disruption of either TgACBP1 (acyl-CoA binding protein) or TgSCP2 caused no obviously phenotypic changes, whereas double disruption results in defects in intracellular growth and virulence to mice. TgACBP1 or TgSCP2 disruption alone leads to decreased abundance of C18:1, whereas double disruption results in reduced abundance of C18:1, C22:1, and C24:1. Loss of TgACBP1 and TgSCP2 cause serious defects in production of glycerides and phospholipids. Collectively, TgACBP1 and TgSCP2 play synergistic roles in lipid metabolism in Toxoplasma gondii
scp2 mutants are strongly attenuated in virulence and this defect manifested itself during penetration. Deletion of scp2 in Ustilago maydis interfers neither with growth nor with peroxisomal beta-oxidation
knockdown of scp2 does not interfere with the patterning of the kidney along its proximo-distal axis, but dramatically decreases the size of the kidney, in particular the proximal tubules. This phenotype is accompanied by a reduction of lipid rafts, but is independent of the peroxisomal or transcriptional activities of scp2. Disrupting lipid microdomains by inhibiting cholesterol synthesis phenocopies the defects seen in scp2 morphants
SCP2 is a binding protein for endocannbinoids N-arachidonylethanolamine and 2-arachidonoylglycerol. N-arachidonylethanolamine and 2-arachidonoylglycerol associate with SCP2 at a putative cholesterol binding pocket with DeltaG values of -3.6 and -4.6 kcal per mol, respectively. SCP2-mediated transfer of cholesterol in vitro is inhibited by micromolar concentrations of N-arachidonylethanolamine, and heterologous expression of SCP2 in HEK-293 cells increases time-related accumulation of N-arachidonylethanolamine in a temperature-dependent fashion
role of SCPX and SCP2 in intracellular cholesterol transport. Sterol carrier protein-2 is a nonspecific lipid-transfer protein in intracellular cholesterol trafficking in testicular Leydig cells
the role of the scp2 gene during plant colonization is analyzed. Virulence function for Scp2 during penetration that is probably carried out by Scp2 in peroxisomes