The road less traveled: modulating signal transduction enzymes by inhibiting their protein–protein interactions

2009 ◽  
Vol 13 (3) ◽  
pp. 284-290 ◽  
Author(s):  
Michelle R Arkin ◽  
Adrian Whitty
Keyword(s):  
Signal Transduction ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
The Road

scholarly journals Properties of the phage-shock-protein (Psp) regulatory complex that govern signal transduction and induction of the Psp response in Escherichia coli

Microbiology ◽  
2010 ◽  
Vol 156 (10) ◽  
pp. 2920-2932 ◽  
Author(s):  
Goran Jovanovic ◽  
Christoph Engl ◽  
Antony J. Mayhew ◽  
Patricia C. Burrows ◽  
Martin Buck
Keyword(s):  
Escherichia Coli ◽  
Signal Transduction ◽  
Protein Interactions ◽  
Leucine Zipper ◽  
Negative Control ◽  
Stress Conditions ◽  
Bacterial Cells ◽  
Protein Protein Interactions ◽  
Regulatory Complex ◽  
And Function

The phage-shock-protein (Psp) response maintains the proton-motive force (pmf) under extracytoplasmic stress conditions that impair the inner membrane (IM) in bacterial cells. In Escherichia coli transcription of the pspABCDE and pspG genes requires activation of σ 54-RNA polymerase by the enhancer-binding protein PspF. A regulatory network comprising PspF–A–C–B–ArcB controls psp expression. One key regulatory point is the negative control of PspF imposed by its binding to PspA. It has been proposed that under stress conditions, the IM-bound sensors PspB and PspC receive and transduce the signal(s) to PspA via protein–protein interactions, resulting in the release of the PspA–PspF inhibitory complex and the consequent induction of psp. In this work we demonstrate that PspB self-associates and interacts with PspC via putative IM regions. We present evidence suggesting that PspC has two topologies and that conserved residue G48 and the putative leucine zipper motif are determinants required for PspA interaction and signal transduction upon stress. We also establish that PspC directly interacts with the effector PspG, and show that PspG self-associates. These results are discussed in the context of formation and function of the Psp regulatory complex.

Protein-Protein Interactions in the Tetraspanin Web

Physiology ◽  
2005 ◽  
Vol 20 (4) ◽  
pp. 218-224 ◽  
Author(s):  
Shoshana Levy ◽  
Tsipi Shoham
Keyword(s):  
Signal Transduction ◽  
Cell Proliferation ◽  
Protein Interactions ◽  
Membrane Microdomains ◽  
Protein Protein Interactions ◽  
Host Parasite Interactions ◽  
Evolutionarily Conserved ◽  
And Migration ◽  
Host Parasite ◽  
Partner Proteins

Tetraspanins are evolutionarily conserved membrane proteins that tend to associate laterally with one another and to cluster dynamically with numerous partner proteins in membrane microdomains. Consequently, members of this family are involved in the coordination of intracellular and intercellular processes, including signal transduction; cell proliferation, adhesion, and migration; cell fusion; and host-parasite interactions.

scholarly journals Src homology region 2 domains direct protein-protein interactions in signal transduction.

1990 ◽  
Vol 87 (21) ◽  
pp. 8622-8626 ◽  
Author(s):  
M. F. Moran ◽  
C. A. Koch ◽  
D. Anderson ◽  
C. Ellis ◽  
L. England ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Homology Region ◽  
Src Homology

scholarly journals IP-FCM Measures Physiologic Protein-Protein Interactions Modulated by Signal Transduction and Small-Molecule Drug Inhibition

PLoS ONE ◽  
2012 ◽  
Vol 7 (9) ◽  
pp. e45722 ◽  
Author(s):  
Stephen E. P. Smith ◽  
Anya T. Bida ◽  
Tessa R. Davis ◽  
Hugues Sicotte ◽  
Steven E. Patterson ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Small Molecule ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Small Molecule Drug ◽  
Drug Inhibition

scholarly journals Spying on IgE receptor signaling

2005 ◽  
Vol 171 (3) ◽  
pp. 415-417
Author(s):  
Derek Toomre
Keyword(s):  
Signal Transduction ◽  
Protein Interactions ◽  
Lipid Raft ◽  
Correlation Spectroscopy ◽  
Receptor Signaling ◽  
Protein Protein Interactions ◽  
Ige Receptor ◽  
Fluorescent Correlation Spectroscopy ◽  
Controversial Topic ◽  
Lipid Raft Microdomains

Plasma membrane organization and the potential role, or not, of lipid raft microdomains in signal transduction is a controversial topic. Cross-correlation fluorescent correlation spectroscopy (CC-FCS) shows promise as a new approach to rapidly probe protein–protein interactions in living cells during signal transduction. CC-FCS data from studies of IgE receptor signaling challenge models of large stable lipid raft signaling domains and reveal a new complexity in the dynamic (re)organization of signaling complexes.

scholarly journals Unravelling the Initial Triggers of Botrytis cinerea Infection: First Description of Its Surfactome

2021 ◽  
Vol 7 (12) ◽  
pp. 1021
Author(s):  
Almudena Escobar-Niño ◽  
Rafael Carrasco-Reinado ◽  
Inés M. Morano ◽  
Jesús M. Cantoral ◽  
Francisco J. Fernandez-Acero
Keyword(s):  
Signal Transduction ◽  
Botrytis Cinerea ◽  
Protein Interactions ◽  
Environmental Changes ◽  
Surface Proteins ◽  
Phytopathogenic Fungus ◽  
Protein Protein Interactions ◽  
Front Line ◽  
Total Proteins ◽  
Potential Pathogenicity

Botrytis cinerea is a critically important phytopathogenic fungus, causing devastating crop losses; signal transduction cascades mediate the “dialogue” among the fungus, plant, and environment. Surface proteins play important roles as front-line receptors. We report the first description of the surfactome of a filamentous fungus. To obtain a complete view of these cascades during infection of B. cinerea, its surfactome has been described by optimization of the “shaving” process and LC–MS/MS at two different infection stages, and with both rapid and late responses to environmental changes. The best results were obtained using PBS buffer in the “shaving” protocol. The surfactome obtained comprises 1010 identified proteins. These have been categorized by gene ontology and protein–protein interactions to reveal new potential pathogenicity/virulence factors. From these data, the percentage of total proteins predicted for the genome of the fungus represented by proteins identified in this and other proteomics studies is calculated at 54%, a big increase over the previous 12%. The new data may be crucial for understanding better its biological activity and pathogenicity. Given its extensive exposure to plants and environmental conditions, the surfactome presents innumerable opportunities for interactions between the fungus and external elements, which should offer the best targets for fungicide development.

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