Consensus, controversies, and conundrums of P4-ATPases: The emerging face of eukaryotic lipid flippases.
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| Title: | Consensus, controversies, and conundrums of P4-ATPases: The emerging face of eukaryotic lipid flippases. |
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| Authors: | Duan, H. Diessel1 diessel.duan@vai.org, Huilin Li1 huilin.li@vai.org |
| Source: | Journal of Biological Chemistry. Jun2024, Vol. 300 Issue 6, p1-14. 14p. |
| Subjects: | Freight & freightage, Phosphorylation, Pamphlets, Lipids |
| Abstract: | The cryo-EM resolution revolution has heralded a new era in our understanding of eukaryotic lipid flippases with a rapidly growing number of high-resolution structures. Flippases belong to the P4 family of ATPases (type IV P-type ATPases) that largely follow the reaction cycle proposed for the more extensively studied cation-transporting P-type ATPases. However, unlike the canonical P-type ATPases, no flippase cargos are transported in the phosphorylation half-reaction. Instead of being released into the intracellular or extracellular milieu, lipid cargos are transported to their destination at the inner leaflet of the membrane. Recent flippase structures have revealed multiple conformational states during the lipid transport cycle. Nonetheless, critical conformational states capturing the lipid cargo “in transit” are still missing. In this review, we highlight the amazing structural advances of these lipid transporters, discuss various perspectives on catalytic and regulatory mechanisms in the literature, and shed light on future directions in further deciphering the detailed molecular mechanisms of lipid flipping. [ABSTRACT FROM AUTHOR] |
| Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 178196597 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Consensus, controversies, and conundrums of P4-ATPases: The emerging face of eukaryotic lipid flippases. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Duan%2C+H%2E+Diessel%22">Duan, H. Diessel</searchLink><relatesTo>1</relatesTo><i> diessel.duan@vai.org</i><br /><searchLink fieldCode="AR" term="%22Huilin+Li%22">Huilin Li</searchLink><relatesTo>1</relatesTo><i> huilin.li@vai.org</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Journal+of+Biological+Chemistry%22">Journal of Biological Chemistry</searchLink>. Jun2024, Vol. 300 Issue 6, p1-14. 14p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Freight+%26+freightage%22">Freight & freightage</searchLink><br /><searchLink fieldCode="DE" term="%22Phosphorylation%22">Phosphorylation</searchLink><br /><searchLink fieldCode="DE" term="%22Pamphlets%22">Pamphlets</searchLink><br /><searchLink fieldCode="DE" term="%22Lipids%22">Lipids</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: The cryo-EM resolution revolution has heralded a new era in our understanding of eukaryotic lipid flippases with a rapidly growing number of high-resolution structures. Flippases belong to the P4 family of ATPases (type IV P-type ATPases) that largely follow the reaction cycle proposed for the more extensively studied cation-transporting P-type ATPases. However, unlike the canonical P-type ATPases, no flippase cargos are transported in the phosphorylation half-reaction. Instead of being released into the intracellular or extracellular milieu, lipid cargos are transported to their destination at the inner leaflet of the membrane. Recent flippase structures have revealed multiple conformational states during the lipid transport cycle. Nonetheless, critical conformational states capturing the lipid cargo “in transit” are still missing. In this review, we highlight the amazing structural advances of these lipid transporters, discuss various perspectives on catalytic and regulatory mechanisms in the literature, and shed light on future directions in further deciphering the detailed molecular mechanisms of lipid flipping. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1016/j.jbc.2024.107387 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 14 StartPage: 1 Subjects: – SubjectFull: Freight & freightage Type: general – SubjectFull: Phosphorylation Type: general – SubjectFull: Pamphlets Type: general – SubjectFull: Lipids Type: general Titles: – TitleFull: Consensus, controversies, and conundrums of P4-ATPases: The emerging face of eukaryotic lipid flippases. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Duan, H. Diessel – PersonEntity: Name: NameFull: Huilin Li IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 06 Text: Jun2024 Type: published Y: 2024 Identifiers: – Type: issn-print Value: 00219258 Numbering: – Type: volume Value: 300 – Type: issue Value: 6 Titles: – TitleFull: Journal of Biological Chemistry Type: main |
| ResultId | 1 |