Mechanism of allosteric activation of glycogen phosphorylase probed by the reactivity of essential arginyl residues. Physicochemical and kinetic studies

Biochemistry ◽  
1980 ◽  
Vol 19 (15) ◽  
pp. 3634-3642 ◽  
Author(s):  
Marc Dreyfus ◽  
Bernard Vandenbunder ◽  
Henri Buc
Keyword(s):  
Glycogen Phosphorylase ◽  
Kinetic Studies ◽  
Allosteric Activation ◽  
Arginyl Residues

Identification of the molecular trigger for allosteric activation in glycogen phosphorylase

1994 ◽  
Vol 1 (5) ◽  
pp. 327-333 ◽  
Author(s):  
Michelle F. Browner ◽  
David Hackos ◽  
Robert Fletterick
Keyword(s):  
Glycogen Phosphorylase ◽  
Allosteric Activation

scholarly journals Architecture of human Rag GTPase heterodimers and their complex with mTORC1

Science ◽  
2019 ◽  
Vol 366 (6462) ◽  
pp. 203-210 ◽  
Author(s):  
Madhanagopal Anandapadamanaban ◽  
Glenn R. Masson ◽  
Olga Perisic ◽  
Alex Berndt ◽  
Jonathan Kaufman ◽  
...  
Keyword(s):  
Kinetic Studies ◽  
The Other ◽  
Allosteric Activation ◽  
Amino Acid Availability ◽  
Cryo Electron Microscopy ◽  
Gtp Binding ◽  
Regulate Cell Growth ◽  
Hotspot Mutations ◽  
Rag Gtpase ◽  
Cell Growth And Proliferation

The Rag guanosine triphosphatases (GTPases) recruit the master kinase mTORC1 to lysosomes to regulate cell growth and proliferation in response to amino acid availability. The nucleotide state of Rag heterodimers is critical for their association with mTORC1. Our cryo–electron microscopy structure of RagA/RagC in complex with mTORC1 shows the details of RagA/RagC binding to the RAPTOR subunit of mTORC1 and explains why only the RagAGTP/RagCGDP nucleotide state binds mTORC1. Previous kinetic studies suggested that GTP binding to one Rag locks the heterodimer to prevent GTP binding to the other. Our crystal structures and dynamics of RagA/RagC show the mechanism for this locking and explain how oncogenic hotspot mutations disrupt this process. In contrast to allosteric activation by RHEB, Rag heterodimer binding does not change mTORC1 conformation and activates mTORC1 by targeting it to lysosomes.

scholarly journals An Isozyme-specific Redox Switch in Human Brain Glycogen Phosphorylase Modulates Its Allosteric Activation by AMP

2016 ◽  
Vol 291 (46) ◽  
pp. 23842-23853 ◽  
Author(s):  
Cécile Mathieu ◽  
Romain Duval ◽  
Angélique Cocaign ◽  
Emile Petit ◽  
Linh-Chi Bui ◽  
...  
Keyword(s):  
Human Brain ◽  
Glycogen Phosphorylase ◽  
Allosteric Activation ◽  
Brain Glycogen ◽  
Redox Switch

scholarly journals An engineered liver glycogen phosphorylase with AMP allosteric activation

1991 ◽  
Vol 266 (24) ◽  
pp. 16113-16119
Author(s):  
W.S. Coats ◽  
M.F. Browner ◽  
R.J. Fletterick ◽  
C.B. Newgard
Keyword(s):  
Glycogen Phosphorylase ◽  
Liver Glycogen ◽  
Allosteric Activation
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