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{{Infobox_gene}}
{{PBB_Controls
'''Oxysterol-binding protein 1''' is a [[protein]] that in humans is encoded by the ''OSBP'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: OSBP oxysterol binding protein| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5007| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Oxysterol binding protein
| HGNCid = 8503
| Symbol = OSBP
| AltSymbols =; OSBP1
| OMIM = 167040
| ECnumber = 
| Homologene = 1919
| MGIid = 97447
| GeneAtlas_image1 = PBB_GE_OSBP_201800_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_OSBP_201799_s_at_tn.png
| Function = {{GNF_GO|id=GO:0008142 |text = oxysterol binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006869 |text = lipid transport}} {{GNF_GO|id=GO:0008202 |text = steroid metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5007
    | Hs_Ensembl = ENSG00000110048
    | Hs_RefseqProtein = NP_002547
    | Hs_RefseqmRNA = NM_002556
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 59098447
    | Hs_GenLoc_end = 59140193
    | Hs_Uniprot = P22059
    | Mm_EntrezGene = 76303
    | Mm_Ensembl = ENSMUSG00000024687
    | Mm_RefseqmRNA = XM_148904
    | Mm_RefseqProtein = XP_148904
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 12033160
    | Mm_GenLoc_end = 12061139
    | Mm_Uniprot = 
  }}
}}
'''Oxysterol binding protein''', also known as '''OSBP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: OSBP oxysterol binding protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5007| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Oxysterol-binding protein (OSBP) is an intracellular protein that was identified as a cytosolic 25-hydroxycholesterol-binding protein.<ref name="ridgway">{{cite journal | vauthors = Ridgway ND, Dawson PA, Ho YK, Brown MS, Goldstein JL | title = Translocation of oxysterol binding protein to Golgi apparatus triggered by ligand binding | journal = J. Cell Biol. | volume = 116 | issue = 2 | pages = 307–19 |date=January 1992 | pmid = 1730758 | pmc = 2289278 | doi = 10.1083/jcb.116.2.307| url = }}</ref> OSBP is a lipid transfer protein that controls cholesterol/PI4P exchange at ER-Golgi [[membrane contact site]]s.<ref name="Mesmin">{{cite journal | vauthors = Mesmin B, Bigay J, Moser von Filseck J, Lacas-Gervais S, Drin G, Antonny B | title = A Four-Step Cycle Driven by PI(4)P Hydrolysis Directs Sterol/PI(4)P Exchange by the ER-Golgi Tether OSBP | journal = Cell | volume = 155 | issue = 4 | pages = 830–43 |date=November 2013 | pmid = 24209621 | doi = 10.1016/j.cell.2013.09.056 }}</ref> 25-hydroxycholesterol acts as a natural inhibitor of this exchange. OSBP regulates ER-Golgi membrane contact sites formation by bridging ER and Golgi membranes together.<ref name="Mesmin" /> OSBP plays also a role as a sterol-regulated scaffolding protein for several cytosolic reactions including the phosphorylation of [[Extracellular signal-regulated kinases|ERK 1/2]].<ref name="wang">{{cite journal | vauthors = Wang PY, Weng J, Anderson RG | title = OSBP is a cholesterol-regulated scaffolding protein in control of ERK 1/2 activation | journal = Science | volume = 307 | issue = 5714 | pages = 1472–6 |date=March 2005 | pmid = 15746430 | doi = 10.1126/science.1107710 }}</ref>
{{PBB_Summary
| section_title =  
| summary_text = Oxysterol binding protein is an intracellular protein that is believed to transport sterols from lysosomes to the nucleus where the sterol down-regulates the genes for the LDL receptor, HMG-CoA reductase, and HMG synthetase<ref name="entrez">{{cite web | title = Entrez Gene: OSBP oxysterol binding protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5007| accessdate = }}</ref>
}}


