Evolution of Hormone-Receptor Complexity by Molecular Exploitation

@article{Bridgham2006EvolutionOH,
  title={Evolution of Hormone-Receptor Complexity by Molecular Exploitation},
  author={Jamie T. Bridgham and Sean M. Carroll and Joseph W. Thornton},
  journal={Science},
  year={2006},
  volume={312},
  pages={101 - 97}
}
According to Darwinian theory, complexity evolves by a stepwise process of elaboration and optimization under natural selection. Biological systems composed of tightly integrated parts seem to challenge this view, because it is not obvious how any element's function can be selected for unless the partners with which it interacts are already present. Here we demonstrate how an integrated molecular system—the specific functional interaction between the steroid hormone aldosterone and its partner… 
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References

SHOWING 1-10 OF 51 REFERENCES
Evolution of vertebrate steroid receptors from an ancestral estrogen receptor by ligand exploitation and serial genome expansions
  • J. W. Thornton
  • Biology, Medicine
    Proceedings of the National Academy of Sciences of the United States of America
  • 2001
TLDR
A model of ligand exploitation is supported in which the terminal ligand in a biosynthetic pathway is the first for which a receptor evolves; selection for this hormone also selects for the synthesis of intermediates despite the absence of receptors, and duplicated receptors then evolve affinity for these substances.
The evolutionary origin of complex features
TLDR
Findings show how complex functions can originate by random mutation and natural selection.
Resurrecting the Ancestral Steroid Receptor: Ancient Origin of Estrogen Signaling
TLDR
These findings indicate that SRs are extremely ancient and widespread, having diversified from a primordial gene before the origin of bilaterally symmetric animals, and that this ancient receptor had estrogen receptor–like functionality.
The Origin of Subfunctions and Modular Gene Regulation
TLDR
The results suggest that even in the absence of any direct selective advantage, genotypic modularity may increase through the formation of new subfunctions under near-neutral processes.
Chance caught on the wing: cis-regulatory evolution and the origin of pigment patterns in Drosophila
TLDR
It is shown that the evolution of this spot involved modifications of an ancestral cis-regulatory element of the yellow pigmentation gene, which has gained multiple binding sites for transcription factors that are deeply conserved components of the regulatory landscape controlling wing development.
Structural and biochemical mechanisms for the specificity of hormone binding and coactivator assembly by mineralocorticoid receptor.
TLDR
This work reports a crystal structure of the MR ligand binding domain containing a single C808S mutation bound to corticosterone and the fourth LXXLL motif of steroid receptor coactivator-1 (SRC1-4) and reveals a compact steroid binding pocket with a unique topology that is primarily defined by key residues of helices 6 and 7.
Principles for modulation of the nuclear receptor superfamily
TLDR
This review provides a general overview of the mechanism of action of nuclear receptors and explores the various factors that are instrumental in modulating their pharmacology.
Multiple aspects of mineralocorticoid selectivity.
TLDR
Several cellular and molecular mechanisms intervene to allow specific aldosterone regulatory effects, despite the large prevalence of glucocorticoid hormones in the plasma.
Multiple corticosteroid receptors in a teleost fish: distinct sequences, expression patterns, and transcriptional activities.
TLDR
The identification of four CR subtypes in teleosts suggests a more complicated corticosteroid signaling in fish than previously recognized.
Natural Selection and the Concept of a Protein Space
TLDR
The number of possible amino-acid sequences is greater by many orders of magnitude than the number of proteins which could have existed on Earth since the origin of life, and hence that functionally effective proteins have a vanishingly small chance of arising by mutation.
...
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5
...