryotic cells, nonvesicular lipid transport between organelles is mediated by lipid-transfer proteins. Recently, a new class of these lipid transporters has been described to facilitate the bulk of inter-organelle lipid transport at contact sites by forming bridge-like structures with a hydrophobic groove through which lipids travel. Because their predicted structure is composed of repeating β-groove (RBG) domains, they have been named the RBG protein superfamily. Early studies on RBG proteins VPS13 and ATG2 recognized the resemblance of their predicted structures to that of the bacterial Lpt system, which transports newly synthesized lipopolysaccharides (LPS) between the inner and the outer membranes (IMs and OMs) of Gram-negative bacteria. In these didermic bacteria, the IMs and OMs are separated by an aqueous periplasmic compartment that is traversed by a bridge-like structure built with β-jelly roll domains from several Lpt proteins that provides a hydrophobic groove for LPS molecules to travel across the periplasm. Despite structural and functional similarities between RBG proteins and the Lpt system, the bacterial AsmA-like protein family has recently emerged as the likely ancestor of RBG proteins and long sought-after transporters that facilitate the transfer of phospholipids from the IM to the OM. Here, we review our current understanding of the structure and function of bacterial AsmA-like proteins, mainly focusing on recent studies that have led to the proposal that AsmA-like proteins mediate the bulk of phospholipid transfer between the IMs and OMs. |
format | Online Article Text |
id | pubmed-10345924 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | SAGE Publications |
record_format | MEDLINE/PubMed |
spelling | pubmed-103459242023-07-15 Bacterial AsmA-Like Proteins: Bridging the Gap in Intermembrane Phospholipid Transport Kumar, Sujeet Ruiz, Natividad Contact (Thousand Oaks) Short Review In eukaryotic cells, nonvesicular lipid transport between organelles is mediated by lipid-transfer proteins. Recently, a new class of these lipid transporters has been described to facilitate the bulk of inter-organelle lipid transport at contact sites by forming bridge-like structures with a hydrophobic groove through which lipids travel. Because their predicted structure is composed of repeating β-groove (RBG) domains, they have been named the RBG protein superfamily. Early studies on RBG proteins VPS13 and ATG2 recognized the resemblance of their predicted structures to that of the bacterial Lpt system, which transports newly synthesized lipopolysaccharides (LPS) between the inner and the outer membranes (IMs and OMs) of Gram-negative bacteria. In these didermic bacteria, the IMs and OMs are separated by an aqueous periplasmic compartment that is traversed by a bridge-like structure built with β-jelly roll domains from several Lpt proteins that provides a hydrophobic groove for LPS molecules to travel across the periplasm. Despite structural and functional similarities between RBG proteins and the Lpt system, the bacterial AsmA-like protein family has recently emerged as the likely ancestor of RBG proteins and long sought-after transporters that facilitate the transfer of phospholipids from the IM to the OM. Here, we review our current understanding of the structure and function of bacterial AsmA-like proteins, mainly focusing on recent studies that have led to the proposal that AsmA-like proteins mediate the bulk of phospholipid transfer between the IMs and OMs. SAGE Publications 2023-07-12 /pmc/articles/PMC10345924/ /pubmed/37455811 http://dx.doi.org/10.1177/25152564231185931 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by-nc/4.0/This article is distributed under the terms of the Creative Commons Attribution-NonCommercial 4.0 License (https://creativecommons.org/licenses/by-nc/4.0/) which permits non-commercial use, reproduction and distribution of the work without further permission provided the original work is attributed as specified on the SAGE and Open Access page (https://us.sagepub.com/en-us/nam/open-access-at-sage). |
spellingShingle | Short Review Kumar, Sujeet Ruiz, Natividad Bacterial AsmA-Like Proteins: Bridging the Gap in Intermembrane Phospholipid Transport |
title | Bacterial AsmA-Like Proteins: Bridging the Gap in Intermembrane Phospholipid Transport |
title_full | Bacterial AsmA-Like Proteins: Bridging the Gap in Intermembrane Phospholipid Transport |
title_fullStr | Bacterial AsmA-Like Proteins: Bridging the Gap in Intermembrane Phospholipid Transport |
title_full_unstemmed | Bacterial AsmA-Like Proteins: Bridging the Gap in Intermembrane Phospholipid Transport |
title_short | Bacterial AsmA-Like Proteins: Bridging the Gap in Intermembrane Phospholipid Transport |
title_sort | bacterial asma-like proteins: bridging the gap in intermembrane phospholipid transport |
topic | Short Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10345924/ https://www.ncbi.nlm.nih.gov/pubmed/37455811 http://dx.doi.org/10.1177/25152564231185931 |
work_keys_str_mv | AT kumarsujeet bacterialasmalikeproteinsbridgingthegapinintermembranephospholipidtransport AT ruiznatividad bacterialasmalikeproteinsbridgingthegapinintermembranephospholipidtransport |