OSBP Antibody

1. the component proteins of the machinery, OSBP, VAP, SAC1, and PITPNB, are all essential host factors for AiV replication. Importantly, the machinery is directly recruited to the RNA replication sites through previously unknown interactions of VAP/OSBP/SAC1 with the AiV proteins and with ACBD3. PMID: 29367253
2. results demonstrate that Sac1 expression in either the ER or Golgi apparatus has a minimal impact on the PI-4P that regulates OSBP activity or recruitment to contact sites PMID: 28471037
3. Cholesterol transfer, PI4P consumption, and control of membrane lipid order by endogenous OSBP have been described. PMID: 28978670
4. Data suggest that OSBP shifts the distribution of phosphatidylinositol 4-phosphate upon localization to endoplasmic reticulum-Golgi contact sites. PMID: 26601944
5. Our results identify OspB as a regulator of mTORC1 and mTORC1-dependent cell proliferation early during S. flexneri infection and establish a role for IQGAP1 in mTORC1 signaling PMID: 26473364
6. These results suggest that poliovirus proteins modulate PI4KB activity and provide PI4P for recruitment of OSBP to accumulate unesterified cholesterol on virus-induced membrane structure for formation of a virus replication complex. PMID: 24527995
7. OSBP-mediated back transfer of phosphatidylinositol 4-phosphate might coordinate the transfer of other lipid species at the endoplasmic reticulum-Golgi interface. PMID: 24209621
8. OSBP is required for efficient replication of intracellular S. Typhimurium. PMID: 21988961
9. Data indicate that phosphorylation on two serine-rich motifs, S381-S391 (site 1) and S192, S195, S200 (site 2), specifically controls oxysterol-binding protein (OSBP) activity at the endoplasmic reticulum (ER). PMID: 22875984
10. PKD negatively regulates HCV secretion/release by attenuating OSBP and CERT functions by phosphorylation inhibition. This study identifies the key role of the Golgi components in the HCV maturation process. PMID: 21285358
11. Results identify a novel substrate of protein kinase D at the Golgi, the oxysterol-binding protein OSBP. PMID: 20444975
12. This review summarizes recent evidence of sterol transfer activity by OSBP, suggesting seemingly disparate functions that could be the result of alterations in membrane sterol distribution or ancillary to this primary activity. PMID: 20545625
13. Electrostatic interaction between oxysterol-binding protein and VAMP-associated protein A revealed by NMR and mutagenesis studies. PMID: 20178991
14. OSBP was found to function as a cholesterol-binding scaffolding protein coordinating the activity of two phosphatases to control the extracellular signal-regulated kinase (ERK) signaling pathway PMID: 15746430
15. Regulation of ceramide transport protein by OSBP, sterols, and vesicle-associated protein reveals a novel mechanism for integrating sterol regulatory signals with ceramide transport and phingomyelin synthesis in the Golgi apparatus. PMID: 16571669
16. OSBP is able to sense both membrane cholesterol and oxidized sterols and link this information to the ERK1/2 signaling pathway. PMID: 18165705
17. functional role of OSBP in the HCV maturation process. PMID: 19570870

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HGNC: 8503

OMIM: 167040

KEGG: hsa:5007

STRING: 9606.ENSP00000263847

UniGene: Hs.597091