Journal articles: 'Lipid transfer proteins'

1

Fielding, Christopher J. "Lipid transfer proteins." Current Opinion in Lipidology 4, no. 3 (June 1993): 218–22. http://dx.doi.org/10.1097/00041433-199306000-00007.

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Ng, Tzi Bun, Randy Chi Fai Cheung, Jack Ho Wong, and Xiujuan Ye. "Lipid-transfer proteins." Biopolymers 98, no. 4 (2012): 268–79. http://dx.doi.org/10.1002/bip.22098.

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Rueckert, Dieter G., and Karlheinz Schmidt. "Lipid transfer proteins." Chemistry and Physics of Lipids 56, no. 1 (November 1990): 1–20. http://dx.doi.org/10.1016/0009-3084(90)90083-4.

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4

Tall, Alan. "Plasma Lipid Transfer Proteins." Annual Review of Biochemistry 64, no. 1 (June 1995): 235–57. http://dx.doi.org/10.1146/annurev.bi.64.070195.001315.

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Tall, A. R. "Plasma lipid transfer proteins." Journal of Lipid Research 27, no. 4 (June 1988): 361–67. http://dx.doi.org/10.1016/s0022-2275(20)38819-2.

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Jiang, Xian-Cheng, and Hong-Wen Zhou. "Plasma lipid transfer proteins." Current Opinion in Lipidology 17, no. 3 (June 2006): 302–8. http://dx.doi.org/10.1097/01.mol.0000226124.94757.ee.

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Levine, Tim P. "A lipid transfer protein that transfers lipid." Journal of Cell Biology 179, no. 1 (October 8, 2007): 11–13. http://dx.doi.org/10.1083/jcb.200709055.

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Very few lipid transfer proteins (LTPs) have been caught in the act of transferring lipids in vivo from a donor membrane to an acceptor membrane. Now, two studies (Halter, D., S. Neumann, S.M. van Dijk, J. Wolthoorn, A.M. de Maziere, O.V. Vieira, P. Mattjus, J. Klumperman, G. van Meer, and H. Sprong. 2007. J. Cell Biol. 179:101–115; D'Angelo, G., E. Polishchuk, G.D. Tullio, M. Santoro, A.D. Campli, A. Godi, G. West, J. Bielawski, C.C. Chuang, A.C. van der Spoel, et al. 2007. Nature. 449:62–67) agree that four-phosphate adaptor protein 2 (FAPP2) transfers glucosylceramide (GlcCer), a lipid that takes an unexpectedly circuitous route.

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Wong, Louise H., Alenka Čopič, and Tim P. Levine. "Advances on the Transfer of Lipids by Lipid Transfer Proteins." Trends in Biochemical Sciences 42, no. 7 (July 2017): 516–30. http://dx.doi.org/10.1016/j.tibs.2017.05.001.

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NISHIMURA, Taki. "Nanoscale Lipid Organization by Lipid Transfer Proteins." Seibutsu Butsuri 62, no. 3 (2022): 170–74. http://dx.doi.org/10.2142/biophys.62.170.

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Bourgis, Fabienne, and Jean-Claude Kader. "Lipid-transfer proteins: Tools for manipulating membrane lipids." Physiologia Plantarum 100, no. 1 (May 1997): 78–84. http://dx.doi.org/10.1111/j.1399-3054.1997.tb03456.x.

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Bourgis, Fabienne, and Jean-Claude Kader. "Lipid-transfer proteins: Tools for manipulating membrane lipids." Physiologia Plantarum 100, no. 1 (May 1997): 78–84. http://dx.doi.org/10.1034/j.1399-3054.1997.1000107.x.

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12

Chasan, Rebecca. "Lipid Transfer Proteins: Moving Molecules?" Plant Cell 3, no. 9 (September 1991): 842. http://dx.doi.org/10.2307/3869145.

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Kader, Jean-Claude. "LIPID-TRANSFER PROTEINS IN PLANTS." Annual Review of Plant Physiology and Plant Molecular Biology 47, no. 1 (June 1996): 627–54. http://dx.doi.org/10.1146/annurev.arplant.47.1.627.

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Chasan, R. "Lipid Transfer Proteins: Moving Molecules?" Plant Cell 3, no. 9 (September 1, 1991): 842–43. http://dx.doi.org/10.1105/tpc.3.9.842.

