Endogenous protein phosphorylation inEscherichia coli extracts

1982 ◽  
Vol 107 (3) ◽  
pp. 981-988 ◽  
Author(s):  
Mohamed Manaï ◽  
Alain J. Cozzone
Keyword(s):  
Protein Phosphorylation ◽  
Inescherichia Coli ◽  
Endogenous Protein

Endogenous protein phosphorylation and casein kinase activity during seed development in Araucaria angustifolia

2002 ◽  
Vol 61 (7) ◽  
pp. 835-842 ◽  
Author(s):  
Edna Lôbo Machado ◽  
Alba Chiesse da Silva ◽  
Márcio J da Silva ◽  
Adilson Leite ◽  
Laura M.M Ottoboni
Keyword(s):  
Protein Phosphorylation ◽  
Seed Development ◽  
Kinase Activity ◽  
Casein Kinase ◽  
Araucaria Angustifolia ◽  
Endogenous Protein

scholarly journals Hormone-induced protein phosphorylation. I. Relationship between secretagogue action and endogenous protein phosphorylation in intact cells from the exocrine pancreas and parotid.

1982 ◽  
Vol 95 (3) ◽  
pp. 903-908 ◽  
Author(s):  
S D Freedman ◽  
J D Jamieson
Keyword(s):  
Protein Phosphorylation ◽  
Exocrine Pancreas ◽  
Second Messengers ◽  
Intact Cells ◽  
Cholecystokinin Octapeptide ◽  
Phosphorylation Of Proteins ◽  
Endogenous Protein ◽  
Dose Dependent Fashion ◽  
Dose Dependent

We undertook studies to determine whether secretagogue action on the exocrine pancreas and parotid is accompanied by phosphorylation of proteins in intact cells. For this purpose, rat pancreatic, and parotid lobules were preincubated with 32Pi for 45 min at 37 degrees C, washed, and then incubated at 37 degrees C in the presence or absence of secretagogues that effect discharge through different second messengers. Among a variety of polypeptides exhibiting enhanced phosphorylation in pancreatic lobules upon a 30-s incubation in the presence of the secretagogues carbamylcholine, cholecystokinin octapeptide, or secretin, one species with an Mr of 29,000 was especially notable for three reasons: (a) its enhanced level of phosphorylation was dependent on the dose of secretagogue used and was still apparent after incubation for 30 min at 37 degrees C; (b) an analogous phosphorylated polypeptide was observed in isoproterenol-stimulated parotid lobules; and (c) in both tissues its selective dephosphorylation was observed upon termination of stimulation by administration of atropine to carbamylcholine-stimulated pancreatic lobules and propranolol to isoproterenol-stimulated parotid lobules. These results suggest that the phosphorylation of one protein with an Mr of 29,000 is closely correlated both temporally and in a dose-dependent fashion with secretagogue action in both the exocrine pancreas and parotid.

Modulation of endogenous protein phosphorylation in plant mitochondria by respiratory substrates

1990 ◽  
Vol 80 (4) ◽  
pp. 493-499 ◽  
Author(s):  
Patrice X. Petit ◽  
Marianne Sommarin ◽  
Christophe Pical ◽  
Ian M. Moller
Keyword(s):  
Protein Phosphorylation ◽  
Plant Mitochondria ◽  
Endogenous Protein

Polyamines stimulate endogenous protein phosphorylation in thyroid cytosol

1985 ◽  
Vol 133 (1) ◽  
pp. 354-360 ◽  
Author(s):  
Steven Levasseur ◽  
Thomas Poleck ◽  
Gerald Burke
Keyword(s):  
Protein Phosphorylation ◽  
Endogenous Protein

An engineered protein-phosphorylation toggle network with implications for endogenous network discovery

Science ◽  
2021 ◽  
Vol 373 (6550) ◽  
pp. eaav0780
Author(s):  
Deepak Mishra ◽  
Tristan Bepler ◽  
Brian Teague ◽  
Bonnie Berger ◽  
Jim Broach ◽  
...  
Keyword(s):  
Protein Phosphorylation ◽  
Biological Networks ◽  
Toggle Switch ◽  
Computational Framework ◽  
Cellular Processes ◽  
Network Discovery ◽  
Endogenous Protein ◽  
Synthetic Protein ◽  
Endogenous Networks ◽  
Cellular Behaviors

Synthetic biological networks comprising fast, reversible reactions could enable engineering of new cellular behaviors that are not possible with slower regulation. Here, we created a bistable toggle switch in Saccharomyces cerevisiae using a cross-repression topology comprising 11 protein-protein phosphorylation elements. The toggle is ultrasensitive, can be induced to switch states in seconds, and exhibits long-term bistability. Motivated by our toggle’s architecture and size, we developed a computational framework to search endogenous protein pathways for other large and similar bistable networks. Our framework helped us to identify and experimentally verify five formerly unreported endogenous networks that exhibit bistability. Building synthetic protein-protein networks will enable bioengineers to design fast sensing and processing systems, allow sophisticated regulation of cellular processes, and aid discovery of endogenous networks with particular functions.

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