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Biochem Soc Trans. 2016 Apr 15;44(2):663-73. doi: 10.1042/BST20150128_2.

Correction: Learning from each other: ABC transporter regulation by protein phosphorylation in plant and mammalian systems.

Biochemical Society transactions

Bibek Aryal, Christophe Laurent, Markus Geisler

Affiliations

  1. Department of Biology-Plant Biology, University of Fribourg, Rue Albert Gockel 3, PER04, CH-1700 Fribourg, Switzerland.
  2. Department of Biology-Plant Biology, University of Fribourg, Rue Albert Gockel 3, PER04, CH-1700 Fribourg, Switzerland [email protected].

PMID: 27068986 DOI: 10.1042/BST20150128_2

Abstract

The ABC (ATP-binding cassette) transporter family in higher plants is highly expanded compared with those of mammalians. Moreover, some members of the plant ABCB subfamily display very high substrate specificity compared with their mammalian counterparts that are often associated with multidrug resistance (MDR) phenomena. In this review we highlight prominent functions of plant and mammalian ABC transporters and summarize our knowledge on their post-transcriptional regulation with a focus on protein phosphorylation. A deeper comparison of regulatory events of human cystic fibrosis transmembrane conductance regulator (CFTR) and ABCB1 from the model plantArabidopsisreveals a surprisingly high degree of similarity. Both physically interact with orthologues of the FK506-binding proteins (FKBPs) that chaperon both transporters to the plasma membrane in an action that seems to involve Hsp90. Further both transporters are phosphorylated at regulatory domains that connect both nucleotide-binding folds. Taken together it appears that ABC transporters exhibit an evolutionary conserved but complex regulation by protein phosphorylation, which apparently is, at least in some cases, tightly connected with protein-protein interactions (PPI).

© 2016 Authors; published by Portland Press Limited.

Keywords: ABCB; ATP-binding cassette (ABC) transporter regulation; FK506-binding protein (FKBP); P-glycoprotein; protein phosphorylation

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