==References==
It has been shown that expression and maturation of [[SREBP|SREBP-1c]] is controlled by OSBP.<ref name="pmid17303778">{{cite journal | vauthors = Yan D, Lehto M, Rasilainen L, Metso J, Ehnholm C, Ylä-Herttuala S, Jauhiainen M, Olkkonen VM | title = Oxysterol binding protein induces upregulation of SREBP-1c and enhances hepatic lipogenesis | journal = Arterioscler. Thromb. Vasc. Biol. | volume = 27 | issue = 5 | pages = 1108–14 |date=May 2007 | pmid = 17303778 | doi = 10.1161/ATVBAHA.106.138545 }}</ref> SREBP-1c is a major transcription factor for hepatic [[lipogenesis]] (fatty acids and triglycerides biosynthesis). OSBP expression levels in transgenic mice affect liver and serum TG levels.  OSBP is thought to be an essential scaffolding compound of the protein complex that regulates the activation state of the [[extracellular signal-regulated kinases|ERK]] protein.<ref name="wang"/> OSBP also acts as a sterol-dependant scaffold for the [[JAK2]] and [[STAT3]] proteins.<ref name="pmid18230613">{{cite journal | vauthors = Romeo GR, Kazlauskas A | title = Oxysterol and diabetes activate STAT3 and control endothelial expression of profilin-1 via OSBP1 | journal = J. Biol. Chem. | volume = 283 | issue = 15 | pages = 9595–605 |date=April 2008 | pmid = 18230613 | doi = 10.1074/jbc.M710092200 }}</ref>
{{reflist|2}}
 
==Further reading==
== Mechanism of action ==
{{refbegin | 2}}
 
{{PBB_Further_reading
OSBP is a multi-domain protein consisting of an N-terminal [[pleckstrin homology]] (PH) domain, a central [[FFAT motif]] (two phenylalanines in an acidic track), and a C-terminal lipid transport domain (ORD). The PH domain binds the trans-[[Golgi apparatus|Golgi]] membrane by contacting the lipid [[Phosphatidylinositol 4-phosphate|PI4P]] and the activated small G protein [[ADP ribosylation factor|Arf1]](-GTP), whereas the [[FFAT motif]] binds the type II ER membrane protein [[VAPA|VAP-A]].<ref name="pmid15350976">{{cite journal | author = Levine T | title = Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions | journal = Trends Cell Biol. | volume = 14 | issue = 9 | pages = 483–90 |date=September 2004 | pmid = 15350976 | doi = 10.1016/j.tcb.2004.07.017 }}</ref><ref name="pmid12023275">{{cite journal | vauthors = Wyles JP, McMaster CR, Ridgway ND | title = Vesicle-associated membrane protein-associated protein-A (VAP-A) interacts with the oxysterol-binding protein to modify export from the endoplasmic reticulum | journal = J. Biol. Chem. | volume = 277 | issue = 33 | pages = 29908–18 |date=August 2002 | pmid = 12023275 | doi = 10.1074/jbc.M201191200 | url = }}</ref> OSBP bridges the Golgi and the ER by establishing contacts with all of these determinants simultaneously.<ref name="Mesmin" />
| citations =  
 
*{{cite journal | author=Ridgway ND, Dawson PA, Ho YK, ''et al.'' |title=Translocation of oxysterol binding protein to Golgi apparatus triggered by ligand binding. |journal=J. Cell Biol. |volume=116 |issue= 2 |pages= 307-19 |year= 1992 |pmid= 1730758 |doi= }}
OSBP is thought to transport cholesterol from the ER to the Golgi, and to transport the phosphoinositide [[Phosphatidylinositol 4-phosphate|PI4P]] backward (from the Golgi to the ER).<ref name="Mesmin" /> Then, PI4P can be hydrolyzed by the phosphatidylinositide phosphatase [[SACM1L|SAC1]], which is an ER-resident protein. Therefore, OSBP acts as a negative regulator of its own attachment to the trans-Golgi (which requires the binding of its PH domain to PI4P). This negative feedback system might coordinate cholesterol transport out of the ER to PI4P level in the Golgi.
*{{cite journal | author=Levanon D, Hsieh CL, Francke U, ''et al.'' |title=cDNA cloning of human oxysterol-binding protein and localization of the gene to human chromosome 11 and mouse chromosome 19. |journal=Genomics |volume=7 |issue= 1 |pages= 65-74 |year= 1990 |pmid= 1970801 |doi= }}
 
