The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain

The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain

GPIHBP1 is a glycolipid-anchored membrane protein of capillary endothelial cells that binds lipoprotein lipase (LPL) within the interstitial space and shuttles it to the capillary lumen. The LPL•GPIHBP1 complex is responsible for margination of triglyceride-rich lipoproteins along capillaries and th...

Full description

Bibliographic Details
Main Authors: Simon Mysling, Kristian Kølby Kristensen, Mikael Larsson, Anne P Beigneux, Henrik Gårdsvoll, Loren G Fong, André Bensadouen, Thomas JD Jørgensen, Stephen G Young, Michael Ploug
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2016-01-01
Series:eLife
Subjects:
familial chylomicronemia
lipolysis
hyperlipidemia
intrinsically disordered protein
HDX-MS
surface plasmon resonance
Online Access:https://elifesciences.org/articles/12095

Internet

https://elifesciences.org/articles/12095

Similar Items