ArticleJournal of molecular evolution2006
Fusion and fission, the evolution of sterol carrier protein-2.
Article in Journal of molecular evolution, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 44 citations in OpenAlex.
- Identification of TFG- and Autophagy-Regulated Proteins and Glycerophospholipids in B Cells.Journal of proteome research · 2024Article
- Integration analysis of ATAC-seq and RNA-seq provides insight into fatty acid biosynthesis in Schizochytrium limacinum under nitrogen limitation stress.BMC genomics · 2024Article
- Transcriptional profiles analysis of effects ofFrontiers in cellular and infection microbiology · 2024Article
- Fatty acid uptake inFrontiers in cellular and infection microbiology · 2022Review
- Suppressing a Putative Sterol Carrier Gene Reduces Plasmodesmal Permeability and Activates Sucrose Transporter Genes during Cotton Fiber Elongation.The Plant cell · 2017Article
- Identification of Novel Genetic Determinants of Erythrocyte Membrane Fatty Acid Composition among Greenlanders.PLoS genetics · 2016Article
- Water-mediated recognition of simple alkyl chains by heart-type fatty-acid-binding protein.Angewandte Chemie (International ed. in English) · 2015Article
- The crystal structure of sterol carrier protein 2 from Yarrowia lipolytica and the evolutionary conservation of a large, non-specific lipid-binding cavity.Journal of structural and functional genomics · 2013Article
- Identification, localization, and functional implications of the microdomain-forming stomatin family in the ciliated protozoan Paramecium tetraurelia.Eukaryotic cell · 2013Article
- Evolution of function of a fused metazoan tRNA synthetase.Molecular biology and evolution · 2011Article
- NMR and X-ray structures of the putative sterol carrier protein 2 from Thermus thermophilus HB8 show conformational changes.Journal of structural and functional genomics · 2010Article
- Fatty acid transfer from Yarrowia lipolytica sterol carrier protein 2 to phospholipid membranes.Biophysical journal · 2009Article
- Role of an ancestral d-bifunctional protein containing two sterol-carrier protein-2 domains in lipid uptake and trafficking in Toxoplasma.Molecular biology of the cell · 2009Article
- Transcriptional profiling uncovers a network of cholesterol-responsive atherosclerosis target genes.PLoS genetics · 2008Article
- Slipins: ancient origin, duplication and diversification of the stomatin protein family.BMC evolutionary biology · 2008Article
- Arabidopsis sterol carrier protein-2 is required for normal development of seeds and seedlings.Journal of experimental botany · 2008Article
- Sterol transport in yeast and the oxysterol binding protein homologue (OSH) family.Biochimica et biophysica acta · 2007Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sterol carrier protein-2 (SCP-2) is an intracellular, small, basic protein domain that in vitro enhances the transfer of lipids between membranes. It is expressed in bacteria, archaea, and eukaryotes. There are five human genes, HSD17B4, SCPX, HSDL2 STOML1, and C20orf79, which encode SCP-2. HSD17B4, SCPX, HSDL2, and STOML1 encode fusion proteins with SCP-2 downstream of another protein domain, whereas C20orf79 encodes an unfused SCP-2. We have extracted SCP-2 domains from databases and analyzed the evolution of the eukaryotic SCP-2. We show that SCPX and HSDL2 are present in most animals from Cnidaria to Chordata. STOML1 are present in nematodes and more advanced animals. HSD17B4 which encodes a D-bifunctional protein (DBP) with domains for D-3-hydroxyacyl-CoA dehydrogenase, enoyl-CoA hydratase, and SCP-2 are found in animals from insects to mammals and also in fungi. Nematodes, amoebas, ciliates, apicomplexans, and oomycetes express an alternative DBP with the SCP-2 domain directly connected to the D-3-hydroxyacyl-CoA dehydrogenase. This fusion has not been retained in plant genomes, which solely express unfused SCP-2 domains. Proteins carrying unfused SCP-2 domains are also encoded in bacteria, archaea, ciliates, fungi, insects, nematodes, and vertebrates. Our results indicate that the fusion between D-3-hydroxyacyl-CoA dehydrogenase and SCP-2 was formed early during eukaryotic evolution. There have since been several gene fission events where genes encoding unfused SCP-2 domains have been formed, as well as gene fusion events placing the SCP-2 domain in novel protein domain contexts.
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