Protein phosphorylation regulates maize endosperm starch synthase IIa activity and protein−protein interactions

2021 ◽  
Author(s):  
Sahar Mehrpouyan ◽  
Usha Menon ◽  
Ian J. Tetlow ◽  
Michael J. Emes
Keyword(s):  
Protein Phosphorylation ◽  
Protein Interactions ◽  
Starch Synthase ◽  
Protein Protein Interactions ◽  
Maize Endosperm ◽  
Endosperm Starch

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

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

Glucan affinity of starch synthase IIa determines binding of starch synthase I and starch-branching enzyme IIb to starch granules

2012 ◽  
Vol 448 (3) ◽  
pp. 373-387 ◽  
Author(s):  
Fushan Liu ◽  
Nadya Romanova ◽  
Elizabeth A. Lee ◽  
Regina Ahmed ◽  
Martin Evans ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Protein Interactions ◽  
Starch Granule ◽  
Protein Complexes ◽  
Starch Synthase ◽  
Starch Granules ◽  
Branching Enzyme ◽  
Wild Type ◽  
Protein Protein Interactions ◽  
Starch Branching Enzyme

The sugary-2 mutation in maize (Zea mays L.) is a result of the loss of catalytic activity of the endosperm-specific SS (starch synthase) IIa isoform causing major alterations to amylopectin architecture. The present study reports a biochemical and molecular analysis of an allelic variant of the sugary-2 mutation expressing a catalytically inactive form of SSIIa and sheds new light on its central role in protein–protein interactions and determination of the starch granule proteome. The mutant SSIIa revealed two amino acid substitutions, one being a highly conserved residue (Gly522→Arg) responsible for the loss of catalytic activity and the inability of the mutant SSIIa to bind to starch. Analysis of protein–protein interactions in sugary-2 amyloplasts revealed the same trimeric assembly of soluble SSI, SSIIa and SBE (starch-branching enzyme) IIb found in wild-type amyloplasts, but with greatly reduced activities of SSI and SBEIIb. Chemical cross-linking studies demonstrated that SSIIa is at the core of the complex, interacting with SSI and SBEIIb, which do not interact directly with each other. The sugary-2 mutant starch granules were devoid of amylopectin-synthesizing enzymes, despite the fact that the respective affinities of SSI and SBEIIb from sugary-2 for amylopectin were the same as observed in wild-type. The data support a model whereby granule-bound proteins involved in amylopectin synthesis are partitioned into the starch granule as a result of their association within protein complexes, and that SSIIa plays a crucial role in trafficking SSI and SBEIIb into the granule matrix.

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).

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