The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1 counteracts this unfolding

The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1 counteracts this unfolding

Lipoprotein lipase (LPL) undergoes spontaneous inactivation via global unfolding and this unfolding is prevented by GPIHBP1 (Mysling et al., 2016). We now show: (1) that ANGPTL4 inactivates LPL by catalyzing the unfolding of its hydrolase domain; (2) that binding to GPIHBP1 renders LPL largely refra...

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Bibliographic Details
Main Authors: Simon Mysling, Kristian Kølby Kristensen, Mikael Larsson, Oleg Kovrov, André Bensadouen, Thomas JD Jørgensen, Gunilla Olivecrona, Stephen G Young, Michael Ploug
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2016-12-01
Series:eLife
Subjects:
HDX-MS
GPIHBP1
ANGTPL4
ANGTPL3
familial chylomicronemia
protein unfolding
Online Access:https://elifesciences.org/articles/20958

Internet

https://elifesciences.org/articles/20958

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