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15

Chen, Shuliang, Melissa A. Roberts, Chun-Yuan Chen, Sebastian Markmiller, Hong-Guang Wei, Gene W. Yeo, James G. Granneman, James A. Olzmann, and Susan Ferro-Novick. "VPS13A and VPS13C Influence Lipid Droplet Abundance." Contact 5 (January 2022): 251525642211256. http://dx.doi.org/10.1177/25152564221125613.

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Lipid transfer proteins mediate the exchange of lipids between closely apposed membranes at organelle contact sites and play key roles in lipid metabolism, membrane homeostasis, and cellular signaling. A recently discovered novel family of lipid transfer proteins, which includes the VPS13 proteins (VPS13A-D), adopt a rod-like bridge conformation with an extended hydrophobic groove that enables the bulk transfer of membrane lipids for membrane growth. Loss of function mutations in VPS13A and VPS13C cause chorea acanthocytosis and Parkinson's disease, respectively. VPS13A and VPS13C localize to multiple organelle contact sites, including endoplasmic reticulum (ER) – lipid droplet (LD) contact sites, but the functional roles of these proteins in LD regulation remains mostly unexplored. Here we employ CRISPR-Cas9 genome editing to generate VPS13A and VPS13C knockout cell lines in U-2 OS cells via deletion of exon 2 and introduction of an early frameshift. Analysis of LD content in these cell lines revealed that loss of either VPS13A or VPS13C results in reduced LD abundance under oleate-stimulated conditions. These data implicate two lipid transfer proteins, VPS13A and VPS13C, in LD regulation.

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Yu, Haijia, Yinghui Liu, Daniel R. Gulbranson, Alex Paine, Shailendra S. Rathore, and Jingshi Shen. "Extended synaptotagmins are Ca2+-dependent lipid transfer proteins at membrane contact sites." Proceedings of the National Academy of Sciences 113, no. 16 (April 4, 2016): 4362–67. http://dx.doi.org/10.1073/pnas.1517259113.

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Organelles are in constant communication with each other through exchange of proteins (mediated by trafficking vesicles) and lipids [mediated by both trafficking vesicles and lipid transfer proteins (LTPs)]. It has long been known that vesicle trafficking can be tightly regulated by the second messenger Ca2+, allowing membrane protein transport to be adjusted according to physiological demands. However, it remains unclear whether LTP-mediated lipid transport can also be regulated by Ca2+. In this work, we show that extended synaptotagmins (E-Syts), poorly understood membrane proteins at endoplasmic reticulum–plasma membrane contact sites, are Ca2+-dependent LTPs. Using both recombinant and endogenous mammalian proteins, we discovered that E-Syts transfer glycerophospholipids between membrane bilayers in the presence of Ca2+. E-Syts use their lipid-accommodating synaptotagmin-like mitochondrial lipid binding protein (SMP) domains to transfer lipids. However, the SMP domains themselves cannot transport lipids unless the two membranes are tightly tethered by Ca2+-bound C2 domains. Strikingly, the Ca2+-regulated lipid transfer activity of E-Syts was fully recapitulated when the SMP domain was fused to the cytosolic domain of synaptotagmin-1, the Ca2+ sensor in synaptic vesicle fusion, indicating that a common mechanism of membrane tethering governs the Ca2+ regulation of lipid transfer and vesicle fusion. Finally, we showed that microsomal vesicles isolated from mammalian cells contained robust Ca2+-dependent lipid transfer activities, which were mediated by E-Syts. These findings established E-Syts as a novel class of LTPs and showed that LTP-mediated lipid trafficking, like vesicular transport, can be subject to tight Ca2+ regulation.

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Snoek, G. T., CM van Tiel, and K. W. A. Wirtz. "Phospbatidylinositol transfer proteins in lipid signalling." Biochemical Society Transactions 28, no. 5 (October 1, 2000): A131. http://dx.doi.org/10.1042/bst028a131c.

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18

D’Angelo, Giovanni, Mariella Vicinanza, and Maria Antonietta De Matteis. "Lipid-transfer proteins in biosynthetic pathways." Current Opinion in Cell Biology 20, no. 4 (August 2008): 360–70. http://dx.doi.org/10.1016/j.ceb.2008.03.013.

