Oxysterol-binding protein homolog
From Proteopedia
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== Function == | == Function == | ||
| - | '''Oxysterol-binding protein homolog''' (Osh) mediate sterol transport from the ER to mitochondria. Sterols are synthesized in the ER and are present in membranes and affect the membrane fluidity and permeability<ref>PMID:29487131</ref>. | + | '''Oxysterol-binding protein homolog''' (Osh) mediate sterol transport from the ER to mitochondria. Sterols are synthesized in the ER and are present in membranes and affect the membrane fluidity and permeability<ref>PMID:29487131</ref>. '''Osh4''' or '''Kes1''' is involved in membrane and lipid trafficking through trans-Golgi network and endosomal systems<ref>PMID:22341443</ref>. |
== Disease == | == Disease == | ||
Revision as of 08:56, 28 November 2018
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3D structures of oxysterol-binding protein homolog
Updated on 28-November-2018
References
- ↑ Tian S, Ohta A, Horiuchi H, Fukuda R. Oxysterol-binding protein homologs mediate sterol transport from the endoplasmic reticulum to mitochondria in yeast. J Biol Chem. 2018 Apr 13;293(15):5636-5648. doi: 10.1074/jbc.RA117.000596. Epub, 2018 Feb 27. PMID:29487131 doi:http://dx.doi.org/10.1074/jbc.RA117.000596
- ↑ Mousley CJ, Yuan P, Gaur NA, Trettin KD, Nile AH, Deminoff SJ, Dewar BJ, Wolpert M, Macdonald JM, Herman PK, Hinnebusch AG, Bankaitis VA. A sterol-binding protein integrates endosomal lipid metabolism with TOR signaling and nitrogen sensing. Cell. 2012 Feb 17;148(4):702-15. doi: 10.1016/j.cell.2011.12.026. PMID:22341443 doi:http://dx.doi.org/10.1016/j.cell.2011.12.026
