Substrates, regulation, cellular functions, and disease associations of P4-ATPases
Abstract P4-ATPases, a subfamily of the P-type ATPase superfamily, play a crucial role in translocating membrane lipids from the exoplasmic/luminal leaflet to the cytoplasmic leaflet. This process generates and regulates transbilayer lipid asymmetry. These enzymes are conserved across all eukaryotes...
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2025-01-01
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| Series: | Communications Biology |
| Online Access: | https://doi.org/10.1038/s42003-025-07549-3 |
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| _version_ | 1832571388548874240 |
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| author | Hye-Won Shin Hiroyuki Takatsu |
| author_facet | Hye-Won Shin Hiroyuki Takatsu |
| author_sort | Hye-Won Shin |
| collection | DOAJ |
| description | Abstract P4-ATPases, a subfamily of the P-type ATPase superfamily, play a crucial role in translocating membrane lipids from the exoplasmic/luminal leaflet to the cytoplasmic leaflet. This process generates and regulates transbilayer lipid asymmetry. These enzymes are conserved across all eukaryotes, and the human genome encodes 14 distinct P4-ATPases. Initially identified as aminophospholipid translocases, P4-ATPases have since been found to translocate other phospholipids, including phosphatidylcholine, phosphatidylinositol, and even glycosphingolipids. Recent advances in structural analysis have significantly improved our understanding of the lipid transport machinery associated with P4-ATPases, as documented in recent reviews. In this review, we highlight the emerging evidence related to substrate diversity, the regulation of cellular localization, enzymatic activities, and their impact on organism homeostasis and diseases. |
| format | Article |
| id | doaj-art-892563743cff4608b89e13e4a9efec33 |
| institution | Kabale University |
| issn | 2399-3642 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Communications Biology |
| spelling | doaj-art-892563743cff4608b89e13e4a9efec332025-02-02T12:37:09ZengNature PortfolioCommunications Biology2399-36422025-01-018111610.1038/s42003-025-07549-3Substrates, regulation, cellular functions, and disease associations of P4-ATPasesHye-Won Shin0Hiroyuki Takatsu1Graduate School of Pharmaceutical Sciences, Kyoto UniversityGraduate School of Pharmaceutical Sciences, Kyoto UniversityAbstract P4-ATPases, a subfamily of the P-type ATPase superfamily, play a crucial role in translocating membrane lipids from the exoplasmic/luminal leaflet to the cytoplasmic leaflet. This process generates and regulates transbilayer lipid asymmetry. These enzymes are conserved across all eukaryotes, and the human genome encodes 14 distinct P4-ATPases. Initially identified as aminophospholipid translocases, P4-ATPases have since been found to translocate other phospholipids, including phosphatidylcholine, phosphatidylinositol, and even glycosphingolipids. Recent advances in structural analysis have significantly improved our understanding of the lipid transport machinery associated with P4-ATPases, as documented in recent reviews. In this review, we highlight the emerging evidence related to substrate diversity, the regulation of cellular localization, enzymatic activities, and their impact on organism homeostasis and diseases.https://doi.org/10.1038/s42003-025-07549-3 |
| spellingShingle | Hye-Won Shin Hiroyuki Takatsu Substrates, regulation, cellular functions, and disease associations of P4-ATPases Communications Biology |
| title | Substrates, regulation, cellular functions, and disease associations of P4-ATPases |
| title_full | Substrates, regulation, cellular functions, and disease associations of P4-ATPases |
| title_fullStr | Substrates, regulation, cellular functions, and disease associations of P4-ATPases |
| title_full_unstemmed | Substrates, regulation, cellular functions, and disease associations of P4-ATPases |
| title_short | Substrates, regulation, cellular functions, and disease associations of P4-ATPases |
| title_sort | substrates regulation cellular functions and disease associations of p4 atpases |
| url | https://doi.org/10.1038/s42003-025-07549-3 |
| work_keys_str_mv | AT hyewonshin substratesregulationcellularfunctionsanddiseaseassociationsofp4atpases AT hiroyukitakatsu substratesregulationcellularfunctionsanddiseaseassociationsofp4atpases |