RBP3 regulates the transport of atROL from ROS to RPE

Stable Identifier
Reaction [uncertain]
Homo sapiens
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Although interphotoreceptor retinoid-binding protein (RBP3, IRBP) (Fong & Bridges 1988, Fong et al. 1990) is not required to move all-trans-retinol (atROL) from photoreceptor cells to the retinal pigment epithelium (RPE), it may function to regulate retinoid trafficking and possibly protect retinoids from biochemical damage. RBP3 is secreted by photoreceptor cells into the interphotoreceptor matrix (IPM), where, being a larger protein (135kDa) than the IPM space, becomes trapped (see mini-review Gonzalez-Fernandez & Ghosh 2008). It is through this space that retinoids move between the RPE and photoreceptor outer segments during the retinoid cycle. Once atROL enters the RPE, it binds with RBP1.

Literature References
PubMed ID Title Journal Year
3170584 Internal quadruplication in the structure of human interstitial retinol-binding protein deduced from its cloned cDNA

Bridges, CD, Fong, SL

J. Biol. Chem. 1988
2303470 Characterization and comparative structural features of the gene for human interstitial retinol-binding protein

Bridges, CD, Kedzie, KM, Fong, WB, Morris, TA, Fong, SL

J. Biol. Chem. 1990
Catalyst Activity

retinoid binding activity of RBP3 [extracellular region]

Orthologous Events
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