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Stein, O., and Y. Stein. "Lipid transfer proteins (LTP) and atherosclerosis." Atherosclerosis 178, no. 2 (February 2005): 217–30. http://dx.doi.org/10.1016/j.atherosclerosis.2004.10.008.

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Scallen, Terence J., Andrzej Pastuszyn, Billie J. Noland, Roland Chanderbhan, Akram Kharroubi, and George V. Vahouny. "Sterol carrier and lipid transfer proteins." Chemistry and Physics of Lipids 38, no. 3 (September 1985): 239–61. http://dx.doi.org/10.1016/0009-3084(85)90019-2.

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21

Zhang, Yongli, Jinghua Ge, Xin Bian, and Avinash Kumar. "Quantitative Models of Lipid Transfer and Membrane Contact Formation." Contact 5 (January 2022): 251525642210960. http://dx.doi.org/10.1177/25152564221096024.

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Lipid transfer proteins (LTPs) transfer lipids between different organelles, and thus play key roles in lipid homeostasis and organelle dynamics. The lipid transfer often occurs at the membrane contact sites (MCS) where two membranes are held within 10–30 nm. While most LTPs act as a shuttle to transfer lipids, recent experiments reveal a new category of eukaryotic LTPs that may serve as a bridge to transport lipids in bulk at MCSs. However, the molecular mechanisms underlying lipid transfer and MCS formation are not well understood. Here, we first review two recent studies of extended synaptotagmin (E-Syt)-mediated membrane binding and lipid transfer using novel approaches. Then we describe mathematical models to quantify the kinetics of lipid transfer by shuttle LTPs based on a lipid exchange mechanism. We find that simple lipid mixing among membranes of similar composition and/or lipid partitioning among membranes of distinct composition can explain lipid transfer against a concentration gradient widely observed for LTPs. We predict that selective transport of lipids, but not membrane proteins, by bridge LTPs leads to osmotic membrane tension by analogy to the osmotic pressure across a semipermeable membrane. A gradient of such tension and the conventional membrane tension may drive bulk lipid flow through bridge LTPs at a speed consistent with the fast membrane expansion observed in vivo. Finally, we discuss the implications of membrane tension and lipid transfer in organelle biogenesis. Overall, the quantitative models may help clarify the mechanisms of LTP-mediated MCS formation and lipid transfer.

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Goto, Asako, Aya Mizuike, and Kentaro Hanada. "Sphingolipid Metabolism at the ER-Golgi Contact Zone and Its Impact on Membrane Trafficking." Contact 3 (January 2020): 251525642095951. http://dx.doi.org/10.1177/2515256420959514.

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Proteins and lipids represent the two major constituents of biological membranes. Different organelles have different lipid compositions, which may be crucial for the execution and control of various organelle-specific functions. The interorganellar transport of lipids is dominated by mechanisms that are distinct from the vesicular mechanisms that underlie the interorganellar transport of proteins. Lipid transfer proteins (LTPs) efficiently and accurately mediate the trafficking of membrane lipids at the interfaces between different organelles. In this review, which focuses on sphingolipids, we describe the coordinated synthesis and transfer of lipids that occur at the endoplasmic reticulum (ER)-Golgi apparatus contact zones and discuss the impacts of lipid metabolism on membrane trafficking from the trans-Golgi network (TGN).

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23

WIRTZ, Karel W. A. "Phospholipid transfer proteins revisited." Biochemical Journal 324, no. 2 (June 1, 1997): 353–60. http://dx.doi.org/10.1042/bj3240353.

