Cargando…

Evolutionary History of Oxysterol-Binding Proteins Reveals Complex History of Duplication and Loss in Animals and Fungi

Cells maintain the specific lipid composition of distinct organelles by vesicular transport as well as non-vesicular lipid trafficking via lipid transport proteins. Oxysterol-binding proteins (OSBPs) are a family of lipid transport proteins that transfer lipids at various membrane contact sites (MCS...

Descripción completa

Detalles Bibliográficos
Autores principales: Singh, Rohan P., Poh, Yu-Ping, Sinha, Savar D., Wideman, Jeremy G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: SAGE Publications 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10243569/
https://www.ncbi.nlm.nih.gov/pubmed/37366416
http://dx.doi.org/10.1177/25152564221150428
_version_ 1785054451526008832
author Singh, Rohan P.
Poh, Yu-Ping
Sinha, Savar D.
Wideman, Jeremy G.
author_facet Singh, Rohan P.
Poh, Yu-Ping
Sinha, Savar D.
Wideman, Jeremy G.
author_sort Singh, Rohan P.
collection PubMed
description Cells maintain the specific lipid composition of distinct organelles by vesicular transport as well as non-vesicular lipid trafficking via lipid transport proteins. Oxysterol-binding proteins (OSBPs) are a family of lipid transport proteins that transfer lipids at various membrane contact sites (MCSs). OSBPs have been extensively investigated in human and yeast cells where 12 have been identified in Homo sapiens and 7 in Saccharomyces cerevisiae. The evolutionary relationship between these well-characterized OSBPs is still unclear. By reconstructing phylogenies of eukaryote OSBPs, we show that the ancestral Saccharomycotina had four OSBPs, the ancestral fungus had five OSBPs, and the ancestral animal had six OSBPs, whereas the shared ancestor of animals and fungi as well as the ancestral eukaryote had only three OSBPs. Our analyses identified three undescribed ancient OSBP orthologues, one fungal OSBP (Osh8) lost in the lineage leading to yeast, one animal OSBP (ORP12) lost in the lineage leading to vertebrates, and one eukaryotic OSBP (OshEu) lost in both the animal and fungal lineages.
format Online
Article
Text
id pubmed-10243569
institution National Center for Biotechnology Information
language English
publishDate 2023
publisher SAGE Publications
record_format MEDLINE/PubMed
spelling pubmed-102435692023-06-26 Evolutionary History of Oxysterol-Binding Proteins Reveals Complex History of Duplication and Loss in Animals and Fungi Singh, Rohan P. Poh, Yu-Ping Sinha, Savar D. Wideman, Jeremy G. Contact (Thousand Oaks) Lipid transfer proteins: From molecular mechanisms to functional validation Cells maintain the specific lipid composition of distinct organelles by vesicular transport as well as non-vesicular lipid trafficking via lipid transport proteins. Oxysterol-binding proteins (OSBPs) are a family of lipid transport proteins that transfer lipids at various membrane contact sites (MCSs). OSBPs have been extensively investigated in human and yeast cells where 12 have been identified in Homo sapiens and 7 in Saccharomyces cerevisiae. The evolutionary relationship between these well-characterized OSBPs is still unclear. By reconstructing phylogenies of eukaryote OSBPs, we show that the ancestral Saccharomycotina had four OSBPs, the ancestral fungus had five OSBPs, and the ancestral animal had six OSBPs, whereas the shared ancestor of animals and fungi as well as the ancestral eukaryote had only three OSBPs. Our analyses identified three undescribed ancient OSBP orthologues, one fungal OSBP (Osh8) lost in the lineage leading to yeast, one animal OSBP (ORP12) lost in the lineage leading to vertebrates, and one eukaryotic OSBP (OshEu) lost in both the animal and fungal lineages. SAGE Publications 2023-01-11 /pmc/articles/PMC10243569/ /pubmed/37366416 http://dx.doi.org/10.1177/25152564221150428 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution 4.0 License (https://creativecommons.org/licenses/by/4.0/) which permits any 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 Lipid transfer proteins: From molecular mechanisms to functional validation
Singh, Rohan P.
Poh, Yu-Ping
Sinha, Savar D.
Wideman, Jeremy G.
Evolutionary History of Oxysterol-Binding Proteins Reveals Complex History of Duplication and Loss in Animals and Fungi
title Evolutionary History of Oxysterol-Binding Proteins Reveals Complex History of Duplication and Loss in Animals and Fungi
title_full Evolutionary History of Oxysterol-Binding Proteins Reveals Complex History of Duplication and Loss in Animals and Fungi
title_fullStr Evolutionary History of Oxysterol-Binding Proteins Reveals Complex History of Duplication and Loss in Animals and Fungi
title_full_unstemmed Evolutionary History of Oxysterol-Binding Proteins Reveals Complex History of Duplication and Loss in Animals and Fungi
title_short Evolutionary History of Oxysterol-Binding Proteins Reveals Complex History of Duplication and Loss in Animals and Fungi
title_sort evolutionary history of oxysterol-binding proteins reveals complex history of duplication and loss in animals and fungi
topic Lipid transfer proteins: From molecular mechanisms to functional validation
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10243569/
https://www.ncbi.nlm.nih.gov/pubmed/37366416
http://dx.doi.org/10.1177/25152564221150428
work_keys_str_mv AT singhrohanp evolutionaryhistoryofoxysterolbindingproteinsrevealscomplexhistoryofduplicationandlossinanimalsandfungi
AT pohyuping evolutionaryhistoryofoxysterolbindingproteinsrevealscomplexhistoryofduplicationandlossinanimalsandfungi
AT sinhasavard evolutionaryhistoryofoxysterolbindingproteinsrevealscomplexhistoryofduplicationandlossinanimalsandfungi
AT widemanjeremyg evolutionaryhistoryofoxysterolbindingproteinsrevealscomplexhistoryofduplicationandlossinanimalsandfungi