RBP4:atROL binds TTR

Stable Identifier
Reaction [binding]
Homo sapiens
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In the bloodstream, circulating retinol binding protein 4 (RBP4, in complex with atROL), binds transthyretin (TTR, a 51 kDa protein) in a 1:1 molar complex (Naylor & Newcomer, 1999). The resultant TTR:RBP4:atROL complex is larger and therefore less susceptible to glomerular filtration, maintaining normal levels of retinoid and RBP4 in the circulation. In TTR-deficient mice, plasma levels of atROL and RBP4 were observed to be 5% of wild type levels, highlighting the importance of TTR binding to RBP4:atROL (Episkopou et al. 1993). TTR is also a transporter for thyroxine in the brain (not shown here) (Herbert et al. 1986).
Literature References
PubMed ID Title Journal Year
3714052 Transthyretin: a choroid plexus-specific transport protein in human brain. The 1986 S. Weir Mitchell award

Herbert, J, Zeviani, M, Goodman, DS, Makover, A, Fremeau, RT, Dwork, A, Pham, KT, Soprano, DR, Wilcox, JN, Zimmerman, EA

Neurology 1986
10052934 The structure of human retinol-binding protein (RBP) with its carrier protein transthyretin reveals an interaction with the carboxy terminus of RBP

Naylor, HM, Newcomer, ME

Biochemistry 1999
8384721 Disruption of the transthyretin gene results in mice with depressed levels of plasma retinol and thyroid hormone

Robertson, EJ, Maeda, S, Gaitanaris, GA, Episkopou, V, Shimada, K, Gottesman, ME, Nishiguchi, S

Proc. Natl. Acad. Sci. U.S.A. 1993
Orthologous Events
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