Search results for PLIN2

Showing 15 results out of 15

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Protein (7 results from a total of 7)

Identifier: R-HSA-400160
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: PLIN2: Q99541
Identifier: R-HSA-9613345
Species: Homo sapiens
Compartment: lipid droplet
Primary external reference: UniProt: Q99541
Identifier: R-HSA-9639397
Species: Homo sapiens
Compartment: lysosomal lumen
Primary external reference: UniProt: PLIN2: Q99541
Identifier: R-HSA-9613667
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: Q99541
Identifier: R-HSA-9613544
Species: Homo sapiens
Compartment: lipid droplet
Primary external reference: UniProt: Q99541
Identifier: R-HSA-9639398
Species: Homo sapiens
Compartment: late endosome lumen
Primary external reference: UniProt: Q99541
Identifier: R-HSA-9626054
Species: Homo sapiens
Compartment: lysosomal membrane
Primary external reference: UniProt: GFAP: P14136

DNA Sequence (1 results from a total of 1)

Identifier: R-HSA-5649938
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: ENSEMBL: ENSG00000147872

Reaction (6 results from a total of 6)

Identifier: R-HSA-1989770
Species: Homo sapiens
Compartment: nucleoplasm, plasma membrane
The Adipophilin (PLIN2) gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
Identifier: R-HSA-9613666
Species: Homo sapiens
Compartment: cytosol, lipid droplet
Lipophagy is the process of autophagic degradation of lipid droplets into fatty acids. Lipid droplets are coated with perilipin (PLIN) proteins and they need to be eliminated for the degradation of the lipids inside. Cytosolic Heat shock cognate 71 kDa protein (HSPA8) binds PLIN2 and PLIN3 on the lipid droplet surface. Subsequently, PRKAA2 binds and phosphorylates perilipins. Phosphorylated PLINs dissociate from PRKAA2 and are believed to translocate to the cytosol (S Kaushik et al. 2015, S Kaushik et al. 2016). Experiments suggesting this event were performed in mouse models.
Identifier: R-HSA-9613530
Species: Homo sapiens
Compartment: cytosol, lipid droplet
Lipophagy is the process of autophagic degradation of lipid droplets into fatty acids. Lipid droplets are coated with perilipin (PLIN) proteins and they need to be eliminated for the degradation of the lipids inside. Cytosolic Heat shock cognate 71 kDa protein (HSPA8) binds PLIN2 and PLIN3 on the lipid droplet surface. Subsequently, AMPK binds and phosphorylates perilipins targeting them for lipophagy (S Kaushik et al. 2015, S Kaushik et al. 2016). The precise phosphorylation site(s) on PLINs are unknown. Experiments confirming this finding were performed in mouse models.
Identifier: R-HSA-9613513
Species: Homo sapiens
Compartment: cytosol, lipid droplet
Lipophagy is the process of autophagic degradation of lipid droplets into fatty acids. Lipid droplets are coated with perilipin (PLIN) protiens and they need to be eliminated for the degradation of the lipids inside. Cytosolic Heat shock cognate 71 kDa protein (HSPA8) binds PLIN2 and PLIN3 on the lipid droplet surface. Consequently, PRKAA2 bind and phosphorylate perilipins targeting them for lipophagy (S Kaushik et al. 2015, S Kaushik et al. 2016). Experiments confirming this interaction were performed in mouse.
Identifier: R-HSA-9613565
Species: Homo sapiens
Compartment: cytosol, lipid droplet
Once phosphorylated, PLINs are believed to dissociate from PRKAA2 and translocate to the cytosol (S Kaushik et al. 2015, S Kaushik et al. 2016). The precise dissociation mechanism of Plins is unclear. The experiments showing this finding were performed in mouse models.
Identifier: R-HSA-9613352
Species: Homo sapiens
Compartment: cytosol, lipid droplet
Lipophagy is the process of autophagic degradation of lipid droplets into fatty acids. A key step in this process is the elimination of perilipin (PLIN) proteins on lipid droplet surface. This mechanism is initiated when the cytosolic Heat shock cognate 71 kDa protein (HSPA8) binds PLIN2 and PLIN3 on the lipid droplet surface. Consequently, perilipins are phosphorylated and targeted to degradation making the lipid available for hydrolysis (S Kaushik et al. 2015). Experiments confirming this interaction were performed in rats.

Icon (1 results from a total of 1)

Species: Homo sapiens
Graphic representation of Perilipin 2 and/or 3
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