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Phosphatidylinositol transfer protein (PI-TP) and the non-specific lipid transfer protein (nsL-TP) (identical with sterol carrier protein 2) belong to the large and diverse family of intracellular lipid-binding proteins. Although these two proteins may express a comparable phospholipid transfer activity in vitro, recent studies in yeast and mammalian cells have indicated that they serve completely different functions. PI-TP (identical with yeast SEC14p) plays an important role in vesicle flow both in the budding reaction from the trans-Golgi network and in the fusion reaction with the plasma membrane. In yeast, vesicle budding is linked to PI-TP regulating Golgi phosphatidylcholine (PC) biosynthesis with the apparent purpose of maintaining an optimal PI/PC ratio of the Golgi complex. In mammalian cells, vesicle flow appears to be dependent on PI-TP stimulating phosphatidylinositol 4,5-bisphosphate (PIP2) synthesis. This latter process may also be linked to the ability of PI-TP to reconstitute the receptor-controlled PIP2-specific phospholipase C activity. The nsL-TP is a peroxisomal protein which, by its ability to bind fatty acyl-CoAs, is most likely involved in the β-oxidation of fatty acids in this organelle. This protein constitutes the N-terminus of the 58 kDa protein which is one of the peroxisomal 3-oxo-acyl-CoA thiolases. Further studies on these and other known phospholipid transfer proteins are bound to reveal new insights in their important role as mediators between lipid metabolism and cell functions.

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Kader, Jean-Claude. "Lipid-transfer proteins: a puzzling family of plant proteins." Trends in Plant Science 2, no. 2 (February 1997): 66–70. http://dx.doi.org/10.1016/s1360-1385(97)82565-4.

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Shamin, Maria, Samantha J. Spratley, Stephen C. Graham, and Janet E. Deane. "A Tetrameric Assembly of Saposin A: Increasing Structural Diversity in Lipid Transfer Proteins." Contact 4 (January 2021): 251525642110523. http://dx.doi.org/10.1177/25152564211052382.

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Saposins are lipid transfer proteins required for the degradation of sphingolipids in the lysosome. These small proteins bind lipids by transitioning from a closed, monomeric state to an open conformation exposing a hydrophobic surface that binds and shields hydrophobic lipid tails from the aqueous environment. Saposins form a range of multimeric assemblies to encompass these bound lipids and present them to hydrolases in the lysosome. This lipid-binding property of human saposin A has been exploited to form lipoprotein nanodiscs suitable for structural studies of membrane proteins. Here we present the crystal structure of a unique tetrameric assembly of murine saposin A produced serendipitously, following modifications of published protocols for making lipoprotein nanodiscs. The structure of this new saposin oligomer highlights the diversity of tertiary arrangement that can be adopted by these important lipid transfer proteins.

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Neuman, Sarah D., Amy T. Cavanagh, and Arash Bashirullah. "The Hob Proteins: Putative, Novel Lipid Transfer Proteins at ER-PM Contact Sites." Contact 4 (January 2021): 251525642110523. http://dx.doi.org/10.1177/25152564211052376.

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Nonvesicular transfer of lipids at membrane contact sites (MCS) has recently emerged as a critical process for cellular function. Lipid transfer proteins (LTPs) mediate this unique transport mechanism, and although several LTPs are known, the cellular complement of these proteins continues to expand. Our recent work has revealed the highly conserved but poorly characterized Hobbit/Hob proteins as novel, putative LTPs at endoplasmic reticulum-plasma membrane (ER-PM) contact sites. Using both S. cerevisiae and D. melanogaster model systems, we demonstrated that the Hob proteins localize to ER-PM contact sites via an N-terminal ER membrane anchor and conserved C-terminal sequences. These conserved C-terminal sequences bind to phosphoinositides (PIPs), and the distribution of PIPs is disrupted in hobbit mutant cells. Recently released structural models of the Hob proteins exhibit remarkable similarity to other bona fide LTPs, like VPS13A and ATG2, that function at MCS. Hobbit is required for viability in Drosophila, suggesting that the Hob proteins are essential genes that may mediate lipid transfer at MCS.

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Routt, Sheri M., and Vytas A. Bankaitis. "Biological functions of phosphatidylinositol transfer proteins." Biochemistry and Cell Biology 82, no. 1 (February 1, 2004): 254–62. http://dx.doi.org/10.1139/o03-089.

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Phosphatidylinositol/phosphatidylcholine transfer proteins (PITPs) are ubiquitous and highly conserved proteins that are believed to regulate lipid-mediated signaling events. Their ubiquity and conservation notwithstanding, PITPs remain remarkably uninvestigated. Little is known about the coupling of specific PITPs to explicit cellular functions or the mechanisms by which PITPs interface with apppropriate cellular functions. The available information indicates a role for these proteins in regulating the interface between lipid metabolism and membrane trafficking in yeast, signaling in plant development, the trafficking of specialized luminal cargo in mammalian enterocytes, and neurological function in mammals. Herein, we review recent advances in PITP biology and discuss as yet unresolved issues in this field.Key words: phosphatidylinositol transfer protein, secretion, lipid signaling, phosphoinositide.