*{{cite journal | author=Laitinen S, Olkkonen VM, Ehnholm C, Ikonen E |title=Family of human oxysterol binding protein (OSBP) homologues. A novel member implicated in brain sterol metabolism. |journal=J. Lipid Res. |volume=40 |issue= 12 |pages= 2204-11 |year= 2000 |pmid= 10588946 |doi= }}
== Regulation ==
*{{cite journal | author=Moreira EF, Jaworski C, Li A, Rodriguez IR |title=Molecular and biochemical characterization of a novel oxysterol-binding protein (OSBP2) highly expressed in retina. |journal=J. Biol. Chem. |volume=276 |issue= 21 |pages= 18570-8 |year= 2001 |pmid= 11278871 |doi= 10.1074/jbc.M011259200 }}
 
*{{cite journal | author=Jaworski CJ, Moreira E, Li A, ''et al.'' |title=A family of 12 human genes containing oxysterol-binding domains. |journal=Genomics |volume=78 |issue= 3 |pages= 185-96 |year= 2002 |pmid= 11735225 |doi= 10.1006/geno.2001.6663 }}
OSBP is regulated by PKD mediated phosphorylation, and by the oxysterol 25-hydroxycholesterol (25-OH), a high-affinity ligand for OSBP (~30 nM).<ref name="ridgway"/><ref name="pmid20444975">{{cite journal | vauthors = Nhek S, Ngo M, Yang X, Ng MM, Field SJ, Asara JM, Ridgway ND, Toker A | title = Regulation of oxysterol-binding protein Golgi localization through protein kinase D-mediated phosphorylation | journal = Mol. Biol. Cell | volume = 21 | issue = 13 | pages = 2327–37 |date=July 2010 | pmid = 20444975 | pmc = 2893995 | doi = 10.1091/mbc.E10-02-0090 }}</ref> Several proteins involved in cholesterol homeostasis, such as [[INSIG-1]] or [[Acyl-CoA:cholesterol acyltransferase|ACAT]], also bind 25-OH.<ref name="pmid17428920">{{cite journal | vauthors = Radhakrishnan A, Ikeda Y, Kwon HJ, Brown MS, Goldstein JL | title = Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: oxysterols block transport by binding to Insig | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 104 | issue = 16 | pages = 6511–8 |date=April 2007 | pmid = 17428920 | pmc = 1851665 | doi = 10.1073/pnas.0700899104 }}</ref> In fact 25-OH is a potent suppressor of sterol synthesis in cultured cells and accelerates cholesterol esterification. In cellular studies it has been shown that OSBP, initially cytosolic, relocates to ER-Golgi membrane contact sites in the presence of 25-OH.<ref name="ridgway"/> 25-OH acts as an inhibitor of sterol transport mediated by OSBP in vitro.<ref name="Mesmin"/>
*{{cite journal | author=Wyles JP, McMaster CR, Ridgway ND |title=Vesicle-associated membrane protein-associated protein-A (VAP-A) interacts with the oxysterol-binding protein to modify export from the endoplasmic reticulum. |journal=J. Biol. Chem. |volume=277 |issue= 33 |pages= 29908-18 |year= 2002 |pmid= 12023275 |doi= 10.1074/jbc.M201191200 }}
 
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
== Isoforms ==
*{{cite journal  | author=Beausoleil SA, Jedrychowski M, Schwartz D, ''et al.'' |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130-5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 }}
 
