氧化甾醇结合蛋白相关蛋白家族的研究进展

doi:10.11983/CBB21045

植物学报 ›› 2021, Vol. 56 ›› Issue (5): 627-640.DOI: 10.11983/CBB21045

• 专题论坛 • 上一篇

氧化甾醇结合蛋白相关蛋白家族的研究进展

邹文娇¹^,³, 葛磊², 予茜²^,^*()

¹山东农业大学生命科学学院, 作物生物学国家重点实验室, 泰安 271018
²青岛农业大学农学院作物组学中心, 青岛 266109
³山东中医药大学, 中医药创新研究院, 济南 250355

收稿日期:2021-03-09 接受日期:2021-05-27 出版日期:2021-09-01 发布日期:2021-08-31
通讯作者: 予茜
作者简介:* E-mail: yuqian@qau.edu.cn
基金资助:
国家自然科学基金(31071066);国家自然科学基金(31370325)

Research Advances in Oxysterol-binding Protein-related Proteins

Wenjiao Zou¹^,³, Lei Ge², Qian Yu²^,^*()

¹State Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Tai’an 271018, China
²Center for Crop Panomics, College of Agronomy, Qingdao Agriculture University, Qingdao 266109, China
³Innovation Institute of Traditional Chinese Medicine, Shandong University of Traditional Chinese Medicine, Jinan 250355, China

Received:2021-03-09 Accepted:2021-05-27 Online:2021-09-01 Published:2021-08-31
Contact: Qian Yu

摘要/Abstract

摘要： 膜脂是细胞膜的主要组分, 也是参与信号转导的重要信号分子。不同脂质分子在细胞膜上的不均等分布需要特殊类型的通道蛋白和运输蛋白来实现。氧化甾醇结合蛋白相关蛋白(ORPs)是一类非常保守的蛋白分子, 能够对磷脂酰肌醇和固醇等脂类分子进行识别并转运, 参与细胞中的许多生理过程, 包括信号转导、囊泡运输、脂类代谢和非囊泡运输等, 对于个体的生长发育具有重要作用。近几年, 关于ORPs在哺乳动物和酵母(Saccharomyces cerevisiae)中结构和功能的研究取得了一系列重要进展, 但在植物中相关研究尚少。该文综述了ORPs及其相关蛋白在哺乳动物、酵母和植物中的研究进展, 探讨了植物ORPs的结构及其与哺乳动物和酵母同源蛋白之间的进化关系, 并对植物ORPs未来的研究方向进行了展望。

关键词: 氧化甾醇结合蛋白相关蛋白, 脂类运输, 膜结合位点

Abstract: Membrane lipids not only are important components of cell membranes, but also participate in signal transduction as signal molecules. The uneven distribution of lipid molecules in membranes requires specific types of transport channels and transporters for each lipid type. Oxysterol-binding protein (OSBP)-related proteins (ORPs) are a highly conserved family of lipid transport proteins that recognize and transport phosphoinositides and sterols, which are involved in many physiological processes including signal transduction, vesicle transport, lipid metabolism and non-vesicle transport, and hence play a very important role in the growth and development of individual organism. In recent years, a series of important findings have been made on the structure and function of ORPs in mammals and yeasts, but the advances in plants are relatively slow. In this paper, we review the progress of ORPs research in mammals, yeasts and plants, analyze the structural domains of ORPs in plants and the phylogenetical relationship to their homologs in mammals and yeasts, and also provide perspectives on the directions of plant ORPs research in the future.

Key words: oxysterol-binding protein-related proteins, lipid transport, membrane contact site

邹文娇, 葛磊, 予茜. 氧化甾醇结合蛋白相关蛋白家族的研究进展. 植物学报, 2021, 56(5): 627-640.

Wenjiao Zou, Lei Ge, Qian Yu. Research Advances in Oxysterol-binding Protein-related Proteins. Chinese Bulletin of Botany, 2021, 56(5): 627-640.

