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Pregled bibliografske jedinice broj: 651794

Molecular characterization of zebrafish Oatp1d1 (Slco1d1), a novel Organic anion transporting polypeptide

Popović, Marta; Žaja, Roko; Fent, Karl; Smital, Tvrtko
Molecular characterization of zebrafish Oatp1d1 (Slco1d1), a novel Organic anion transporting polypeptide // The Journal of biological chemistry, 288 (2013), 47; 33894-33911 doi:10.1074/jbc.M113.518506 (međunarodna recenzija, članak, znanstveni)

Molecular characterization of zebrafish Oatp1d1 (Slco1d1), a novel Organic anion transporting polypeptide

Popović, Marta ; Žaja, Roko ; Fent, Karl ; Smital, Tvrtko

The Journal of biological chemistry (0021-9258) 288 (2013), 47; 33894-33911

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
OATP/Oatp; zebrafish Oatp1d1; phylogeny; substrate specificity; physiological role

Organic anion transporting polypeptide (OATP/Oatp) superfamily includes group of polyspecific transporters that mediate transport of large amphipathic, mostly anionic molecules across cell membranes of eukaryotes. OATPs/Oatps are involved in disposition and elimination of numerous physiological and foreign compounds. However, in non-mammalian species functional properties of Oatps remain unknown. We aimed to elucidate the role of Oatp1d1 in zebrafish to gain insights into the functional and structural evolution of the OATP1/Oatp1 superfamily. We show that diversification of the OATP1/Oatp1 family occurs after the emergence of jawed fish and that OATP1A/Oatp1a and OATP1B/Oatp1b subfamilies appeared at the root of tetrapods. The Oatp1d subfamily emerged in teleosts and is absent in tetrapods. The zebrafish Oatp1d1 is similar to mammalian OATP1A/Oatp1a and OATP1B/Oatp1b members, with the main physiological role in transport and balance of steroid hormones. Oatp1d1 activity is dependent upon pH gradient which could indicate bicarbonate exchange as a mode of transport. Our analysis of evolutionary conservation and structural properties revealed that: (i) H79 in the intracellular loop 3 is conserved within OATP1/Oatp1 family and is crucial for the transport activity ; (ii) N-glycosylation impacts membrane targeting and is conserved within the OATP1/Oatp1 family with N122, N133, N499 and N512 residues involved ; (iii) evolutionary conserved CRAC motif is important for membrane localization ; and (iv) Oatp1d1 is present in dimeric and possibly oligomeric form in the cell membrane. In conclusion, we describe the first detailed characterization of a new Oatp transporter in zebrafish, offering important insights into the functional evolution of OATP1/Oatp1 family and the physiological role of Oatp1d1.

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Znanstvena područja


Projekt / tema
098-0982934-2745 - Ekotoksikološko značenje ABC transportnih proteina u vodenih organizama (Tvrtko Smital, )

Institut "Ruđer Bošković", Zagreb

Časopis indeksira:

  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus