LRAT esterifies RBP1:atROL and FACYLs to atREs

Stable Identifier
Reaction [transition]
Homo sapiens
LRAT esterifies all-trans-retinol in RPE
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Lecithin retinol acyltransferase (LRAT) mediates the esterification of all-trans-retinol (atROL) to form all-trans-retinyl esters (atREs). atREs are stored in lipid droplet form called retinosomes (Imanishi et al. 2004). Cellular retinol-binding protein 1 (RBP1) is an effective donor of atROL for LRAT (Ruiz et al. 1999). LRAT is an important enzyme required for the clearance of atROL as it drives the uptake of atROL from the bloodstream through the receptor STRA6 (Kawaguchi et al. 2011) and clearance of atROL from rod outer segments (ROS). In addition, the esterified form of atROL serves as substrate for RPE65.

Literature References
PubMed ID Title Journal Year
15314061 Retinosomes: new insights into intracellular managing of hydrophobic substances in lipid bodies

Imanishi, Y, Gerke, V, Palczewski, K

J. Cell Biol. 2004
9920938 Molecular and biochemical characterization of lecithin retinol acyltransferase.

Rando, RR, Ruiz, A, Lim, YH, Gilbert, BA, Winston, A, Bok, D

J Biol Chem 1999
21774515 Receptor-mediated cellular uptake mechanism that couples to intracellular storage

Travis, GH, Yu, J, Ong, D, Cheng, G, Sun, H, Zhong, M, Yuan, Q, Jin, M, Ter-Stepanian, M, Kawaguchi, R

ACS Chem. Biol. 2011
Catalyst Activity

O-palmitoyltransferase activity of LRAT [endoplasmic reticulum membrane]

Orthologous Events
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