导出引用管理器 EndNote|Ris|BibTeX

链接本文: https://www.chinbullbotany.com/CN/10.11983/CBB21045

https://www.chinbullbotany.com/CN/Y2021/V56/I5/627

图/表 4

表1 动物及酵母中ORPs的亚细胞定位及功能

Table 1 Subcellular localization and function of ORPs in animal and yeast

蛋白	膜结合位点	运输脂类	参考文献
OSBP	ER (endoplasmic reticulum)- trans-Golgi	Cholesterol, PI4P	Mesmin et al., 2013
ORP1	ER-late endosome/lysomes	Cholesterol	Rocha et al., 2009; Kobuna et al., 2010; Vihervaara et al., 2011
ORP2	ER-lipid droplet, ER-PM (plasma membrane)	Cholesterol, PI(4,5)P2	Hynynen et al., 2009; Jansen et al., 2011; Weber-Boyvat et al., 2015b; Wang et al., 2019
ORP3	ER-PM	PI4P	Weber-Boyvat et al., 2015a; Gulyás et al., 2020
ORP4	Unknown	Cholesterol	Wyles et al., 2007
ORP5	ER-PM, ER-late endosome?	PS, PI4P, cholesterol, PI(4,5)P₂	Du et al., 2011; Chung et al., 2015; Ghai et al., 2017
ORP6	ER-PM	PI4P	Mochizuki et al., 2018
ORP7	Unknown	Unknown	None
ORP8	ER-PM, ER-mitochondrion	PS, PI4P	Chung et al., 2015; Ghai et al., 2017
ORP9	ER-trans-Golgi	Cholesterol, PI4P	Ngo and Ridgway, 2009; Liu and Ridgway, 2014
ORP10	Unknown	PS	Maeda et al., 2013
ORP11	trans-Golgi-late endosome	Unknown	Zhou et al., 2010
Osh1p	Nucleus-vacuole junction	Cholesterol, ergosterol, PI4P	Levine and Munro, 2001; Schulz et al., 2009
Osh2p	ER-PM	Cholesterol	Schulz et al., 2009
Osh3p	ER-PM	PI4P, Cholesterol	Schulz et al., 2009; Tong et al., 2013
Osh4p	ER-PM, ER-mitochondrion	Sterol, PI4P, PI(4,5) P₂	Raychaudhuri et al., 2006; Schulz et al., 2009; de Saint-Jean et al., 2011; von Filseck et al., 2015b
Osh5p	Unknown	Cholesterol	Schulz et al., 2009
Osh6p	ER-PM	PS, PI4P	Wang et al., 2005a; Maeda et al., 2013
Osh7p	ER-PM	PS, PI4P	Maeda et al., 2013

图1 氧化固醇结合蛋白(OSBP)在内质网和高尔基体之间膜结合位点转运胆固醇的功能模式图(改自Mesmin et al., 2013; Pietrangelo and Ridgway, 2018) OSBP通过FFAT基序与VAP27-A互作, 定位于内质网, 通过PH蛋白结构域定位在高尔基体。OSBP一般通过Coiled-coil结构域形成二聚体行使功能。ORD蛋白结构域在磷脂酰肌醇-4-磷酸(PI4P)逆行转运的驱动下, 将胆固醇从内质网转移到高尔基体。

Figure 1 Working model of oxysterol-binding protein (OSBP) function in cholesterol transportation at membrane contact site (MCS) between endoplasmic reticulum (ER) and trans-Golgi (modified from Mesmin et al., 2013; Pietrangelo and Ridgway, 2018) OSBP is located in ER by FFAT motif interacting with VAP27-A and in trans-Golgi by the PH domain. OSBP usually forms dimers through the Coiled-coil domain to play its role. The ORD domain could move cholesterol from the ER to trans-Golgi, driven by the retrograde transport of phosphatidylinositol-4-phosphate (PI4P).

图2 拟南芥ORPs家族成员进化树及蛋白结构域分析

Figure 2 Phylogenetic tree and protein domain analysis of Arabidopsis ORPs family

图3 拟南芥、人类和酵母ORPs氨基酸序列的进化分析拟南芥ORPs包括ORP1A、ORP1B、ORP1C、ORP1D、ORP2A、ORP2B、ORP3A、ORP3B、ORP3C、ORP4A、ORP4B和ORP4C; 酵母ORPs包括Osh1-7p; 人类ORPs包括OSBP和ORP1-11。

Figure 3 Phylogenetic analysis of ORPs in Arabidopsis thaliana, human and yeast Arabidopsis ORPs include ORP1A, ORP1B, ORP1C, ORP1D, ORP2A, ORP2B, ORP3A, ORP3B, ORP3C, ORP4A, ORP4B, and ORP4C; Yeast ORPs include Osh1-7p; Human ORPs include OSBP and ORP1-11.

