Associated Papers
Ammonia stimulates SCAP/Insig dissociation and SREBP-1 activation to promote lipogenesis and tumour growth.
Cheng C et al.
Nature Metabolism, 2022
Structural advances in sterol-sensing domain-containing proteins.
Wu X et al.
Trends in Biochemical Sciences, 2022
Structural basis for sterol sensing by Scap and Insig.
Yan R et al.
Cell Reports, 2021
A structure of human Scap bound to Insig-2 suggests how their interaction is regulated by sterols.
Yan R et al.
Science (new York, N.y.), 2021
Retrospective on Cholesterol Homeostasis: The Central Role of Scap.
Brown MS et al.
Annual Review of Biochemistry, 2018
Point mutation in luminal loop 7 of Scap protein blocks interaction with loop 1 and abolishes movement to Golgi.
Zhang Y et al.
The Journal of Biological Chemistry, 2013
The sterol-sensing domain (SSD) directly mediates signal-regulated endoplasmic reticulum-associated degradation (ERAD) of 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase isozyme Hmg2.
Theesfeld CL et al.
The Journal of Biological Chemistry, 2011
Identification of twenty-three mutations in fission yeast Scap that constitutively activate SREBP.
Hughes AL et al.
Journal of Lipid Research, 2008
Intramembrane aspartic acid in SCAP protein governs cholesterol-induced conformational change.
Feramisco JD et al.
Proceedings of the National Academy of Sciences of the United States of America, 2005
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