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Tabar, AI, A. Diaz-Perales, BE Garcia, B. Gomez, Domingo Barber, G. Salcedo, and R. Sanchez-Monge. "Lipid-transfer proteins (LTPs) and asparagus allergy." Journal of Allergy and Clinical Immunology 109, no. 1 (January 2002): S309. http://dx.doi.org/10.1016/s0091-6749(02)82084-x.

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Ahrazem, Oussama, M. Dolores Ibáñez, Gema López-Torrejón, Rosa Sánchez-Monge, Joaquin Sastre, Manuel Lombardero, Domingo Barber, and Gabriel Salcedo. "Lipid Transfer Proteins and Allergy to Oranges." International Archives of Allergy and Immunology 137, no. 3 (2005): 201–10. http://dx.doi.org/10.1159/000086332.

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30

Quintão, Eder C. R., and Patrícia M. Cazita. "Lipid transfer proteins: Past, present and perspectives." Atherosclerosis 209, no. 1 (March 2010): 1–9. http://dx.doi.org/10.1016/j.atherosclerosis.2009.08.002.

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31

Lev, Sima. "Non-vesicular lipid transport by lipid-transfer proteins and beyond." Nature Reviews Molecular Cell Biology 11, no. 10 (September 8, 2010): 739–50. http://dx.doi.org/10.1038/nrm2971.

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32

Wong, Louise H., and Tim P. Levine. "Lipid transfer proteins do their thing anchored at membrane contact sites… but what is their thing?" Biochemical Society Transactions 44, no. 2 (April 11, 2016): 517–27. http://dx.doi.org/10.1042/bst20150275.

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Membrane contact sites are structures where two organelles come close together to regulate flow of material and information between them. One type of inter-organelle communication is lipid exchange, which must occur for membrane maintenance and in response to environmental and cellular stimuli. Soluble lipid transfer proteins have been extensively studied, but additional families of transfer proteins have been identified that are anchored into membranes by transmembrane helices so that they cannot diffuse through the cytosol to deliver lipids. If such proteins target membrane contact sites they may be major players in lipid metabolism. The eukaryotic family of so-called Lipid transfer proteins Anchored at Membrane contact sites (LAMs) all contain both a sterol-specific lipid transfer domain in the StARkin superfamily (related to StART/Bet_v1), and one or more transmembrane helices anchoring them in the endoplasmic reticulum (ER), making them interesting subjects for study in relation to sterol metabolism. They target a variety of membrane contact sites, including newly described contacts between organelles that were already known to make contact by other means. Lam1–4p target punctate ER–plasma membrane contacts. Lam5p and Lam6p target multiple contacts including a new category: vacuolar non-NVJ cytoplasmic ER (VancE) contacts. These developments confirm previous observations on tubular lipid-binding proteins (TULIPs) that established the importance of membrane anchored proteins for lipid traffic. However, the question remaining to be solved is the most difficult of all: are LAMs transporters, or alternately are they regulators that affect traffic more indirectly?

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Tamura, Yasushi, Shin Kawano, and Toshiya Endo. "Lipid homeostasis in mitochondria." Biological Chemistry 401, no. 6-7 (May 26, 2020): 821–33. http://dx.doi.org/10.1515/hsz-2020-0121.

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AbstractMitochondria are surrounded by the two membranes, the outer and inner membranes, whose lipid compositions are optimized for proper functions and structural organizations of mitochondria. Although a part of mitochondrial lipids including their characteristic lipids, phosphatidylethanolamine and cardiolipin, are synthesized within mitochondria, their precursor lipids and other lipids are transported from other organelles, mainly the ER. Mitochondrially synthesized lipids are re-distributed within mitochondria and to other organelles, as well. Recent studies pointed to the important roles of inter-organelle contact sites in lipid trafficking between different organelle membranes. Identification of Ups/PRELI proteins as lipid transfer proteins shuttling between the mitochondrial outer and inner membranes established a part of the molecular and structural basis of the still elusive intra-mitochondrial lipid trafficking.

