phosphorylated HSL dimer + FABP4 -> phosphorylated HSL dimer:FABP4 complex

Stable Identifier
R-HSA-163549
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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Rat FABPA associates with HSL and increases the rate of triacylglycerol hydrolysis, possibly by sequestering the released fatty acids (Shen et al. 1999; Shen et al. 2001). A similar association of HSL and FABP4 at the lipid droplet surface has been demonstrated in human adipocytes (Smith et al. 2004). The stoichiometry of the fatty acid:FABP complex is unknown. This model implies that HSL-associated FABP loaded with fatty acid should exchange with unloaded, unassociated FABP, allowing HSL to continue to work efficiently while moving newly generated fatty acids away from the lipid particle. To date, there is no evidence for or against such a shuttling process.

Literature References
PubMed ID Title Journal Year
15456755 Physical association between the adipocyte fatty acid-binding protein and hormone-sensitive lipase: a fluorescence resonance energy transfer analysis

Smith, AJ, Sanders, MA, Thompson, BR, Londos, C, Kraemer, FB, Bernlohr, DA

J Biol Chem 2004
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