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

Stable Identifier
R-RNO-163523
Type
Reaction [binding]
Species
Rattus norvegicus
Compartment
lipid droplet
ReviewStatus
5/5
General
SVG | 
PNG
Low
Medium
High
 | PPTX  | SBGN
phosphorylated HSL dimer + FABPA -> phosphorylated HSL dimer:FABPA complex
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
10318917 Interaction of rat hormone-sensitive lipase with adipocyte lipid-binding protein

Shen, WJ, Sridhar, K, Bernlohr, DA, Kraemer, FB

Proc Natl Acad Sci U S A 1999
11682468 Characterization of the functional interaction of adipocyte lipid-binding protein with hormone-sensitive lipase

Shen, WJ, Liang, Y, Hong, R, Patel, S, Natu, V, Sridhar, K, Jenkins, A, Bernlohr, DA, Kraemer, FB

J Biol Chem 2001
Participants
Input
Output
Orthologous Events
phosphorylated HSL dimer + FABP4 -> phosphorylated HSL dimer:FABP4 complex (Homo sapiens)
Authored
D'Eustachio, P  (2005-05-02)
Created
D'Eustachio, P  (2005-05-02)
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