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Delfosse, Vanessa, William Bourguet, and Guillaume Drin. "Structural and Functional Specialization of OSBP-Related Proteins." Contact 3 (January 2020): 251525642094662. http://dx.doi.org/10.1177/2515256420946627.

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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.

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35

Cockcroft, Shamshad. "Trafficking of phosphatidylinositol by phosphatidylinositol transfer proteins." Biochemical Society Symposia 74 (January 12, 2007): 259–71. http://dx.doi.org/10.1042/bss2007c21.

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PtdIns is synthesized at the endoplasmic reticulum and its intracellular distribution to other organelles can be facilitated by lipid transfer proteins [PITPs (phosphatidylinositol transfer proteins)]. In this review, I summarize the current understanding of how PITPs are regulated by phosphorylation, how can they dock to membranes to exchange their lipid cargo and how cells use PITPs in signal transduction and membrane delivery. Mammalian PITPs, PITPα and PITPβ, are paralogous genes that are 94% similar in sequence. Their structural design demonstrates that they can sequester PtdIns or PtdCho (phosphatidylcholine) in their hydrophobic cavity. To deliver the lipid cargo to a membrane, PITP has to undergo a conformational change at the membrane interface. PITPs have a higher affinity for PtdIns than PtdCho, which is explained by hydrogen-bond contacts between the inositol ring of PtdIns and the side-chains of four amino acid residues, Thr59, Lys61, Glu86 and Asn90, in PITPs. Regardless of species, these residues are conserved in all known PITPs. PITP transfer activity is regulated by a conserved serine residue (Ser166) that is phosphorylated by protein kinase C. Ser166 is only accessible for phosphorylation when a conformational change occurs in PITPs while docking at the membrane interface during lipid transfer, thereby coupling regulation of activity with lipid transfer function. Biological roles of PITPs include their ability to couple phospholipase C signalling to neurite outgrowth, cell division and stem cell growth.

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Shadan, Sadaf, Roman Holic, Nicolas Carvou, Patrick Ee, Michelle Li, Judith Murray-Rust, and Shamshad Cockcroft. "Dynamics of Lipid Transfer by Phosphatidylinositol Transfer Proteins in Cells." Traffic 9, no. 10 (October 2008): 1743–56. http://dx.doi.org/10.1111/j.1600-0854.2008.00794.x.

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37

Guerbette, Françoise, Michèle Grosbois, Alain Jolliot-Croquin, Jean-Claude Kader, and Alain Zachowski. "Comparison of Lipid Binding and Transfer Properties of Two Lipid Transfer Proteins from Plants†." Biochemistry 38, no. 43 (October 1999): 14131–37. http://dx.doi.org/10.1021/bi990952l.

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Melnikova, Daria N., Ekaterina I. Finkina, Ivan V. Bogdanov, Andrey A. Tagaev, and Tatiana V. Ovchinnikova. "Features and Possible Applications of Plant Lipid-Binding and Transfer Proteins." Membranes 13, no. 1 (December 20, 2022): 2. http://dx.doi.org/10.3390/membranes13010002.

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In plants, lipid trafficking within and inside the cell is carried out by lipid-binding and transfer proteins. Ligands for these proteins are building and signaling lipid molecules, secondary metabolites with different biological activities due to which they perform diverse functions in plants. Many different classes of such lipid-binding and transfer proteins have been found, but the most common and represented in plants are lipid transfer proteins (LTPs), pathogenesis-related class 10 (PR-10) proteins, acyl-CoA-binding proteins (ACBPs), and puroindolines (PINs). A low degree of amino acid sequence homology but similar spatial structures containing an internal hydrophobic cavity are common features of these classes of proteins. In this review, we summarize the latest known data on the features of these protein classes with particular focus on their ability to bind and transfer lipid ligands. We analyzed the structural features of these proteins, the diversity of their possible ligands, the key amino acids participating in ligand binding, the currently known mechanisms of ligand binding and transferring, as well as prospects for possible application.

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Zhou, D. "Editing of CD1d-Bound Lipid Antigens by Endosomal Lipid Transfer Proteins." Science 303, no. 5657 (January 23, 2004): 523–27. http://dx.doi.org/10.1126/science.1092009.

