The oxysterol-binding protein superfamily: New concepts and old proteins
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 d...
| Main Authors: | , , |
|---|---|
| Format: | Journal Article |
| Published: |
2012
|
| Online Access: | http://hdl.handle.net/20.500.11937/33949 |
| _version_ | 1848754087697317888 |
|---|---|
| author | Villasmil, M. Bankaitis, V. Mousley, Carl |
| author_facet | Villasmil, M. Bankaitis, V. Mousley, Carl |
| author_sort | Villasmil, M. |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | 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. |
| first_indexed | 2025-11-14T08:34:50Z |
| format | Journal Article |
| id | curtin-20.500.11937-33949 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T08:34:50Z |
| publishDate | 2012 |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-339492023-02-22T06:24:18Z The oxysterol-binding protein superfamily: New concepts and old proteins Villasmil, M. Bankaitis, V. Mousley, Carl 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. 2012 Journal Article http://hdl.handle.net/20.500.11937/33949 10.1042/BST20120012 unknown |
| spellingShingle | Villasmil, M. Bankaitis, V. Mousley, Carl The oxysterol-binding protein superfamily: New concepts and old proteins |
| title | The oxysterol-binding protein superfamily: New concepts and old proteins |
| title_full | The oxysterol-binding protein superfamily: New concepts and old proteins |
| title_fullStr | The oxysterol-binding protein superfamily: New concepts and old proteins |
| title_full_unstemmed | The oxysterol-binding protein superfamily: New concepts and old proteins |
| title_short | The oxysterol-binding protein superfamily: New concepts and old proteins |
| title_sort | oxysterol-binding protein superfamily: new concepts and old proteins |
| url | http://hdl.handle.net/20.500.11937/33949 |