VLDLR
Function
Multifunctional cell surface receptor that binds VLDL and transports it into cells by endocytosis and therefore plays an important role in energy metabolism. Binds also to a wide range of other molecules including Reelin/RELN or apolipoprotein E/APOE-containing ligands as well as clusterin/CLU (PubMed:24381170, PubMed:30873003). In the off-state of the pathway, forms homooligomers or heterooligomers with LRP8 (PubMed:30873003). Upon binding to ligands, homooligomers are rearranged to higher order receptor clusters that transmit the extracellular RELN signal to intracellular signaling processes by binding to DAB1 (PubMed:30873003). This interaction results in phosphorylation of DAB1 leading to the ultimate cell responses required for the correct positioning of newly generated neurons. Later, mediates a stop signal for migrating neurons, preventing them from entering the marginal zone (By similarity).
(Microbial infection) Acts as a receptor for Semliki Forest virus.
Involvement in disease
Cerebellar ataxia, impaired intellectual development, and dysequilibrium syndrome 1
CAMRQ1
An autosomal recessive, congenital, non-progressive cerebellar ataxia associated with disturbed equilibrium, delayed ambulation, intellectual disability, cerebellar hypoplasia and mild cerebral gyral simplification. Additional features include short stature, strabismus, pes planus and, rarely, seizures.
None
The disease is caused by variants affecting the gene represented in this entry.
Post-translational modifications
Ubiquitinated at Lys-839 by MYLIP leading to degradation.
Glycosylated.
Tissue Specificity
Abundant in heart and skeletal muscle; also ovary and kidney; not in liver.
Cellular localization
- Cell membrane
- Single-pass type I membrane protein
- Membrane
- Clathrin-coated pit
- Single-pass type I membrane protein
Alternative names
Very low-density lipoprotein receptor, VLDL receptor, VLDL-R, VLDLR