参考文献 129

[1]	Amarilio R, Ramachandran S, Sabanay H, Lev S (2005). Differential regulation of endoplasmic reticulum structure through VAP-Nir protein interaction. J Biol Chem 280, 5934-5944. PMID
[2]	Anniss AM, Apostolopoulos J, Dworkin S, Purton LE, Sparrow RL (2002). An oxysterol-binding protein family identified in the mouse. DNA Cell Biol 21, 571-580. DOI URL
[3]	Balla T, Bondeva T, Varnai P (2000). How accurately can we image inositol lipids in living cells? Trends Pharmacol Sci 21, 238-241. PMID
[4]	Balla T, Kim YJ, Alvarez-Prats A, Pemberton J (2019). Lipid dynamics at contact sites between the endoplasmic reticulum and other organelles. Annu Rev Cell Dev Biol 35, 85-109. DOI URL
[5]	Beh CT, Cool L, Phillips J, Rine J (2001). Overlapping functions of the yeast oxysterol-binding protein homologues. Genetics 157, 1117-1140. PMID
[6]	Beh CT, Rine J (2004). A role for yeast oxysterol-binding protein homologs in endocytosis and in the maintenance of intracellular sterol-lipid distribution. J Cell Sci 117, 2983-2996. DOI URL
[7]	Berendzen KW, Böhmer M, Wallmeroth N, Peter S, Vesić M, Zhou Y, Tiesler FKE, Schleifenbaum F, Harter K (2012). Screening for in planta protein-protein interactions combining bimolecular fluorescence complementation with flow cytometry. Plant Methods 8, 25. PMID
[8]	Boutté Y, Grebe M (2009). Cellular processes relying on sterol function in plants. Curr Opin Plant Biol 12, 705-713. DOI URL
[9]	Chen HJ, Anagnostou G, Chai A, Withers J, Morris A, Adhikaree J, Pennetta G, de Belleroche JS (2010). Characterization of the properties of a novel mutation in VAPB in familial amyotrophic lateral sclerosis. J Biol Chem 285, 40266-40281. DOI URL
[10]	Chung J, Torta F, Masai K, Lucast L, Czapla H, Tanner LB, Narayanaswamy P, Wenk MR, Nakatsu F, De Camilli P (2015). PI4P/phosphatidylserine countertransport at ORP5- and ORP8-mediated ER-plasma membrane contacts. Science 349, 428-432.
[11]	Chung T (2019). How phosphoinositides shape autophagy in plant cells. Plant Sci 281, 146-158. DOI URL
[12]	D'Angelo G, Vicinanza M, De Matteis MA (2008). Lipid- transfer proteins in biosynthetic pathways. Curr Opin Cell Biol 20, 360-370. DOI URL
[13]	De Craene JO, Bertazzi DL, Bär S, Friant S (2017). Phosphoinositides, major actors in membrane trafficking and lipid signaling pathways. Int J Mol Sci 18, 634. DOI URL
[14]	De Saint-Jean M, Delfosse V, Douguet D, Chicanne G, Payrastre B, Bourguet W, Antonny B, Drin G (2011). Osh4p exchanges sterols for phosphatidylinositol 4-phosphate between lipid bilayers. J Cell Biol 195, 965-978. DOI PMID
[15]	Deeks MJ, Calcutt JR, Ingle EKS, Hawkins TJ, Chapman S, Richardson AC, Mentlak DA, Dixon MR, Cartwright F, Smertenko AP, Oparka K, Hussey PJ (2012). A superfamily of actin-binding proteins at the actin-membrane nexus of higher plants. Curr Biol 22, 1595-1600. DOI URL
[16]	Dong R, Saheki Y, Swarup S, Lucast L, Harper JW, De Camilli P (2016). Endosome-ER contacts control actin nucleation and retromer function through VAP-dependent regulation of PI4P. Cell 166, 408-423. DOI PMID
[17]	Du XM, Kumar J, Ferguson C, Schulz TA, Ong YS, Hong WJ, Prinz WA, Parton RG, Brown AJ, Yang HY (2011). A role for oxysterol-binding protein-related protein 5 in endosomal cholesterol trafficking. J Cell Biol 192, 121-135. DOI URL
[18]	Eisenberg-Bord M, Shai N, Schuldiner M, Bohnert M (2016). A tether is a tether is a tether: tethering at membrane contact sites. Dev Cell 39, 395-409. DOI PMID
[19]	Ferrer A, Altabella T, Arró M, Boronat A (2017). Emerging roles for conjugated sterols in plants. Prog Lipid Res 67, 27-37. DOI URL
[20]	Friedman JR, Voeltz GK (2011). The ER in 3D: a multifunctional dynamic membrane network. Trends Cell Biol 21, 709-717. DOI URL
[21]	Galmes R, Houcine A, van Vliet AR, Agostinis P, Jackson CL, Giordano F (2016). ORP5/ORP8 localize to endoplasmic reticulum-mitochondria contacts and are involved in mitochondrial function. EMBO Rep 17, 800-810. DOI URL
[22]	Gatta AT, Levine TP (2017). Piecing together the patchwork of contact sites. Trends Cell Biol 27, 214-229. DOI URL
[23]	Geldner N, Dénervaud-Tendon V, Hyman DL, Mayer U, Stierhof YD, Chory J (2009). Rapid, combinatorial analysis of membrane compartments in intact plants with a multicolor marker set. Plant J 59, 169-178. DOI URL
