Regulation of Phospholipid Methylation by Reversible Phosphorylation

1986 ◽  
pp. 89-99
Author(s):  
I. Varela ◽  
M. Pajares ◽  
I. Merida ◽  
M. Villalba ◽  
C. Cabrero ◽  
...  
Keyword(s):  
Reversible Phosphorylation

scholarly journals Reversible Phosphorylation and Kinase Cascades: the Work of Edwin G. Krebs

2005 ◽  
Vol 280 (43) ◽  
pp. e40-e42
Author(s):  
Nicole Kresge ◽  
Robert D. Simoni ◽  
Robert L. Hill
Keyword(s):  
Reversible Phosphorylation

scholarly journals De novo design of a reversible phosphorylation-dependent switch for membrane targeting

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Leon Harrington ◽  
Jordan M. Fletcher ◽  
Tamara Heermann ◽  
Derek N. Woolfson ◽  
Petra Schwille
Keyword(s):  
Protein Interactions ◽  
Lipid Membrane ◽  
De Novo ◽  
Protein Localization ◽  
Protein Structures ◽  
Spatiotemporal Pattern ◽  
Membrane Targeting ◽  
Protein Protein Interactions ◽  
Reversible Phosphorylation ◽  
Potential Applications

AbstractModules that switch protein-protein interactions on and off are essential to develop synthetic biology; for example, to construct orthogonal signaling pathways, to control artificial protein structures dynamically, and for protein localization in cells or protocells. In nature, the E. coli MinCDE system couples nucleotide-dependent switching of MinD dimerization to membrane targeting to trigger spatiotemporal pattern formation. Here we present a de novo peptide-based molecular switch that toggles reversibly between monomer and dimer in response to phosphorylation and dephosphorylation. In combination with other modules, we construct fusion proteins that couple switching to lipid-membrane targeting by: (i) tethering a ‘cargo’ molecule reversibly to a permanent membrane ‘anchor’; and (ii) creating a ‘membrane-avidity switch’ that mimics the MinD system but operates by reversible phosphorylation. These minimal, de novo molecular switches have potential applications for introducing dynamic processes into designed and engineered proteins to augment functions in living cells and add functionality to protocells.

How to tell the time: the regulation of phosphoenolpyruvate carboxylase in Crassulacean acid metabolism (CAM) plants

2003 ◽  
Vol 31 (3) ◽  
pp. 728-730 ◽  
Author(s):  
H.G. Nimmo
Keyword(s):  
Circadian Rhythms ◽  
Phosphoenolpyruvate Carboxylase ◽  
Crassulacean Acid Metabolism ◽  
Acid Metabolism ◽  
Circadian Oscillator ◽  
Cam Plants ◽  
Reversible Phosphorylation ◽  
Circadian Expression ◽  
Phosphoenolpyruvate Carboxylase Kinase ◽  
Co2 Metabolism

Crassulacean acid metabolism (CAM) plants exhibit persistent circadian rhythms of CO2 metabolism. These rhythms are driven by changes in the flux through phosphoenolpyruvate carboxylase, which is regulated by reversible phosphorylation in response to a circadian oscillator. This article reviews progress in our understanding of the circadian expression of phosphoenolpyruvate carboxylase kinase.

Enzymes Involved in the Reversible Phosphorylation in Microvessels of the Brain

1991 ◽  
pp. 137-141
Author(s):  
U. Dechert ◽  
M. Weber-Schaueffelen ◽  
S. Lang-Heinrich ◽  
E. Wollny
Keyword(s):  
Reversible Phosphorylation ◽  
The Brain

Reversible Phosphorylation in Glycogen and Starch

2021 ◽  
pp. 163-180
Author(s):  
Katherine J. Donohue ◽  
Andrea Kuchtova ◽  
Craig W. Vander Kooi ◽  
Matthew S. Gentry
Keyword(s):  
Reversible Phosphorylation
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