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An ATP-binding cassette protein from grape berry (VvABCC1) transports glucosylated anthocyanins.

Type of publication Peer-reviewed
Publikationsform Original article (peer-reviewed)
Publication date 2013
Author Francisco R, Regalado A, Agegeorges A, Burla B, Bassin B, Eisenach C, zarouk O, Chaves MM, Martinoia E, Nagy R,
Project ABC transporters involved in signalling events
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Original article (peer-reviewed)

Journal The Plant Cell
Volume (Issue) 25
Page(s) 1840 - 1854
Title of proceedings The Plant Cell
DOI doi/10.1105/tpc.112.102152

Open Access

Type of Open Access Publisher (Gold Open Access)


Accumulation of anthocyanins in the exocarp of red grapevine (Vitis vinifera) cultivars is one of several events that characterize the onset of grape berry ripening (véraison). Despite our thorough understanding of anthocyanin biosynthesis and regulation, little is known about the molecular aspects of their transport. The participation of ATP binding cassette (ABC) proteins in vacuolar anthocyanin transport has long been a matter of debate. Here, we present biochemical evidence that an ABC protein, ABCC1, localizes to the tonoplast and is involved in the transport of glucosylated anthocyanidins. ABCC1 is expressed in the exocarp throughout berry development and ripening, with a significant increase at véraison (i.e., the onset of ripening). Transport experiments using microsomes isolated from ABCC1-expressing yeast cells showed that ABCC1 transports malvidin 3-O- glucoside. The transport strictly depends on the presence of GSH, which is cotransported with the anthocyanins and is sensitive to inhibitors of ABC proteins. By exposing anthocyanin-producing grapevine root cultures to buthionine sulphoximine, which reduced GSH levels, a decrease in anthocyanin concentration is observed. In conclusion, we provide evidence that ABCC1 acts as an anthocyanin transporter that depends on GSH without the formation of an anthocyanin-GSH conjugate.