[24]	Geuns JMC (1983). Plant steroid hormones. Biochem Soc Trans 11, 543-548. DOI URL
[25]	Ghai R, Du XM, Wang H, Dong JQ, Ferguson C, Brown AJ, Parton RG, Wu JW, Yang HY (2017). ORP5 and ORP8 bind phosphatidylinositol-4,5-biphosphate (PtdIns (4,5)P₂) and regulate its level at the plasma membrane. Nat Commun 8, 757. DOI URL
[26]	Godi A, Di Campli A, Konstantakopoulos A, Di Tullio G, Alessi DR, Kular GS, Daniele T, Marra P, Lucocq JM, De Matteis MA (2004). FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P. Nat Cell Biol 6, 393-404. DOI URL
[27]	Guimil S, Dunand C (2007). Cell growth and differentiation in Arabidopsis epidermal cells. J Exp Bot 58, 3829-3840. PMID
[28]	Gulyás G, Sohn M, Kim YJ, Várnai P, Balla T (2020). ORP3 phosphorylation regulates phosphatidylinositol 4-phosphate and Ca²⁺ dynamics at plasma membrane-ER contact sites. J Cell Sci 133, jcs237388.
[29]	Harayama T, Riezman H (2018). Understanding the diversity of membrane lipid composition. Nat Rev Mol Cell Biol 19, 281-296. DOI URL
[30]	Heilmann I (2016). Phosphoinositide signaling in plant development. Development 143, 2044-2055. DOI PMID
[31]	Helle SCJ, Kanfer G, Kolar K, Lang A, Michel AH, Kornmann B (2013). Organization and function of membrane contact sites. Biochim Biophys Acta Mol Cell Res 1833, 2526-2541. DOI URL
[32]	Hong YY, Zhao J, Guo L, Kim SC, Deng XJ, Wang GL, Zhang GY, Li MY, Wang XM (2016). Plant phospholipases D and C and their diverse functions in stress responses. Prog Lipid Res 62, 55-74. DOI URL
[33]	Hynynen R, Suchanek M, Spandl J, Bäck N, Thiele C, Olkkonen VM (2009). OSBP-related protein 2 is a sterol receptor on lipid droplets that regulates the metabolism of neutral lipids. J Lipid Res 50, 1305-1315. DOI PMID
[34]	Ishikawa S, Nagai Y, Masuda T, Koga Y, Nakamura T, Imamura Y, Takamori H, Hirota M, Funakosi A, Fukushima M, Baba H (2010). The role of oxysterol binding protein-related protein 5 in pancreatic cancer. Cancer Sci 101, 898-905. DOI URL
[35]	Jansen M, Ohsaki Y, Rega LR, Bittman R, Olkkonen VM, Ikonen E (2011). Role of ORPs in sterol transport from plasma membrane to ER and lipid droplets in mammalian cells. Traffic 12, 218-231. DOI URL
[36]	Jaworski CJ, Moreira E, Li AG, Lee R, Rodriguez IR (2001). A family of 12 human genes containing oxysterol-binding domains. Genomics 78, 185-196. PMID
[37]	Jia Q, Kong DF, Li QH, Sun S, Song JL, Zhu YB, Liang KL, Ke QM, Lin WX, Huang JW (2019). The function of inositol phosphatases in plant tolerance to abiotic stress. Int J Mol Sci 20, 3999. DOI URL
[38]	Johansson M, Lehto M, Tanhuanpää K, Cover TL, Olkkonen VM (2005). The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments. Mol Biol Cell 16, 5480-5492. PMID
[39]	Johansson M, Rocha N, Zwart W, Jordens I, Janssen L, Kuijl C, Olkkonen VM, Neefjes J (2007). Activation of endosomal dynein motors by stepwise assembly of Rab7- RILP-p150^Glued, ORP1L, and the receptorβlll spectrin. J Cell Biol 176, 459-471. PMID
[40]	Kabashi E, El Oussini H, Bercier V, Gros-Louis F, Valdmanis PN, McDearmid J, Mejier IA, Dion PA, Dupre N, Hollinger D, Sinniger J, Dirrig-Grosch S, Camu W, Meininger V, Loeffler JP, René F, Drapeau P, Rouleau GA, Dupuis L (2013). Investigating the contribution of VAPB/ALS8 loss of function in amyotrophic lateral sclerosis. Hum Mol Genet 22, 2350-2360. DOI PMID
[41]	Kagiwada S, Hashimoto M (2007). The yeast VAP homolog Scs2p has a phosphoinositide-binding ability that is correlated with its activity. Biochem Biophys Res Commun 364, 870-876. DOI URL
[42]	Kagiwada S, Zen R (2003). Role of the yeast VAP homolog, Scs2p, in INO1 expression and phospholipid metabolism. J Biochem 133, 515-522. PMID
[43]	Kandutsch AA, Thompson EB (1980). Cytosolic proteins that bind oxygenated sterols. Cellular distribution, specificity, and some properties. J Biol Chem 255, 10813-10821. PMID
[44]	Kawano M, Kumagai K, Nishijima M, Hanada K (2006). Efficient trafficking of ceramide from the endoplasmic reticulum to the Golgi apparatus requires a VAMP-associated protein-interacting FFAT motif of CERT. J Biol Chem 281, 30279-30288. DOI URL
[45]	Ketelaar T, Allwood EG, Hussey PJ (2007). Actin organization and root hair development are disrupted by ethanol-induced overexpression of Arabidopsis actin interacting protein 1 (AIP1). New Phytol 174, 57-62. DOI PMID
