Phosphorylated HSL dimer translocates from the cytosol to the lipid particle

Stable Identifier
R-HSA-163554
Type
Reaction [omitted]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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In primary adipocytes from young rats and in adipocytes derived from 3T3-L1 cells in vitro, phosphorylated hormone-sensitive lipase (HSL) translocates from the cytosol to the surfaces of lipid droplets following the phosphorylation of perilipin (Clifford et al. 2000; Su et al. 2003; Sztalryd et al. 2003).

Recent studies have identified the structural domain of HSL that mediates its interaction with lipid droplets, and raise the possibility, not annotated here, that under some conditions unphosphorylated HSL can interact with lipid droplets (Peng et al. 2025).

The human reaction is inferred from the well-studied rat one.

Literature References
PubMed ID Title Journal Year
10671541 Translocation of hormone-sensitive lipase and perilipin upon lipolytic stimulation of rat adipocytes

Clifford, GM, Londos, C, Kraemer, FB, Vernon, RG, Yeaman, SJ

J Biol Chem 2000
12832420 Mutational analysis of the hormone-sensitive lipase translocation reaction in adipocytes

Su, CL, Sztalryd, C, Contreras, JA, Holm, C, Kimmel, AR, Londos, C

J Biol Chem 2003
40221426 Molecular determinants for the association of human hormone-sensitive lipase with lipid droplets

Peng, H, Xu, Q, Zhang, T, Zhu, J, Pan, J, Guan, X, Feng, S, Wu, J, Hu, Q

Nat Commun 2025
12810697 Perilipin A is essential for the translocation of hormone-sensitive lipase during lipolytic activation

Sztalryd, C, Xu, G, Dorward, H, Tansey, JT, Contreras, JA, Kimmel, AR, Londos, C

J Cell Biol 2003
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