Transduction of biochemical signals across cell membranes

@article{Hendrickson2005TransductionOB,
  title={Transduction of biochemical signals across cell membranes},
  author={Wayne A. Hendrickson},
  journal={Quarterly Reviews of Biophysics},
  year={2005},
  volume={38},
  pages={321 - 330}
}
  • W. Hendrickson
  • Published 1 November 2005
  • Biology
  • Quarterly Reviews of Biophysics
1. Introduction 321 2. Tyrosine kinase receptors 322 3. Histidine kinase sensors 325 4. G-protein coupled receptors 327 5. Principles 328 6. Acknowledgments 329 7. References 330 Biological cells need to be responsive to various stimuli, primarily chemical ligands from their environments. Specific receptor molecules embedded in the plasma membrane detect the different biochemical signals that impact the cell, and these receptors are the conduits for transmission of this information to the cell… 
Membrane domain structures of three classes of histidine kinase receptors by cell-free expression and rapid NMR analysis
TLDR
Three backbone structures for the TM domains of the three classes of Escherichia coli histidine kinase receptors are determined consecutively within 8 months, offering insight into the abundant and underrepresented in the Protein Data Bank class of 2–4 TM crossers and demonstrating the efficiency of the CF combinatorial dual-labeling strategy.
Modeling Transmembrane Domain Dimers/Trimers of Plexin Receptors: Implications for Mechanisms of Signal Transmission across the Membrane
TLDR
This work pursued a strategy to predict helix oligomers that is based on packing considerations and is followed by a refinement of structures, utilizing microsecond all-atom molecular dynamics simulations to apply to plexin TM receptors, a family of 9 human proteins involved in the regulation of cell guidance and motility.
Symmetric signalling within asymmetric dimers of the Staphylococcus aureus receptor histidine kinase AgrC
TLDR
Results demonstrate that signalling through either individual AgrC protomer causes symmetric activation of both kinase domains and suggest that such signalling across the dimer interface may be an important mechanism for dimeric quorum‐sensing receptors to rapidly elicit a response upon signal detection.
A Bipartite Trigger for Dislocation Directs the Proteasomal Degradation of an Endoplasmic Reticulum Membrane Glycoprotein*
TLDR
The data support a model in which US2-mediated class I degradation occurs as a highly regulated process where the US2 transmembrane domain and cytoplasmic tail work in concert to eliminate class I molecules.
Creation of cross-linked bilayer membranes that can incorporate membrane proteins from oligo-Asp-based peptide gemini surfactants.
TLDR
The designed PG surfactants are a new class of bilayer-forming amphiphiles that may be applied to the study of various membrane proteins.
C4-dicarboxylates sensing mechanism revealed by the crystal structures of DctB sensor domain.
Bacterial Metabolism–Coupled Energetics
The Ron receptor tyrosine kinase in tissue morphogenesis.
TLDR
The author’s home country, the United States, and some of the authors’ relatives, have contributed to this work through the years.
...
...

References

SHOWING 1-10 OF 17 REFERENCES
Transmembrane signaling in bacterial chemoreceptors.
Crystal structure of rhodopsin: a G-protein-coupled receptor.
Heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors (GPCRs) respond to a variety of different external stimuli and activate G proteins. GPCRs share many structural
Structure of the entire cytoplasmic portion of a sensor histidine‐kinase protein
TLDR
The first crystal structure of the complete cytoplasmic region of a sensor HK is described, one from the thermophile Thermotoga maritima in complex with ADPβN at 1.9 Å resolution, which reveals previously unidentified functions for several conserved residues and reveals the relative disposition of domains in a state seemingly poised for phosphotransfer.
Molecular basis of transmembrane signalling by sensory rhodopsin II–transducer complex
TLDR
The X-ray structure of the complex between N. pharaonis SRII and the receptor-binding domain of HtrII at 1.94 Å resolution provides an atomic picture of the first signal transduction step, providing evidence for a common mechanism for this process in phototaxis and chemotaxis.
Interaction between proteins localized in membranes.
TLDR
It is calculated that the presence of other proteins at high concentrations and the high concentration and preoriented state of the reactive species can increase the likelihood of forming dimers 10(6)-fold and of forming trimers and higher oligomers many orders of magnitude greater.
The Ants Go Marching Two by Two: Oligomeric Structure of G-Protein-Coupled Receptors
TLDR
Experimental evidence supports the hypothesis that class A receptors may exist as higher-order oligomers, or even as arrays, with distinct symmetrical interfaces in both the first and fourth transmembrane segments.
Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation
TLDR
Comparisons with other kinase structures indicate that tyrosine phophophorylation and ligand binding may in general elicit two distinct hinge-like movements between the kinase subdomains, and a basis for inhibition by phosphorylation at Tyr 505 is suggested.
Structural interactions of fibroblast growth factor receptor with its ligands.
TLDR
The crystal structure, determined by multiwavelength anomalous diffraction analysis of the selenomethionyl protein, is a dimeric assemblage of 1:1 ligand:receptor complexes that provides a structural mechanism for FGF signal transduction.
Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase.
The structure of a 20-amino acid peptide inhibitor bound to the catalytic subunit of cyclic AMP-dependent protein kinase, and its interactions with the enzyme, are described. The x-ray crystal
...
...