Literature DB >> 27416800

Direct protein-protein interactions and substrate channeling between cellular retinoic acid binding proteins and CYP26B1.

Cara H Nelson1, Chi-Chi Peng1, Justin D Lutz1, Catherine K Yeung1, Alex Zelter2, Nina Isoherranen1.   

Abstract

Cellular retinoic acid binding proteins (CRABPs) bind all-trans-retinoic acid (atRA) tightly. This study aimed to determine whether atRA is channeled directly to cytochrome P450 (CYP) CYP26B1 by CRABPs, and whether CRABPs interact directly with CYP26B1. atRA bound to CRABPs (holo-CRABP) was efficiently metabolized by CYP26B1. Isotope dilution experiments showed that delivery of atRA to CYP26B1 in solution was similar with or without CRABP. Holo-CRABPs had higher affinity for CYP26B1 than free atRA, but both apo-CRABPs inhibited the formation of 4-OH-RA by CYP26B1. Similar protein-protein interactions between soluble binding proteins and CYPs may be important for other lipophilic CYP substrates.
© 2016 Federation of European Biochemical Societies.

Entities:  

Keywords:  binding proteins; cytochrome P450; retinoic acid; substrate channeling

Mesh:

Substances:

Year:  2016        PMID: 27416800      PMCID: PMC4997814          DOI: 10.1002/1873-3468.12303

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  24 in total

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