[46]	Kobuna H, Inoue T, Shibata M, Gengyo-Ando K, Yamamoto A, Mitani S, Arai H (2010). Multivesicular body formation requires OSBP-related proteins and cholesterol. PLoS Genet 6, e1001055. DOI URL
[47]	Kun-Rodrigues C, Ganos C, Guerreiro R, Schneider SA, Schulte C, Lesage S, Darwent L, Holmans P, Singleton A, International Parkinson's Disease Genomics Consortium (IPDGC), Bhatia K, Bras J (2015). A systematic screening to identify de novo mutations causing sporadic early-onset Parkinson’s disease. Hum Mol Genet 24, 6711-6720. DOI PMID
[48]	Lagace TA, Byers DM, Cook HW, Ridgway ND (1997). Altered regulation of cholesterol and cholesteryl ester synthesis in Chinese-hamster ovary cells overexpressing the oxysterol-binding protein is dependent on the pleckstrin homology domain. Biochem J 326(Pt1), 205-213. DOI URL
[49]	Lehto M, Laitinen S, Chinetti G, Johansson M, Ehnholm C, Staels B, Ikonen E, Olkkonen VM (2001). The OSBP-related protein family in humans. J Lipid Res 42, 1203-1213. PMID
[50]	Lemmon MA (2003). Phosphoinositide recognition domains. Traffic 4, 201-213. PMID
[51]	Lemmon MA (2007). Pleckstrin homology (PH) domains and phosphoinositides. Biochem Soc Symp 74, 81-93. DOI URL
[52]	Lessmann E, Ngo M, Leitges M, Minguet S, Ridgway ND, Huber M (2007). Oxysterol-binding protein-related protein (ORP) 9 is a PDK-2 substrate and regulates Akt phosphorylation. Cell Signal 19, 384-392. PMID
[53]	Lev S, Halevy DB, Peretti D, Dahan N (2008). The VAP protein family: from cellular functions to motor neuron disease. Trends Cell Biol 18, 282-290. DOI URL
[54]	Levine T (2004). Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions. Trends Cell Biol 14, 483-490. PMID
[55]	Levine TP, Munro S (2001). Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein, to both the Golgi and the nucleus-vacuole junction. Mol Biol Cell 12, 1633-1644. PMID
[56]	Levine TP, Munro S (2002). Targeting of Golgi-specific pleckstrin homology domains involves both PtdIns 4-kinase- dependent and-independent components. Curr Biol 12, 695-704. DOI URL
[57]	Li DY, Inoue H, Takahashi M, Kojima T, Shiraiwa M, Takahara H (2008). Molecular characterization of a novel salt-inducible gene for an OSBP (oxysterol-binding protein)-homologue from soybean. Gene 407, 12-20. DOI URL
[58]	Li ZC, He YH (2020). Roles of brassinosteroids in plant reproduction. Int J Mol Sci 21, 872. DOI URL
[59]	Liu XW, Ridgway ND (2014). Characterization of the sterol and phosphatidylinositol 4-phosphate binding properties of Golgi-associated OSBP-related protein 9 (ORP9). PLoS One 9, e108368. DOI URL
[60]	Liu Y, Su Y, Wang XM (2013). Phosphatidic acid-mediated signaling. Adv Exp Med Biol 991, 159-176. DOI PMID
[61]	Loewen CJR, Roy A, Levine TP (2003). A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP. EMBO J 22, 2025-2035. DOI URL
[62]	Lundbæk JA, Collingwood SA, Ingólfsson HI, Kapoor R, Andersen OS (2010). Lipid bilayer regulation of membrane protein function: gramicidin channels as molecular force probes. J R Soc Interface 7, 373-395. DOI URL
[63]	Luo J, Yang HY, Song BL (2020). Mechanisms and regulation of cholesterol homeostasis. Nat Rev Mol Cell Biol 21, 225-245. DOI URL
[64]	Ma XH, Shor O, Diminshtein S, Yu L, Im YJ, Perera I, Lomax A, Boss WF, Moran N (2009). Phosphatidylinositol (4,5) bisphosphate inhibits K⁺-efflux channel activity in NT1 tobacco cultured cells. Plant Physiol 149, 1127-1140. DOI URL
[65]	Ma ZG, Liu ZH, Huang X (2010). OSBP- and FAN-mediated sterol requirement for spermatogenesis in Drosophila. Development 137, 3775-3784. DOI URL
[66]	Maeda K, Anand K, Chiapparino A, Kumar A, Poletto M, Kaksonen M, Gavin AC (2013). Interactome map uncovers phosphatidylserine transport by oxysterol-binding proteins. Nature 501, 257-261. DOI URL
[67]	Malinsky J, Opekarova M, Grossmann G, Tanner W (2013). Membrane microdomains, rafts, and detergent- resistant membranes in plants and fungi. Annu Rev Plant Biol 64, 501-529. DOI PMID
[68]	Manik MK, Yang H, Tong J, Im YJ (2017). Structure of yeast OSBP-related protein OSH1 reveals key determinants for lipid transport and protein targeting at the nucleus-vacuole junction. Structure 25, 617-629. DOI URL
