SREBP cleavage-activating protein

Nakajima T, Ota N, Kodama T, Emi M. Isolation and radiation hybrid mapping of a highly polymorphic CA repeat sequence at the SREBP cleavage-activating protein (SCAP) locus. J Hum Genet 1999 44 350-351. 

FIGURE 21-43 SREBP activation. Sterol regulatory element-binding proteins (SREBPs, shown in green) are embedded in the ER when first synthesized, in a complex with the protein SREBP cleavage-activating protein (SCAP, red). (N and C represent the amino and carboxyl termini of the proteins.) When bound to SCAP, SREBPs are inactive. When... 

X. Hua, A. Nohturfft, J. L. Goldstein, and M. S. Brown. Sterol resistance in CHO cells traced to point mutation in SREBP cleavage activating protein, (SCAP). Cett, 87, 415-426, 1996. 

Nohturfft A, DeBose-Boyd RA, Scheek S, Goldstein JL, Brown MS. Sterols regulate cycling of SREBP cleavage-activating protein (SCAP) between endoplasmic reticulum and Golgi. Proc. Natl. Acad. Sci. U.S.A. 1999 96 11235-11240. 

Matsuda, M., Kom, B. S., Hammer, R. E., Moon, Y. A., Komuro, R., Horton, J. D., Goldstein, J. L., Brown, M. S., and Shimomura, I. SREBP cleavage-activating protein (SCAP) is required for increased Upid synthesis in liver induced by cholesterol deprivation and insulin elevation. Genes Dev 15 (2001) 1206-1216. 

Abbreviations a-BFAs anteiso-branched fatty acids AGP acyl carrier protein BHLH active soluble domain of SREBP CNS central nervous system DSD delta 5 desaturase D6D delta 6 desaturase ER endoplasmic reticulum Hik histidine kinase HUFA highly unsaturated fatty acid LXR liver X receptor MUFA monounsaturated fatty add NF-Y nuclear factor Y PLs phospholipids PP peroxisome proliferator PPAR PP-activated receptor PPRE PP response element PUFA polyunsaturated fatty acid PUFA-BP PUFA binding protein PUFA-RE PUFA response element RXR retinoid X receptor SCAP SREBP cleavage-activating protein SCD steraroyl CoA desaturase SFA saturated fatty acid SRE sterol response... 

SREBP cleavage activating protein (SCAP) A cholesterol-sensing protein that, in the absence of cholesterol, escorts SREBP from the endoplasmic reticulum to the Golgi, where it is proteolyticaUy activated. 

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