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40

Wong, Louise H., Alberto T. Gatta, and Tim P. Levine. "Lipid transfer proteins: the lipid commute via shuttles, bridges and tubes." Nature Reviews Molecular Cell Biology 20, no. 2 (October 18, 2018): 85–101. http://dx.doi.org/10.1038/s41580-018-0071-5.

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Soccio, Raymond E., and Jan L. Breslow. "StAR-related Lipid Transfer (START) Proteins: Mediators of Intracellular Lipid Metabolism." Journal of Biological Chemistry 278, no. 25 (April 30, 2003): 22183–86. http://dx.doi.org/10.1074/jbc.r300003200.

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42

Drin, Guillaume, Joachim Moser von Filseck, and Alenka Čopič. "New molecular mechanisms of inter-organelle lipid transport." Biochemical Society Transactions 44, no. 2 (April 11, 2016): 486–92. http://dx.doi.org/10.1042/bst20150265.

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Lipids are precisely distributed in cell membranes, along with associated proteins defining organelle identity. Because the major cellular lipid factory is the endoplasmic reticulum (ER), a key issue is to understand how various lipids are subsequently delivered to other compartments by vesicular and non-vesicular transport pathways. Efforts are currently made to decipher how lipid transfer proteins (LTPs) work either across long distances or confined to membrane contact sites (MCSs) where two organelles are at close proximity. Recent findings reveal that proteins of the oxysterol-binding protein related-proteins (ORP)/oxysterol-binding homology (Osh) family are not all just sterol transporters/sensors: some can bind either phosphatidylinositol 4-phosphate (PtdIns(4)P) and sterol or PtdIns(4)P and phosphatidylserine (PS), exchange these lipids between membranes, and thereby use phosphoinositide metabolism to create cellular lipid gradients. Lipid exchange is likely a widespread mechanism also utilized by other LTPs to efficiently trade lipids between organelle membranes. Finally, the discovery of more proteins bearing a lipid-binding module (SMP or START-like domain) raises new questions on how lipids are conveyed in cells and how the activities of different LTPs are coordinated.

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Shamin, Maria, Tomasz H. Benedyk, Stephen C. Graham, and Janet E. Deane. "The lipid transfer protein Saposin B does not directly bind CD1d for lipid antigen loading." Wellcome Open Research 4 (August 2, 2019): 117. http://dx.doi.org/10.12688/wellcomeopenres.15368.1.

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Background: Lipid antigens are presented on the surface of cells by the CD1 family of glycoproteins, which have structural and functional similarity to MHC class I molecules. The hydrophobic lipid antigens are embedded in membranes and inaccessible to the lumenal lipid-binding domain of CD1 molecules. Therefore, CD1 molecules require lipid transfer proteins for lipid loading and editing. CD1d is loaded with lipids in late endocytic compartments, and lipid transfer proteins of the saposin family have been shown to play a crucial role in this process. However, the mechanism by which saposins facilitate lipid binding to CD1 molecules is not known and is thought to involve transient interactions between protein components to ensure CD1-lipid complexes can be efficiently trafficked to the plasma membrane for antigen presentation. Of the four saposin proteins, the importance of Saposin B (SapB) for loading of CD1d is the most well-characterised. However, a direct interaction between CD1d and SapB has yet to be described. Methods: In order to determine how SapB might load lipids onto CD1d, we used purified, recombinant CD1d and SapB and carried out a series of highly sensitive binding assays to monitor direct interactions. We performed equilibrium binding analysis, chemical cross-linking and co-crystallisation experiments, under a range of different conditions. Results: We could not demonstrate a direct interaction between SapB and CD1d using any of these binding assays. Conclusions: This work establishes comprehensively that the role of SapB in lipid loading does not involve direct binding to CD1d. We discuss the implication of this for our understanding of lipid loading of CD1d and propose several factors that may influence this process.

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Shamin, Maria, Tomasz H. Benedyk, Stephen C. Graham, and Janet E. Deane. "The lipid transfer protein Saposin B does not directly bind CD1d for lipid antigen loading." Wellcome Open Research 4 (October 18, 2019): 117. http://dx.doi.org/10.12688/wellcomeopenres.15368.2.