[69]	Mao DX, Lin G, Tepe B, Zuo ZY, Tan KL, Senturk M, Zhang S, Arenkiel BR, Sardiello M, Bellen HJ (2019). VAMP associated proteins are required for autophagic and lysosomal degradation by promoting a PtdIns4P-medIated endosomal pathway. Autophagy 15, 1214-1233. DOI URL
[70]	Martin TF (2015). PI(4,5)P₂-binding effector proteins for vesicle exocytosis. Biochim Biophys Acta Mol Cell Biol Lipids 1851, 785-793.
[71]	Mesmin B, Bigay J, Polidori J, Jamecna D, Lacas-Ger-vais S, Antonny B (2017). Sterol transfer, PI4P consumption, and control of membrane lipid order by endogenous OSBP. EMBO J 36, 3156-3174. DOI PMID
[72]	Mesmin B, Bigay J, von Filseck JM, Lacas-Gervais S, Drin G, Antonny B (2013). A four-step cycle driven by PI(4)P hydrolysis directs sterol/PI(4)P exchange by the ER-Golgi tether OSBP. Cell 155, 830-843. DOI PMID
[73]	Mochizuki S, Miki H, Zhou RY, Kido Y, Nishimura W, Kikuchi M, Noda Y (2018). Oxysterol-binding protein- related protein (ORP) 6 localizes to the ER and ER- plasma membrane contact sites and is involved in the turnover of PI4P in cerebellar granule neurons. Exp Cell Res 370, 601-612. DOI PMID
[74]	Moreau P, Hartmann MA, Perret AM, Sturbois-Balcerzak B, Cassagne C (1998). Transport of sterols to the plasma membrane of leek seedlings. Plant Physiol 117, 931-937. PMID
[75]	Murphy SE, Levine TP (2016). VAP, a versatile access point for the endoplasmic reticulum: review and analysis of FFAT-like motifs in the VAPome. Biochim Biophys Acta Mol Cell Biol Lipids 1861, 952-961.
[76]	Ngo M, Ridgway ND (2009). Oxysterol binding protein- related protein 9 (ORP9) is a cholesterol transfer protein that regulates Golgi structure and function. Mol Biol Cell 20, 1388-1399. DOI URL
[77]	Nishimura AL, Mitne-Neto M, Silva HCA, Richieri-Costa A, Middleton S, Cascio D, Kok F, Oliveira JRM, Gillingwater T, Webb J, Skehel P, Zatz M (2004). A mutation in the vesicle-trafficking protein VAPB causes late-onset spinal muscular atrophy and amyotrophic lateral sclerosis. Am J Hum Genet 75, 822-831. PMID
[78]	Nishimura Y, Hayashi M, Inada H, Tanaka T (1999). Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-assocIated (VAMP-associated) proteins. Biochem Biophys Res Commun 254, 21-26. DOI URL
[79]	Petersen NH, Joensen J, McKinney LV, Brodersen P, Petersen M, Hofius D, Mundy J (2009). Identification of proteins interacting with Arabidopsis ACD11. J Plant Physiol 166, 661-666. DOI URL
[80]	Pietrangelo A, Ridgway ND (2018). Bridging the molecular and biological functions of the oxysterol-binding protein family. Cell Mol Life Sci 75, 3079-3098. DOI PMID
[81]	Raychaudhuri S, Im YJ, Hurley JH, Prinz WA (2006). Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositides. J Cell Biol 173, 107-119. PMID
[82]	Raychaudhuri S, Prinz WA (2010). The diverse functions of oxysterol-binding proteins. Annu Rev Cell Dev Biol 26, 157-177. DOI PMID
[83]	Rocha N, Kuijl C, van der Kant R, Janssen L, Houben D, Janssen H, Zwart W, Neefjes J (2009). Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150^Glued and late endosome positioning. J Cell Biol 185, 1209-1225. DOI PMID
[84]	Roy A, Levine TP (2004). Multiple pools of phosphatidylinositol 4-phosphate detected using the pleckstrin homology domain of Osh2p. J Biol Chem 279, 44683-44689. DOI URL
[85]	Rusten TE, Stenmark H (2006). Analyzing phosphoinositides and their interacting proteins. Nat Methods 3, 251-258. PMID
[86]	Saheki Y, De Camilli P (2017). Endoplasmic reticulum- plasma membrane contact sites. Annu Rev Biochem 86, 659-684. DOI URL
[87]	Saravanan RS, Slabaugh E, Singh VR, Lapidus LJ, Haas T, Brandizzi F (2009). The targeting of the oxysterol- binding protein ORP3a to the endoplasmic reticulum relies on the plant VAP33 homolog PVA12. Plant J 58, 817-830. DOI URL
[88]	Schaaf G, Ortlund EA, Tyeryar KR, Mousley CJ, Ile KE, Garrett TA, Ren JH, Woolls MJ, Raetz CRH, Redinbo MR, Bankaitis VA (2008). Functional anatomy of phospholipid binding and regulation of phosphoinositide homeostasis by proteins of the sec14 superfamily. Mol Cell 29, 191-206. DOI URL
[89]	Schulz TA, Choi MG, Raychaudhuri S, Mears JA, Ghirlando R, Hinshaw JE, Prinz WA (2009). Lipid-regulated sterol transfer between closely apposed membranes by oxysterol-binding protein homologues. J Cell Biol 187, 889-903. DOI URL
