Associated Papers
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
The ER cholesterol sensor SCAP promotes CARTS biogenesis at ER-Golgi membrane contact sites.
Wakana Y et al.
The Journal of Cell Biology, 2021
Structural basis of sterol recognition by human hedgehog receptor PTCH1.
Qi C et al.
Science Advances, 2019
Retrospective on Cholesterol Homeostasis: The Central Role of Scap.
Brown MS et al.
Annual Review of Biochemistry, 2018
Deficiency in the Lipid Exporter ABCA1 Impairs Retrograde Sterol Movement and Disrupts Sterol Sensing at the Endoplasmic Reticulum.
Yamauchi Y et al.
The Journal of Biological Chemistry, 2015
Identification of twenty-three mutations in fission yeast Scap that constitutively activate SREBP.
Hughes AL et al.
Journal of Lipid Research, 2008
Mutations within the membrane domain of HMG-CoA reductase confer resistance to sterol-accelerated degradation.
Lee PC et al.
Journal of Lipid Research, 2007
Severe facial clefting in Insig-deficient mouse embryos caused by sterol accumulation and reversed by lovastatin.
Engelking LJ et al.
The Journal of Clinical Investigation, 2006
The sterol-sensing domain of the Niemann-Pick C1 (NPC1) protein regulates trafficking of low density lipoprotein cholesterol.
Millard EE et al.
The Journal of Biological Chemistry, 2005
Membrane topology of human insig-1, a protein regulator of lipid synthesis.
Feramisco JD et al.
The Journal of Biological Chemistry, 2004
The steroidal analog GW707 activates the SREBP pathway through disruption of intracellular cholesterol trafficking.
Zhang J et al.
Journal of Lipid Research, 2004
Three mutations in sterol-sensing domain of SCAP block interaction with insig and render SREBP cleavage insensitive to sterols.
Yabe D et al.
Proceedings of the National Academy of Sciences of the United States of America, 2002
The sterol-sensing domain: multiple families, a unique role?
Kuwabara PE et al.
Trends in Genetics : Tig, 2002
Distinct consequences of sterol sensor mutations in Drosophila and mouse patched homologs.
Johnson RL et al.
Developmental Biology, 2002
Niemann-pick type C1 (NPC1) overexpression alters cellular cholesterol homeostasis.
Millard EE et al.
The Journal of Biological Chemistry, 2000
Overexpression of membrane domain of SCAP prevents sterols from inhibiting SCAP.SREBP exit from endoplasmic reticulum.
Yang T et al.
The Journal of Biological Chemistry, 2000
Topological analysis of Niemann-Pick C1 protein reveals that the membrane orientation of the putative sterol-sensing domain is identical to those of 3-hydroxy-3-methylglutaryl-CoA reductase and sterol regulatory element binding protein cleavage-activating protein.
Davies JP et al.
The Journal of Biological Chemistry, 2000
Genomic structure of the gene encoding human 3-hydroxy-3-methyl-glutaryl coenzyme A reductase: comparison of exon/intron organization of sterol-sensing domains among four related genes.
Nakajima T et al.
Journal of Human Genetics, 2000
Mutations in the leucine zipper motif and sterol-sensing domain inactivate the Niemann-Pick C1 glycoprotein.
Watari H et al.
The Journal of Biological Chemistry, 1999
Genomic structure and chromosomal mapping of the human sterol regulatory element binding protein (SREBP) cleavage-activating protein (SCAP) gene.
Nakajima T et al.
Journal of Human Genetics, 1999
Sterols regulate processing of carbohydrate chains of wild-type SREBP cleavage-activating protein (SCAP), but not sterol-resistant mutants Y298C or D443N.
Nohturfft A et al.
Proceedings of the National Academy of Sciences of the United States of America, 1998
Isolation of cholesterol-requiring mutant Chinese hamster ovary cells with defects in cleavage of sterol regulatory element-binding proteins at site 1.
Rawson RB et al.
The Journal of Biological Chemistry, 1998
Niemann-Pick C1 disease gene: homology to mediators of cholesterol homeostasis.
Carstea ED et al.
Science (new York, N.y.), 1997
Cleavage site for sterol-regulated protease localized to a leu-Ser bond in the lumenal loop of sterol regulatory element-binding protein-2.
Duncan EA et al.
The Journal of Biological Chemistry, 1997
Recurrent G-to-A substitution in a single codon of SREBP cleavage-activating protein causes sterol resistance in three mutant Chinese hamster ovary cell lines.
Nohturfft A et al.
Proceedings of the National Academy of Sciences of the United States of America, 1996
Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein.
Hua X et al.
Cell, 1996