The oxysterol-binding protein superfamily: New concepts and old proteins
dc.contributor.author | Villasmil, M. | |
dc.contributor.author | Bankaitis, V. | |
dc.contributor.author | Mousley, Carl | |
dc.date.accessioned | 2017-01-30T13:40:24Z | |
dc.date.available | 2017-01-30T13:40:24Z | |
dc.date.created | 2015-10-29T04:09:45Z | |
dc.date.issued | 2012 | |
dc.identifier.citation | Villasmil, M. and Bankaitis, V. and Mousley, C. 2012. The oxysterol-binding protein superfamily: New concepts and old proteins. Biochemical Society Transactions. 40 (2): pp. 469-473. | |
dc.identifier.uri | http://hdl.handle.net/20.500.11937/33949 | |
dc.identifier.doi | 10.1042/BST20120012 | |
dc.description.abstract |
The Kes1 OSBP (oxysterol-binding protein) is a key regulator of membrane trafficking through the TGN (trans-Golgi network) and endosomal membranes. We demonstrated recently that Kes1 acts as a sterolregulated rheostat for TGN/endosomal phosphatidylinositol 4-phosphate signalling. Kes1 utilizes its dual lipid-binding activities to integrate endosomal lipid metabolism with TORC1 (target of rapamycin complex 1)-dependent proliferative pathways and transcriptional control of nutrient signalling. ©The Authors Journal compilation ©2012 Biochemical Society. | |
dc.title | The oxysterol-binding protein superfamily: New concepts and old proteins | |
dc.type | Journal Article | |
dcterms.source.volume | 40 | |
dcterms.source.number | 2 | |
dcterms.source.startPage | 469 | |
dcterms.source.endPage | 473 | |
dcterms.source.issn | 0300-5127 | |
dcterms.source.title | Biochemical Society Transactions | |
curtin.department | School of Biomedical Sciences | |
curtin.accessStatus | Open access via publisher |
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