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Abstract:

Background: Lipid antigens are presented on the surface of cells by the CD1 family of glycoproteins, which have structural and functional similarity to MHC class I molecules. The hydrophobic lipid antigens are embedded in membranes and inaccessible to the lumenal lipid-binding domain of CD1 molecules. Therefore, CD1 molecules require lipid transfer proteins for lipid loading and editing. CD1d is loaded with lipids in late endocytic compartments, and lipid transfer proteins of the saposin family have been shown to play a crucial role in this process. However, the mechanism by which saposins facilitate lipid binding to CD1 molecules is not known and is thought to involve transient interactions between protein components to ensure CD1-lipid complexes can be efficiently trafficked to the plasma membrane for antigen presentation. Of the four saposin proteins, the importance of Saposin B (SapB) for loading of CD1d is the most well-characterised. However, a direct interaction between CD1d and SapB has yet to be described. Methods: In order to determine how SapB might load lipids onto CD1d, we used purified, recombinant CD1d and SapB and carried out a series of highly sensitive binding assays to monitor direct interactions. We performed equilibrium binding analysis, chemical cross-linking and co-crystallisation experiments, under a range of different conditions. Results: We could not demonstrate a direct interaction between SapB and CD1d using any of these binding assays. Conclusions: This work strongly indicates that the role of SapB in lipid loading does not involve direct binding to CD1d. We discuss the implication of this for our understanding of lipid loading of CD1d and propose several factors that may influence this process.

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Ghanbarpour, Alireza, Diana P. Valverde, Thomas J. Melia, and Karin M. Reinisch. "A model for a partnership of lipid transfer proteins and scramblases in membrane expansion and organelle biogenesis." Proceedings of the National Academy of Sciences 118, no. 16 (April 13, 2021): e2101562118. http://dx.doi.org/10.1073/pnas.2101562118.

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The autophagy protein ATG2, proposed to transfer bulk lipid from the endoplasmic reticulum (ER) during autophagosome biogenesis, interacts with ER residents TMEM41B and VMP1 and with ATG9, in Golgi-derived vesicles that initiate autophagosome formation. In vitro assays reveal TMEM41B, VMP1, and ATG9 as scramblases. We propose a model wherein membrane expansion results from the partnership of a lipid transfer protein, moving lipids between the cytosolic leaflets of apposed organelles, and scramblases that reequilibrate the leaflets of donor and acceptor organelle membranes as lipids are depleted or augmented. TMEM41B and VMP1 are implicated broadly in lipid homeostasis and membrane dynamics processes in which their scrambling activities likely are key.

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Missaoui, Khawla, Zulema Gonzalez-Klein, Diego Pazos-Castro, Guadalupe Hernandez-Ramirez, Maria Garrido-Arandia, Faical Brini, Araceli Diaz-Perales, and Jaime Tome-Amat. "Plant non-specific lipid transfer proteins: An overview." Plant Physiology and Biochemistry 171 (January 2022): 115–27. http://dx.doi.org/10.1016/j.plaphy.2021.12.026.

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Holič, Roman, Dominik Šťastný, and Peter Griač. "Sec14 family of lipid transfer proteins in yeasts." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1866, no. 10 (October 2021): 158990. http://dx.doi.org/10.1016/j.bbalip.2021.158990.

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SILVER, DAVID L., XIAN-CHENG JIANG, TAKESHI ARAI, CAN BRUCE, and ALAN R. TALL. "Receptors and Lipid Transfer Proteins in HDL Metabolism." Annals of the New York Academy of Sciences 902, no. 1 (January 25, 2006): 103–12. http://dx.doi.org/10.1111/j.1749-6632.2000.tb06305.x.

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Ohnishi, T., S. Yokoyama, and A. Yamamoto. "Rapid purification of human plasma lipid transfer proteins." Journal of Lipid Research 31, no. 3 (March 1990): 397–406. http://dx.doi.org/10.1016/s0022-2275(20)43162-1.

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Wirtz, K. W. A. "Phospholipid transfer proteins: From lipid monolayers to cells." Klinische Wochenschrift 69, no. 3 (February 1991): 105–11. http://dx.doi.org/10.1007/bf01795953.

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Journal articles on the topic 'Lipid transfer proteins'

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