Search results for LDLR

Showing 21 results out of 49

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Protein (4 results from a total of 6)

Identifier: R-HSA-171053
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: LDLR: P01130
Identifier: R-HSA-171105
Species: Homo sapiens
Compartment: clathrin-coated endocytic vesicle membrane
Primary external reference: UniProt: P01130
Identifier: R-HSA-171127
Species: Homo sapiens
Compartment: endosome membrane
Primary external reference: UniProt: P01130
Identifier: R-HSA-6784818
Species: Homo sapiens
Compartment: endolysosome membrane
Primary external reference: UniProt: P01130

Reaction (4 results from a total of 27)

Identifier: R-HSA-171087
Species: Homo sapiens
Compartment: endosome membrane
LDL receptors in the endosome membrane are quickly returned to the cell surface (Goldstein et al. 1979).
Identifier: R-HSA-8863471
Species: Homo sapiens
Compartment: plasma membrane
Internalization of the low density lipoprotein receptor (LDLR) depends on the recognition of its atypical FDNPVY sequence by the CLASP (clathrin-associated sorting protein) LDLRAP1 (also known as ARH) and DAB2, which may be functionally redundant (Chen et al, 1990; Morris et al, 2001; Mishra et al, 2002a; He et al, 2002; Mishra et al, 2002b; Zhou et al, 2003; Mishra et al, 2005). Both DAB2 and LDLRAP1 also interact with both clathrin and AP-2 as well as with PI(4,5)P2 in the plasma membrane (Morris et al, 2001; Mishar et al, 2002a; He et al, 2002; Mishra et al, 2002b; Zhou et al, 2003). Consistent with the notion that cargo contributes to the regulation of CCP formation, overexpression of LDLR results in an increase in abortive CCP turnover, a decrease in the rate of CCP maturation and an increase in CCP size in an LDLRAP1- and DAB2-dependent manner (Mettlen et al, 2010).
Identifier: R-HSA-6784734
Species: Homo sapiens
Compartment: plasma membrane, extracellular region
PCSK9 (Proprotein convertase subtilisin/kexin type 9) binds to LDLR (Low-density lipoprotein receptor) on the cell surface. The binding site of PCSK9 has been localized to the epidermal growth factor-like repeat A (EGF-A) domain of the LDLR (Zhang et al. 2007). The complex PCSK9:LDLR is internalized via clathrin-mediated endocytosis and then routed to lysosomes via a mechanism that does not require ubiquitination and is distinct from the autophagy and proteosomal degradation pathways. In lysosomes, the affinity of the interaction between PCSK9 and LDLR dramatically increases. This promotes the final degradation of PCSK9 and LDLR without recycling. Monoclonal antibodies targeting PCSK9 have been shown to markedly reduce LDL cholesterol levels and are a novel treatment strategy for adults with hypercholesterolemia (Navarese et al. 2015).
Identifier: R-HSA-2424254
Species: Homo sapiens
Compartment: extracellular region, plasma membrane, early endosome
Chylomicron remnants (CRs) are "sieved" when they arrive at the liver by size, the appropriate sized remnants passing through the space of Disse. Once inside, CRs containing all-trans-retinyl esters (atREs) can be directly and rapidly taken up by liver parenchymal cells via the low-density lipoprotein receptor (LDLR) using apolipoprotein E (apoE) as a ligand. Internalization of remnants occur via endocytosis (see review D'Ambrosio et al. 2011). This reaction is inferred from uptake studies in mice (Yu et al. 2000). Defects in LDLR cause familial hypercholesterolemia (FH, MIM:143890), a common autosomal disease that affects about 1 in 500 people in most countries. Abnormal LDLR doesn't remove LDL from circulation resulting in high levels of LDL in blood, leading to early cardiovascular disease via atherosclerosis. The defect was first described by Brown and Goldstein (1974).

