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Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Intrinsically Disordered Proteins02:18

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Scientists record evolutionary history by analyzing fossil, morphological, and genetic data. The fossil record documents the history of life on Earth and provides evidence for evolution. However, both fossil and living organisms offer evidence that outlines Earth’s evolutionary history.
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Around 4 billion years ago, oceans began to condense on earth while volcanic eruptions released nitrogen, carbon dioxide, methane, ammonia, and hydrogen into the primordial atmosphere. However, organisms with the characteristics of life were not initially present on earth. Scientists have used experimentation to determine how organisms evolved that could grow, reproduce, and maintain an internal environment.

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Genetic Engineering of Dictyostelium discoideum Cells Based on Selection and Growth on Bacteria
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Published on: January 25, 2019

Origin and evolution of dishevelled.

Adler R Dillman1, Paul J Minor, Paul W Sternberg

  • 1Howard Hughes Medical Institute, Division of Biology, California Institute of Technology, Pasadena, California 91125, USA.

G3 (Bethesda, Md.)
|February 8, 2013
PubMed
Summary

Dishevelled (Dsh) protein evolution shows dynamic changes, especially in nematodes, with new domains and nuclear signals suggesting functional specialization in Wnt signaling pathways.

Keywords:
C. elegansNematodaWntdishevelledprotein evolution

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Area of Science:

  • Evolutionary developmental biology
  • Molecular signaling pathways
  • Comparative genomics

Background:

  • Dishevelled (Dsh) is a crucial signaling protein in Wnt pathways, essential for various developmental processes.
  • Dsh is highly conserved across metazoans and has diversified into multiple genes in many animal lineages.
  • While Dsh orthologs often show functional overlap, evidence for specialization is increasing.

Purpose of the Study:

  • To conduct a comparative analysis of Dishevelled (Dsh) protein architecture across diverse animal species.
  • To identify conserved and divergent features of Dsh, focusing on invertebrates like nematodes, to understand functional specialization.
  • To explore the evolutionary dynamics of Dsh, particularly its role as a central signaling hub.

Main Methods:

  • Comparative analysis of Dishevelled (Dsh) protein sequences and structures across various animal taxa.
  • Bioinformatic identification of conserved and novel protein domains.
  • Analysis of predicted protein localization signals, such as nuclear localization signals.

Main Results:

  • Evidence of dynamic evolution in Dsh, with nematode lineages exhibiting variable ortholog numbers (one to three).
  • Identification of a novel protein domain unique to certain nematode Dsh orthologs.
  • Discovery of a conserved, unexpected nuclear localization signal in numerous Dsh orthologs.

Conclusions:

  • The evolution of Dishevelled (Dsh) is complex, with significant diversification observed, especially within nematodes.
  • The identified novel domain and conserved nuclear localization signal suggest mechanisms for functional specialization.
  • Findings provide insights into protein evolution and how organisms manage complex signaling networks, generating testable hypotheses.