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Cholesterol homeostasis is regulated, at least in part, by sterol regulatory element (SRE)-binding proteins (e.g., SREBP1\; MIM 184756) and by liver X receptors (e.g., LXRA\; MIM 602423). Additionally we are shipping STARD4 Antibodies (28) and STARD4 Proteins (6) and many more products for this protein.
This study shows that nonvesicular sterol transport mechanisms and STARD4 in particular account for a large fraction of sterol transport between the plasma membrane and the ERC (show ERC1 ELISA Kits).
Studies show the 3 steroidogenic acute regulatory-related lipid transfer (START) domain proteins StarD4, StarD5 (show STARD5 ELISA Kits) and StarD6 (show STARD6 ELISA Kits) have a similar lipid binding pocket specific for sterols (cholesterol in particular), but differing regulation and localization.
The data indicate a role for STARD4 in nonvesicular transport of cholesterol from the plasma membrane and the endocytic recycling compartment to the endoplasmic reticulum and perhaps other intracellular compartments as well.
cholesterol transport mediated by STARD4 is an important component of the cholesterol homeostasis regulatory machinery
Study provide strong evidence for StarD4 as a highly regulated, non-vesicular, directional, intracellular transporter of cholesterol which plays a key role in the maintenance of intracellular cholesterol homeostasis.
StarD4-accelerated 7 alpha-OOH transfer to mitochondria resulted in greater susceptibility to free radical lipid peroxidation and loss of membrane potential than in a non-StarD4 control.
StarD4 is regulated by sterols via SREBP-2 (show SREBF2 ELISA Kits), and StarD5 (show STARD5 ELISA Kits) is activated by ER stress cholesterol metabolism; they serve different functions
Induction of STARD4 depended on both transcription factor ATF6 (show ATF6 ELISA Kits) and an ERSE-like element in its promoter.
StarD4 plays an important role as a directional cholesterol transporter in the maintenance of cellular cholesterol homeostasis
a model of STARD4 membrane interaction and sterol binding and release that requires dynamic movement of both the Omega1 loop and membrane insertion of the C-terminal alpha-helix.
StARD4's role can largely be compensated for by other intracellular cholesterol transporters.
Cholesterol homeostasis is regulated, at least in part, by sterol regulatory element (SRE)-binding proteins (e.g., SREBP1\; MIM 184756) and by liver X receptors (e.g., LXRA\; MIM 602423). Upon sterol depletion, LXRs are inactive and SREBPs are cleaved, after which they bind promoter SREs and activate genes involved in cholesterol biosynthesis and uptake. Sterol transport is mediated by vesicles or by soluble protein carriers, such as steroidogenic acute regulatory protein (STAR\; MIM 600617). STAR is homologous to a family of proteins containing a 200- to 210-amino acid STAR-related lipid transfer (START) domain, including STARD4 (Soccio et al., 2002
START domain containing 4 sterol-regulated
, START domain containing 4, sterol regulated
, START domain-containing protein 4
, stAR-related lipid transfer protein 4