The oxysterol-binding protein superfamily: New concepts and old proteins

Villasmil, M.; Bankaitis, V.; Mousley, Carl

doi:10.1042/BST20120012

Access Status

Open access via publisher

Authors

Villasmil, M.

Bankaitis, V.

Mousley, Carl

Date

2012

Type

Journal Article

Metadata

Show full item record

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.

Source Title

Biochemical Society Transactions

DOI

10.1042/BST20120012

ISSN

0300-5127

School

School of Biomedical Sciences

URI

http://hdl.handle.net/20.500.11937/33949

Collection

Curtin Research Publications

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.