Protein Phosphorylation and Protein-Protein Interactions

The ABC (ATP-binding cassette) transporter family in higher plants is highly expanded compared with those of mammalians. Moreover, some members of the plant ABC subfamily B (ABCB) display very high substrate specificity compared with their mammalian counterparts that are often associated with multi-drug resistance 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 plant Arabidopsis reveals a surprisingly high degree of similarity. Both physically interact with orthologues of the FK506-binding proteins that chaperon both transporters to the plasma membrane in an action that seems to involve heat shock protein (Hsp)90. Further, both transporters are phosphorylated at regulatory domains that connect both nt-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).

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Protein Phosphorylation in Amyloplasts Regulates Starch Branching Enzyme Activity and Protein–Protein Interactions

The Plant Cell ◽

10.1105/tpc.017400 ◽

2004 ◽

Vol 16 (3) ◽

pp. 694-708 ◽

Cited By ~ 240

Author(s):

Ian J. Tetlow ◽

Robin Wait ◽

Zhenxiao Lu ◽

Rut Akkasaeng ◽

Caroline G. Bowsher ◽

...

Keyword(s):

Enzyme Activity ◽

Protein Phosphorylation ◽

Protein Interactions ◽

Branching Enzyme ◽

Protein Protein Interactions ◽

Starch Branching Enzyme

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

Biochemical Society Transactions ◽

10.1042/bst20150128_2 ◽

2016 ◽

Vol 44 (2) ◽

pp. 663-673 ◽

Cited By ~ 2

Author(s):

Bibek Aryal ◽

Christophe Laurent ◽

Markus Geisler

Keyword(s):

Protein Phosphorylation ◽

Protein Interactions ◽

Abc Transporters ◽

Higher Plants ◽

Protein Protein Interactions ◽

Regulatory Domains ◽

Transporter Family ◽

Fk506 Binding Proteins ◽

Post Transcriptional Regulation ◽

High Degree

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 plant Arabidopsis reveals 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).

Download Full-text