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
OSBP is the founding member of the [[Oxysterol-binding protein|ORP]] (OSBP-related proteins) family of lipid transfer proteins. Mammals have 16 different ORPs, whereas the yeast S. cerevisiae genome encodes seven ORP homologues (Osh). ORP and Osh proteins contain a lipid transport domain called ORD (OSBP-related domain) encompassing the EQVSHHPP signature sequence.<ref name="pmid16136145">{{cite journal | vauthors = Im YJ, Raychaudhuri S, Prinz WA, Hurley JH | title = Structural mechanism for sterol sensing and transport by OSBP-related proteins | journal = Nature | volume = 437 | issue = 7055 | pages = 154–8 |date=September 2005 | pmid = 16136145 | pmc = 1431608 | doi = 10.1038/nature03923 }}</ref> The ORD structure consists in a hydrophobic pocket. Because the EQVSHHPP sequence is crucial for PI4P binding to the ORD, but not for sterol binding, it has been proposed that PI4P transport is a common function of Osh/ORP proteins.<ref name="pmid22162133">{{cite journal | vauthors = de Saint-Jean M, Delfosse V, Douguet D, Chicanne G, Payrastre B, Bourguet W, Antonny B, Drin G | title = Osh4p exchanges sterols for phosphatidylinositol 4-phosphate between lipid bilayers | journal = J. Cell Biol. | volume = 195 | issue = 6 | pages = 965–78 |date=December 2011 | pmid = 22162133 | pmc = 3241724 | doi = 10.1083/jcb.201104062 }}</ref>
*{{cite journal  | author=Wang PY, Weng J, Anderson RG |title=OSBP is a cholesterol-regulated scaffolding protein in control of ERK 1/2 activation. |journal=Science |volume=307 |issue= 5714 |pages= 1472-6 |year= 2005 |pmid= 15746430 |doi= 10.1126/science.1107710 }}
 
*{{cite journal  | author=Perry RJ, Ridgway ND |title=Oxysterol-binding protein and vesicle-associated membrane protein-associated protein are required for sterol-dependent activation of the ceramide transport protein. |journal=Mol. Biol. Cell |volume=17 |issue= 6 |pages= 2604-16 |year= 2006 |pmid= 16571669 |doi= 10.1091/mbc.E06-01-0060 }}
== References ==
*{{cite journal  | author=Olsen JV, Blagoev B, Gnad F, ''et al.'' |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635-48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 }}
{{reflist|35em}}
}}
 
== Further reading ==
{{refbegin|35em}}
* {{cite journal | vauthors = Levanon D, Hsieh CL, Francke U, Dawson PA, Ridgway ND, Brown MS, Goldstein JL | title = cDNA cloning of human oxysterol-binding protein and localization of the gene to human chromosome 11 and mouse chromosome 19 | journal = Genomics | volume = 7 | issue = 1 | pages = 65–74 |date=May 1990 | pmid = 1970801 | doi = 10.1016/0888-7543(90)90519-Z }}
* {{cite journal | vauthors = Laitinen S, Olkkonen VM, Ehnholm C, Ikonen E | title = Family of human oxysterol binding protein (OSBP) homologues. A novel member implicated in brain sterol metabolism | journal = J. Lipid Res. | volume = 40 | issue = 12 | pages = 2204–11 |date=December 1999 | pmid = 10588946 | doi = }}
*{{cite journal | vauthors = Moreira EF, Jaworski C, Li A, Rodriguez IR | title = Molecular and biochemical characterization of a novel oxysterol-binding protein (OSBP2) highly expressed in retina | journal = J. Biol. Chem. | volume = 276 | issue = 21 | pages = 18570–8 |date=May 2001 | pmid = 11278871 | doi = 10.1074/jbc.M011259200 }}
* {{cite journal | vauthors = Jaworski CJ, Moreira E, Li A, Lee R, Rodriguez IR | title = A family of 12 human genes containing oxysterol-binding domains | journal = Genomics | volume = 78 | issue = 3 | pages = 185–96 |date=December 2001 | pmid = 11735225 | doi = 10.1006/geno.2001.6663 }}
* {{cite journal | vauthors = Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP | title = Large-scale characterization of HeLa cell nuclear phosphoproteins | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 101 | issue = 33 | pages = 12130–5 |date=August 2004 | pmid = 15302935 | pmc = 514446 | doi = 10.1073/pnas.0404720101 }}
* {{cite journal | vauthors = Perry RJ, Ridgway ND | title = Oxysterol-binding protein and vesicle-associated membrane protein-associated protein are required for sterol-dependent activation of the ceramide transport protein | journal = Mol. Biol. Cell | volume = 17 | issue = 6 | pages = 2604–16 |date=June 2006 | pmid = 16571669 | pmc = 1474796 | doi = 10.1091/mbc.E06-01-0060 }}
{{refend}}
{{refend}}
{{protein-stub}}
{{WikiDoc Sources}}

