very-low-density lipoprotein particle receptor binding

Definition

Target type: molecularfunction

Binding to a very-low-density lipoprotein receptor. [GOC:BHF, GOC:mah]

Very-low-density lipoprotein (VLDL) particle receptor binding involves the interaction of VLDL particles with specific receptors on the surface of cells. VLDL particles are composed of triglycerides, cholesterol esters, phospholipids, and apolipoproteins, primarily apolipoprotein B-100 (apoB-100). The receptor responsible for VLDL binding is the low-density lipoprotein receptor (LDLR), which is a transmembrane protein expressed in various cell types, including liver, adipose tissue, and muscle. The LDLR recognizes and binds to apoB-100 on VLDL particles, initiating the process of VLDL uptake into cells. This binding event triggers a series of intracellular events, including receptor-mediated endocytosis. The VLDL particle is internalized within a coated pit, which then detaches from the cell surface and forms a vesicle. The vesicle moves through the cytoplasm and fuses with lysosomes, where the VLDL particle is broken down into its constituent components. The triglycerides and cholesterol esters are hydrolyzed, releasing free fatty acids and cholesterol, respectively. These components can be utilized by the cell for energy production or biosynthesis. The apoB-100 is degraded, and the LDLR is recycled back to the cell surface to bind more VLDL particles. VLDL receptor binding plays a crucial role in lipid metabolism, regulating the transport and clearance of triglycerides and cholesterol from the bloodstream. It is a complex process involving multiple steps and interactions between VLDL particles, receptors, and intracellular pathways.'
"

Proteins (1)

Compounds (2)