scholarly journals ATP Site Ligands Determine the Assembly State of the Abelson Kinase Regulatory Core via the Activation Loop Conformation

2018 ◽  
Vol 140 (5) ◽  
pp. 1863-1869 ◽  
Author(s):  
Rajesh Sonti ◽  
Ines Hertel-Hering ◽  
Allan Joaquim Lamontanara ◽  
Oliver Hantschel ◽  
Stephan Grzesiek
Keyword(s):  
Activation Loop ◽  
Abelson Kinase ◽  
Loop Conformation

scholarly journals The structure of phosphorylated P38γ is monomeric and reveals a conserved activation-loop conformation

Structure ◽  
1999 ◽  
Vol 7 (9) ◽  
pp. 1057-1065 ◽  
Author(s):  
Steve Bellon ◽  
Matthew J Fitzgibbon ◽  
Ted Fox ◽  
Hsun-Mei Hsiao ◽  
Keith P Wilson
Keyword(s):  
Activation Loop ◽  
Loop Conformation

Cyclic Analogues of the Chemerin C-Terminus Mimic a Loop Conformation Essential for Activating the Chemokine-like Receptor 1

2021 ◽  
Vol 64 (6) ◽  
pp. 3048-3058
Author(s):  
Tobias F. Fischer ◽  
Clara T. Schoeder ◽  
Tristan Zellmann ◽  
Jan Stichel ◽  
Jens Meiler ◽  
...  
Keyword(s):  
C Terminus ◽  
Loop Conformation

scholarly journals Differential Role of Threonine and Tyrosine Phosphorylation in the Activation and Activity of the Yeast MAPK Slt2

2021 ◽  
Vol 22 (3) ◽  
pp. 1110
Author(s):  
Gema González-Rubio ◽  
Ángela Sellers-Moya ◽  
Humberto Martín ◽  
María Molina
Keyword(s):  
Cell Wall ◽  
Biological Activity ◽  
Biological Significance ◽  
Mitogen Activated Protein Kinase ◽  
Activation Loop ◽  
High Increase ◽  
Dual Specificity ◽  
Mitogen Activated Protein ◽  
Full Activation

The Mitogen-Activated Protein Kinase (MAPK) Slt2 is central to signaling through the yeast Cell Wall Integrity (CWI) pathway. MAPKs are regulated by phosphorylation at both the threonine and tyrosine of the conserved TXY motif within the activation loop (T190/Y192 in Slt2). Since phosphorylation at both sites results in the full activation of MAPKs, signaling through MAPK pathways is monitored with antibodies that detect dually phosphorylated forms. However, most of these antibodies also recognize monophosphorylated species, whose relative abundance and functionality are diverse. By using different phosphospecific antibodies and phosphate-affinity (Phos-tag) analysis on distinct Slt2 mutants, we determined that Y192- and T190-monophosphorylated species coexist with biphosphorylated Slt2, although most of the Slt2 pool remains unphosphorylated following stress. Among the monophosphorylated forms, only T190 exhibited biological activity. Upon stimulation, Slt2 is first phosphorylated at Y192, mainly by the MAPKK Mkk1, and this phosphorylation is important for the subsequent T190 phosphorylation. Similarly, dephosphorylation of Slt2 by the Dual Specificity Phosphatase (DSP) Msg5 is ordered, with dephosphorylation of T190 depending on previous Y192 dephosphorylation. Whereas Y192 phosphorylation enhances the Slt2 catalytic activity, T190 is essential for this activity. The conserved T195 residue is also critical for Slt2 functionality. Mutations that abolish the activity of Slt2 result in a high increase in inactive Y192-monophosphorylated Slt2. The coexistence of different Slt2 phosphoforms with diverse biological significance highlights the importance of the precise detection of the Slt2 phosphorylation status.

PLCε1 mediates one-lung ventilation injury by regulating the p38/RhoA/NFκB activation loop

2021 ◽  
Vol 133 ◽  
pp. 135-145
Author(s):  
Xin-Guo ◽  
Yong-Yang ◽  
Jia-Qin Ma ◽  
Xi-Zou ◽  
Li-Sha Li ◽  
...  
Keyword(s):  
Lung Ventilation ◽  
Activation Loop ◽  
One Lung Ventilation
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