[90]	Skehel PA, Martin KC, Kandel ER, Bartsch D (1995). A VAMP-binding protein from Aplysia required for neurotransmitter release. Science 269, 1580-1583. PMID
[91]	Skirpan AL, Dowd PE, Sijacic P, Jaworski CJ, Gilroy S, Kao TH (2006). Identification and characterization of PiORP1, a Petunia oxysterol-binding-protein related protein involved in receptor-kinase mediated signaling in pollen, and analysis of the ORP gene family in Arabidopsis. Plant Mol Biol 61, 553-565. PMID
[92]	Soussan L, Burakov D, Daniels MP, Toister-Achituv M, Porat A, Yarden Y, Elazar Z (1999). ERG30, a VAP-33- related protein, functions in protein transport mediated by COPI vesicles. J Cell Biol 146, 301-312. PMID
[93]	Stefano G, Renna L, Wormsbaecher C, Gamble J, Zienkiewicz K, Brandizzi F (2018). Plant endocytosis requires the ER membrane-anchored proteins VAP27-1 and VAP27-3. Cell Rep 23, 2299-2307. DOI URL
[94]	Takáč T, Novák D, Šamaj J (2019). Recent advances in the cellular and developmental biology of phospholipases in plants. Front Plant Sci 10, 362. DOI URL
[95]	Takahashi D, Kawamura Y, Uemura M (2013). Changes of detergent-resistant plasma membrane proteins in oat and rye during cold acclimation: association with differential freezing tolerance. J Proteome Res 12, 4998-5011. DOI PMID
[96]	Tapken W, Murphy AS (2015). Membrane nanodomains in plants: capturing form, function, and movement. J Exp Bot 66, 1573-1586. DOI URL
[97]	Tarkowská D (2019). Plants are capable of synthesizing animal steroid hormones. Molecules 24, 2585. DOI URL
[98]	Taylor FR, Kandutsch AA (1985). [2] Use of oxygenated sterols to probe the regulation of 3-hydroxy-3-methylglutaryl-CoA reductase and sterologenesis. Methods Enzymol 110, 9-19.
[99]	Taylor FR, Saucier SE, Shown EP, Parish EJ, Kandutsch AA (1984). Correlation between oxysterol binding to a cytosolic binding protein and potency in the repression of hydroxymethylglutaryl coenzyme a reductase. J Biol Chem 259, 12382-12387. PMID
[100]	Tong JS, Yang H, Yang HY, Eom SH, Im YJ (2013). Structure of Osh3 reveals a conserved mode of phosphoinositide binding in oxysterol-binding proteins. Structure 21, 1203-1213. DOI URL
[101]	van der Kant R, Fish A, Janssen L, Janssen H, Krom S, Ho N, Brummelkamp T, Carette J, Rocha N, Neefjes J (2013). Late endosomal transport and tethering are coupled processes controlled by RILP and the cholesterol sensor ORP1L. J Cell Sci 126, 3462-3474. DOI PMID
[102]	van Meer G, Voelker DR, Feigenson GW (2008). Membrane lipids: where they are and how they behave. Nat Rev Mol Cell Biol 9, 112-124. DOI URL
[103]	Vihervaara T, Uronen RL, Wohlfahrt G, Björkhem I, Ikonen E, Olkkonen VM (2011). Sterol binding by OSBP- related protein 1L regulates late endosome motility and function. Cell Mol Life Sci 68, 537-551. DOI PMID
[104]	von Filseck JM, Čopič A, Delfosse V, Vanni S, Jackson CL, Bourguet W, Drin G (2015a). Phosphatidylserine transport by ORP/Osh proteins is driven by phosphatidylinositol 4-phosphate. Science 349, 432-436.
[105]	von Filseck JM, Vanni S, Mesmin B, Antonny B, Drin G (2015b). A phosphatidylinositol-4-phosphate powered exchange mechanism to create a lipid gradient between membranes. Nat Commun 6, 6671. DOI URL
[106]	Wang H, Ma QL, Qi YF, Dong JQ, Du XM, Rae J, Wang J, Wu WF, Brown AJ, Parton RG, Wu JW, Yang HY (2019a). ORP2 delivers cholesterol to the plasma membrane in exchange for phosphatidylinositol 4,5-bisphosphate (PI(4,5)P₂). Mol Cell 73, 458-473. DOI URL
[107]	Wang PH, Duan W, Munn AL, Yang HY (2005a). Molecular characterization of Osh6p, an oxysterol binding protein homolog in the yeast Saccharomyces cerevisiae. FEBS J 272, 4703-4715. DOI URL
[108]	Wang PW, Hawkins TJ, Richardson C, Cummins I, Deeks MJ, Sparkes I, Hawes C, Hussey PJ (2014). The plant cytoskeleton, NET3C, and VAP27 mediate the link between the plasma membrane and endoplasmic reticulum. Curr Biol 24, 1397-1405. DOI URL
[109]	Wang PW, Pleskot R, Zang JZ, Winkler J, Wang J, Yperman K, Zhang T, Wang K, Gong JL, Guan YJ, Richardson C, Duckney P, Vandorpe M, Mylle E, Fiserova J, Van Damme D, Hussey PJ (2019b). Plant AtEH/Pan1 proteins drive autophagosome formation at ER-PM contact sites with actin and endocytic machinery. Nat Commun 10, 5132. DOI URL
