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...
Autores principales: | , , , |
---|---|
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 |