Cargando…
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...
Autores principales: | Mysling, Simon, Kristensen, Kristian Kølby, Larsson, Mikael, Beigneux, Anne P, Gårdsvoll, Henrik, Fong, Loren G, Bensadouen, André, Jørgensen, Thomas JD, Young, Stephen G, Ploug, Michael |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4755760/ https://www.ncbi.nlm.nih.gov/pubmed/26725083 http://dx.doi.org/10.7554/eLife.12095 |
Ejemplares similares
-
The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1 counteracts this unfolding
por: Mysling, Simon, et al.
Publicado: (2016) -
Structure of the lipoprotein lipase–GPIHBP1 complex that mediates plasma triglyceride hydrolysis
por: Birrane, Gabriel, et al.
Publicado: (2019) -
Cooperative unfolding of distinctive mechanoreceptor domains transduces force into signals
por: Ju, Lining, et al.
Publicado: (2016) -
A protein of capillary endothelial cells, GPIHBP1, is crucial for plasma triglyceride metabolism
por: Young, Stephen G., et al.
Publicado: (2022) -
GPIHBP1 expression in gliomas promotes utilization of lipoprotein-derived nutrients
por: Hu, Xuchen, et al.
Publicado: (2019)