[110]	Wang PW, Richardson C, Hawkins TJ, Sparkes I, Hawes C, Hussey PJ (2016a). Plant VAP27 proteins: domain characterization, intracellular localization and role in plant development. New Phytol 210, 1311-1326. DOI URL
[111]	Wang PY, Weng J, Anderson RGW (2005b). OSBP is a cholesterol-regulated scaffolding protein in control of ERK1/2 activation. Science 307, 1472-1476. DOI URL
[112]	Wang WM, Liu PQ, Xu YJ, Xiao SY (2016b). Protein trafficking during plant innate immunity. J Integr Plant Biol 58, 284-298. DOI URL
[113]	Weber-Boyvat M, Kentala H, Lilja J, Vihervaara T, Hanninen R, Zhou Y, Peränen J, Nyman TA, Ivaska J, Olkkonen VM (2015a). OSBP-related protein 3 (ORP3) coupling with VAMP-associated protein A regulates R-Ras activity. Exp Cell Res 331, 278-291. DOI PMID
[114]	Weber-Boyvat M, Kentala H, Peränen J, Olkkonen VM (2015b). Ligand-dependent localization and function of ORP-VAP complexes at membrane contact sites. Cell Mol Life Sci 72, 1967-1987. DOI PMID
[115]	Wijdeven RH, Janssen H, Nahidiazar L, Janssen L, Jalink K, Berlin I, Neefjes J (2016). Cholesterol and ORP1L- mediated ER contact sites control autophagosome transport and fusion with the endocytic pathway. Nat Commun 7, 11808. DOI PMID
[116]	Wong LH, Gatta AT, Levine TP (2019). Lipid transfer proteins: the lipid commute via shuttles, bridges and tubes. Nat Rev Mol Cell Biol 20, 85-101. DOI URL
[117]	Wyles JP, McMaster CR, Ridgway ND (2002). Vesicle- associated membrane protein-associated protein-A (VAP- A) interacts with the oxysterol-binding protein to modify export from the endoplasmic reticulum. J Biol Chem 277, 29908-29918. DOI URL
[118]	Wyles JP, Perry RJ, Ridgway ND (2007). Characterization of the sterol-binding domain of oxysterol-binding protein (OSBP)-related protein 4 reveals a novel role in vimentin organization. Exp Cell Res 313, 1426-1437. DOI URL
[119]	Wyles JP, Ridgway ND (2004). VAMP-associated protein-A regulates partitioning of oxysterol-binding protein-related protein-9 between the endoplasmic reticulum and Golgi apparatus. Exp Cell Res 297, 533-547. DOI URL
[120]	Xing JJ, Zhang L, Duan ZK, Lin JX (2021). Coordination of phospholipid-based signaling and membrane trafficking in plant immunity. Trends Plant Sci 26, 407-420. DOI URL
[121]	Xue HW, Chen X, Mei Y (2009). Function and regulation of phospholipid signaling in plants. Biochem J 421, 145-156. DOI URL
[122]	Yan DG, Lehto M, Rasilainen L, Metso J, Ehnholm C, Ylä-Herttuala S, Jauhiainen M, Olkkonen VM (2007). Oxysterol binding protein induces upregulation of SREBP- 1c and enhances hepatic lipogenesis. Arterioscler Thromb Vasc Biol 27, 1108-1114. DOI URL
[123]	Yan DG, Mäyränpää MI, Wong J, Perttilä J, Lehto M, Jauhiainen M, Kovanen PT, Ehnholm C, Brown AJ, Olkkonen VM (2008). OSBP-related protein 8 (ORP8) suppresses ABCA1 expression and cholesterol efflux from macrophages. J Biol Chem 283, 332-340. DOI URL
[124]	Ye H, Ji CY, Guo RF, Jiang LW (2020). Membrane contact sites and organelles interaction in plant autophagy. Front Plant Sci 11, 477. DOI URL
[125]	Yu JW, Mendrola JM, Audhya A, Singh S, Keleti D, DeWald DB, Murray D, Emr SD, Lemmon MA (2004). Genome-wide analysis of membrane targeting by S. cerevisiae pleckstrin homology domains. Mol Cell 13, 677-688. DOI URL
[126]	Zauber H, Burgos A, Garapati P, Schulze WX (2014). Plasma membrane lipid-protein interactions affect signaling processes in sterol-biosynthesis mutants in Arabidopsis thaliana. Front Plant Sci 5, 78.
[127]	Zhou Y, Li SQ, Mäyränpää MI, Zhong WB, Bäck N, Yan DG, Olkkonen VM (2010). OSBP-related protein 11 (ORP11) dimerizes with ORP9 and localizes at the Golgi- late endosome interface. Exp Cell Res 316, 3304-3316. DOI PMID
[128]	Zhu DM, Zhang MD, Gao CJ, Shen JB (2020). Protein trafficking in plant cells: tools and markers. Sci China Life Sci 63, 343-363. DOI URL
[129]	Zhuang XH, Chung KP, Cui Y, Lin WL, Gao CJ, Kang BH, Jiang LW (2017). ATG9 regulates autophagosome progression from the endoplasmic reticulum in Arabidopsis. Proc Natl Acad Sci USA 114, E426-E435. DOI URL

氧化甾醇结合蛋白相关蛋白家族的研究进展

Research Advances in Oxysterol-binding Protein-related Proteins

RichHTML

PDF (PC)

可视化

被引次数

摘要/Abstract

引用本文

使用本文

图/表 4

参考文献 129

相关文章 0

编辑推荐

Metrics

本文评价