Latest revision as of 00:35, 7 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Oxysterol-binding protein 1 is a protein that in humans is encoded by the OSBP gene.[1]

Function

Oxysterol-binding protein (OSBP) is an intracellular protein that was identified as a cytosolic 25-hydroxycholesterol-binding protein.[2] OSBP is a lipid transfer protein that controls cholesterol/PI4P exchange at ER-Golgi membrane contact sites.[3] 25-hydroxycholesterol acts as a natural inhibitor of this exchange. OSBP regulates ER-Golgi membrane contact sites formation by bridging ER and Golgi membranes together.[3] OSBP plays also a role as a sterol-regulated scaffolding protein for several cytosolic reactions including the phosphorylation of ERK 1/2.[4]

It has been shown that expression and maturation of SREBP-1c is controlled by OSBP.[5] SREBP-1c is a major transcription factor for hepatic lipogenesis (fatty acids and triglycerides biosynthesis). OSBP expression levels in transgenic mice affect liver and serum TG levels. OSBP is thought to be an essential scaffolding compound of the protein complex that regulates the activation state of the ERK protein.[4] OSBP also acts as a sterol-dependant scaffold for the JAK2 and STAT3 proteins.[6]

Mechanism of action

OSBP is a multi-domain protein consisting of an N-terminal pleckstrin homology (PH) domain, a central FFAT motif (two phenylalanines in an acidic track), and a C-terminal lipid transport domain (ORD). The PH domain binds the trans-Golgi membrane by contacting the lipid PI4P and the activated small G protein Arf1(-GTP), whereas the FFAT motif binds the type II ER membrane protein VAP-A.[7][8] OSBP bridges the Golgi and the ER by establishing contacts with all of these determinants simultaneously.[3]

OSBP is thought to transport cholesterol from the ER to the Golgi, and to transport the phosphoinositide PI4P backward (from the Golgi to the ER).[3] Then, PI4P can be hydrolyzed by the phosphatidylinositide phosphatase SAC1, which is an ER-resident protein. Therefore, OSBP acts as a negative regulator of its own attachment to the trans-Golgi (which requires the binding of its PH domain to PI4P). This negative feedback system might coordinate cholesterol transport out of the ER to PI4P level in the Golgi.

Regulation

OSBP is regulated by PKD mediated phosphorylation, and by the oxysterol 25-hydroxycholesterol (25-OH), a high-affinity ligand for OSBP (~30 nM).[2][9] Several proteins involved in cholesterol homeostasis, such as INSIG-1 or ACAT, also bind 25-OH.[10] In fact 25-OH is a potent suppressor of sterol synthesis in cultured cells and accelerates cholesterol esterification. In cellular studies it has been shown that OSBP, initially cytosolic, relocates to ER-Golgi membrane contact sites in the presence of 25-OH.[2] 25-OH acts as an inhibitor of sterol transport mediated by OSBP in vitro.[3]

