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dc.contributor.authorVillasmil, M.
dc.contributor.authorBankaitis, V.
dc.contributor.authorMousley, Carl
dc.date.accessioned2017-01-30T13:40:24Z
dc.date.available2017-01-30T13:40:24Z
dc.date.created2015-10-29T04:09:45Z
dc.date.issued2012
dc.identifier.citationVillasmil, 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.urihttp://hdl.handle.net/20.500.11937/33949
dc.identifier.doi10.1042/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.titleThe oxysterol-binding protein superfamily: New concepts and old proteins
dc.typeJournal Article
dcterms.source.volume40
dcterms.source.number2
dcterms.source.startPage469
dcterms.source.endPage473
dcterms.source.issn0300-5127
dcterms.source.titleBiochemical Society Transactions
curtin.departmentSchool of Biomedical Sciences
curtin.accessStatusOpen access via publisher


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