SCAP
Description
The SCAP (SREBF chaperone) is a protein-coding gene located on chromosome 3.
SCAP is an abbreviation that can refer to multiple entities. In the context of human genes, SCAP stands for Sterol regulatory element-binding protein cleavage-activating protein. It plays a crucial role in regulating cholesterol and lipid homeostasis.
SCAP is a key player in cholesterol and lipid homeostasis. It escorts the SCAP-SREBP complex from the endoplasmic reticulum (ER) to the Golgi apparatus when cholesterol levels are low. This movement regulates the processing of sterol regulatory element-binding proteins (SREBPs), specifically SREBF1/SREBP1 and SREBF2/SREBP2. When cholesterol is abundant, SCAP forms a complex with INSIG (INSIG1 or INSIG2), masking the ER export signal and keeping the complex in the ER. However, when cholesterol is low, INSIG is released, triggering a conformational change in SCAP's SSD domain. This unmasks the ER export signal, allowing the SCAP-SREBP complex to enter COPII-coated vesicles and travel to the Golgi. In the Golgi, SREBPs are processed, releasing their transcription factor fragment, which then enters the nucleus and boosts the production of LDLR, INSIG1, and components of the mevalonate pathway. SCAP also directly binds cholesterol through its SSD domain.
SCAP is also known as -.