Complex (4 results from a total of 6)

Identifier: R-HSA-6784822
Species: Homo sapiens
Compartment: endolysosome membrane
Identifier: R-HSA-6784730
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-8862887
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-8869194
Species: Homo sapiens
Compartment: clathrin-coated endocytic vesicle membrane

Interactor (2 results from a total of 2)

Identifier: Q92673-PRO_0000033164
Species: Homo sapiens
Primary external reference: UniProt: Q92673-PRO_0000033164
Identifier: Q14696
Species: Homo sapiens
Primary external reference: UniProt: Q14696

Set (2 results from a total of 2)

Identifier: R-HSA-8862885
Species: Homo sapiens
Compartment: cytosol, plasma membrane
Identifier: R-HSA-8869153
Species: Homo sapiens
Compartment: clathrin-coated endocytic vesicle membrane, cytosol

Pathway (4 results from a total of 5)

Identifier: R-HSA-8866427
Species: Homo sapiens
The steps involved in proprotein convertase PCSK9-induced degradation of VLDLR are described here (Poirier et al. 2008). The rate of this catabolic process plays a clinically significant role in determining the efficiency of lipoprotein clearance from the blood.
Identifier: R-HSA-9031525
Species: Homo sapiens
Liver X receptors NR1H3 (LXR alpha) and NR1H2 (LXR beta) are sterol-responsive transcription factors that become activated upon the engagement with their cognate oxysterol ligands. Ligand-activated NR1H2 & NR1H3 induce a genetic program aimed at reducing the cellular sterol load by limiting cholesterol uptake, attenuating cholesterol biosynthesis and promoting cholesterol efflux. This Reactome module describes the NR1H2 & NR1H3-regulated expression of MYLIP (IDOL) gene, an E3 ubiquitin ligase, that triggers ubiquitination of the low-density lipoprotein receptor (LDLR) on its cytoplasmic domain, targeting it for degradation and thereby limiting cholesterol uptake (Zelcer N et al. 2009; Zhang L et al. 2012).
Identifier: R-HSA-8964043
Species: Homo sapiens
Circulating chylomicrons acquire molecules of apolipoproteins C and E and through interaction with endothelial lipases lose a large fraction of their triacylglycerol. These changes convert them to chylomicron remnants which bind to LDL receptors, primarily on the surfaces of liver cells, clearing them from the circulation (Redgrave 2004).
Most very-low-density lipoproteins (VLDL) are converted to low-density lipoproteins (LDL) (VLDL remodeling pathway). A small fraction are taken up by VLDL receptors on extrahepatic cells, as annotated here. Clearance of LDL from the blood involves binding to LDL receptors associated with coated pits at the cell surface, forming complexes that are internalized and passed via clathrin-coated vesicles to endosomes, where they dissociate. The LDL particles move into lysosomes and are degraded while the LDL receptors are returned to the cell surface. This process occurs in most cell types but is especially prominent in hepatocytes. It plays a major role in returning cholesterol from peripheral tissues to the liver (Hobbs et al. 1990).
Clearance of circulating HDL particles involves particle binding to cell-surface SR-BI receptors, particle disassembly with rlease of pre-beta HDL (Silver & Tall 2001), and uptake of the latter mediated by cell-surface CUBN:AMN complex (Kozyraki et al. 1999).
VLDLR internalization plays a clinically significant role in determining the efficiency of lipoprotein clearance from the blood (Poirier et al. 2008).
Identifier: R-HSA-8964026
Species: Homo sapiens
Circulating chylomicrons acquire molecules of apolipoproteins C and E and through interaction with endothelial lipases lose a large fraction of their triacylglycerol. These changes convert them to chylomicron remnants which bind to LDL receptors, primarily on the surfaces of liver cells, clearing them from the circulation.
This binding and clearance process involves several steps and requires the presence of heparan sulfate proteoglycan (HSPG)-associated hepatic lipase (HL). The molecular details of LDLR binding, and of the following steps of remnant endocytosis, are inferred from those of the coorresponding step of LDLR-mediated low-density lipoprotein (LDL) endocytosis (Redgrave 2004).

OtherEntity (1 results from a total of 1)

Identifier: R-ALL-450386
Compartment: cytosol
KSRP binds AU-rich elements in the following mRNAs: IL-8, LDLR, and NOS2 (iNOS). Binding of KSRP to the mRNA encoding Beta-catenin is inferred from mouse.
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