Isoforms

OSBP is the founding member of the ORP (OSBP-related proteins) family of lipid transfer proteins. Mammals have 16 different ORPs, whereas the yeast S. cerevisiae genome encodes seven ORP homologues (Osh). ORP and Osh proteins contain a lipid transport domain called ORD (OSBP-related domain) encompassing the EQVSHHPP signature sequence.[11] The ORD structure consists in a hydrophobic pocket. Because the EQVSHHPP sequence is crucial for PI4P binding to the ORD, but not for sterol binding, it has been proposed that PI4P transport is a common function of Osh/ORP proteins.[12]

References

  1. ↑ "Entrez Gene: OSBP oxysterol binding protein".
  2. ↑ 2.0 2.1 2.2 Ridgway ND, Dawson PA, Ho YK, Brown MS, Goldstein JL (January 1992). "Translocation of oxysterol binding protein to Golgi apparatus triggered by ligand binding". J. Cell Biol. 116 (2): 307–19. doi:10.1083/jcb.116.2.307. PMC 2289278. PMID 1730758.
  3. ↑ 3.0 3.1 3.2 3.3 3.4 Mesmin B, Bigay J, Moser von Filseck J, Lacas-Gervais S, Drin G, Antonny B (November 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 (4): 830–43. doi:10.1016/j.cell.2013.09.056. PMID 24209621.
  4. ↑ 4.0 4.1 Wang PY, Weng J, Anderson RG (March 2005). "OSBP is a cholesterol-regulated scaffolding protein in control of ERK 1/2 activation". Science. 307 (5714): 1472–6. doi:10.1126/science.1107710. PMID 15746430.
  5. ↑ Yan D, Lehto M, Rasilainen L, Metso J, Ehnholm C, Ylä-Herttuala S, Jauhiainen M, Olkkonen VM (May 2007). "Oxysterol binding protein induces upregulation of SREBP-1c and enhances hepatic lipogenesis". Arterioscler. Thromb. Vasc. Biol. 27 (5): 1108–14. doi:10.1161/ATVBAHA.106.138545. PMID 17303778.
  6. ↑ Romeo GR, Kazlauskas A (April 2008). "Oxysterol and diabetes activate STAT3 and control endothelial expression of profilin-1 via OSBP1". J. Biol. Chem. 283 (15): 9595–605. doi:10.1074/jbc.M710092200. PMID 18230613.
  7. ↑ Levine T (September 2004). "Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions". Trends Cell Biol. 14 (9): 483–90. doi:10.1016/j.tcb.2004.07.017. PMID 15350976.
  8. ↑ Wyles JP, McMaster CR, Ridgway ND (August 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 (33): 29908–18. doi:10.1074/jbc.M201191200. PMID 12023275.
  9. ↑ Nhek S, Ngo M, Yang X, Ng MM, Field SJ, Asara JM, Ridgway ND, Toker A (July 2010). "Regulation of oxysterol-binding protein Golgi localization through protein kinase D-mediated phosphorylation". Mol. Biol. Cell. 21 (13): 2327–37. doi:10.1091/mbc.E10-02-0090. PMC 2893995. PMID 20444975.
  10. ↑ Radhakrishnan A, Ikeda Y, Kwon HJ, Brown MS, Goldstein JL (April 2007). "Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: oxysterols block transport by binding to Insig". Proc. Natl. Acad. Sci. U.S.A. 104 (16): 6511–8. doi:10.1073/pnas.0700899104. PMC 1851665. PMID 17428920.
  11. ↑ Im YJ, Raychaudhuri S, Prinz WA, Hurley JH (September 2005). "Structural mechanism for sterol sensing and transport by OSBP-related proteins". Nature. 437 (7055): 154–8. doi:10.1038/nature03923. PMC 1431608. PMID 16136145.
  12. ↑ de Saint-Jean M, Delfosse V, Douguet D, Chicanne G, Payrastre B, Bourguet W, Antonny B, Drin G (December 2011). "Osh4p exchanges sterols for phosphatidylinositol 4-phosphate between lipid bilayers". J. Cell Biol. 195 (6): 965–78. doi:10.1083/jcb.201104062. PMC 3241724. PMID 22162133.

Further reading

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