Protein Phosphorylation and Protein-Protein Interactions

2002 ◽  
pp. 3-19
Author(s):  
Vincent Goffin ◽  
Paul A. Kelly
Keyword(s):  
Protein Phosphorylation ◽  
Protein Interactions ◽  
Protein Protein Interactions

scholarly journals The Bacterial Phosphoenolpyruvate:Carbohydrate Phosphotransferase System: Regulation by Protein Phosphorylation and Phosphorylation-Dependent Protein-Protein Interactions

2014 ◽  
Vol 78 (2) ◽  
pp. 231-256 ◽  
Author(s):  
Josef Deutscher ◽  
Francine Moussan Désirée Aké ◽  
Meriem Derkaoui ◽  
Arthur Constant Zébré ◽  
Thanh Nguyen Cao ◽  
...  
Keyword(s):  
Protein Phosphorylation ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Phosphotransferase System ◽  
Dependent Protein

scholarly journals Development of Bispecific Molecules for the In Situ Detection of Protein-Protein Interactions and Protein Phosphorylation

2014 ◽  
Vol 21 (3) ◽  
pp. 357-368 ◽  
Author(s):  
Jan van Dieck ◽  
Volker Schmid ◽  
Dieter Heindl ◽  
Sebastian Dziadek ◽  
Michael Schraeml ◽  
...  
Keyword(s):  
Protein Phosphorylation ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
In Situ Detection

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

2015 ◽  
Vol 43 (5) ◽  
pp. 966-974 ◽  
Author(s):  
Bibek Aryal ◽  
Christophe Laurent ◽  
Markus Geisler
Keyword(s):  
Protein Phosphorylation ◽  
Protein Interactions ◽  
Abc Transporters ◽  
Higher Plants ◽  
Multi Drug Resistance ◽  
Protein Protein Interactions ◽  
Regulatory Domains ◽  
Transporter Family ◽  
Hsp 90 ◽  
Post Transcriptional Regulation

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).

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

2004 ◽  
Vol 16 (3) ◽  
pp. 694-708 ◽  
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

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

2016 ◽  
Vol 44 (2) ◽  
pp. 663-673 ◽  
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).

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