Structural and Functional Specialization of OSBP-Related Proteins
Autor: | William Bourguet, Vanessa Delfosse, Guillaume Drin |
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Přispěvatelé: | Institut de pharmacologie moléculaire et cellulaire (IPMC), Centre National de la Recherche Scientifique (CNRS)-Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Université Côte d'Azur (UCA), Centre de Biochimie Structurale [Montpellier] (CBS), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM), DELFOSSE, VANESSA, Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Université Nice Sophia Antipolis (1965 - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA) |
Jazyk: | angličtina |
Rok vydání: | 2020 |
Předmět: |
[SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry
Molecular Biology/Structural Biology [q-bio.BM] [SDV.BBM.BP] Life Sciences [q-bio]/Biochemistry Molecular Biology/Biophysics membrane contact sites Computational biology Biology [SDV.BBM.BM] Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology 03 medical and health sciences 0302 clinical medicine sterol Organelle structural biology [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM] [SDV.BBM.BC] Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM] OSBP ComputingMilieux_MISCELLANEOUS Eukaryotic cell 030304 developmental biology 0303 health sciences [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] Functional specialization [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology General Medicine phosphoinositide [SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biophysics Lipid Transfer Protein (LTP) Structural biology Identity (object-oriented programming) Oxysterol Binding Protein (OSBP) 030217 neurology & neurosurgery Function (biology) |
Zdroj: | Contact Contact, Institute of Ophthalmology, University College London, UK, 2020, 3, ⟨10.1177/2515256420946627⟩ Contact, Institute of Ophthalmology, University College London, UK, 2020, 3, pp.251525642094662. ⟨10.1177/2515256420946627⟩ Contact, 2020, 3, pp.251525642094662. ⟨10.1177/2515256420946627⟩ |
ISSN: | 2515-2564 |
Popis: | International audience; Lipids are precisely distributed in the eukaryotic cell where they help to define organelle identity and function, in addition to their structural role. Once synthesized, many lipids must be delivered to other compartments by non-vesicular routes, a process that is undertaken by proteins called Lipid Transfer Proteins (LTPs). OSBP and the closely-related ORP and Osh proteins constitute a major, evolutionarily conserved family of LTPs in eukaryotes. Most of these target one or more subcellular regions, and membrane contact sites in particular, where two organelle membranes are in close proximity. It was initially thought that such proteins were strictly dedicated to sterol sensing or transport. However, over the last decade, numerous studies have revealed that these proteins have many more functions, and we have expanded our understanding of their mechanisms. In particular, many of them are lipid exchangers that exploit PI(4)P or possibly other phosphoinositide gradients to directionally transfer sterol or PS between two compartments. Importantly, these transfer activities are tightly coupled to processes such as lipid metabolism, cellular signalling and vesicular trafficking. This review describes the molecular architecture of OSBP/ORP/Osh proteins, showing how their specific structural features and internal configurations impart unique cellular functions. |
Databáze: | OpenAIRE |
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