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Related Experiment Videos

The FHA domain.

Daniel Durocher1, Stephen P Jackson

  • 1Samuel Lumenfeld Research Institute, Mount Sinai Hospital, Toronto, ON, Canada M5G 1 X5. durocher@mshri.on.ca

FEBS Letters
|March 26, 2002
PubMed
Summary
This summary is machine-generated.

The forkhead-associated (FHA) domain recognizes phosphothreonine, a key modification in protein regulation. This ancient and widespread protein module is vital for assembling protein complexes across eukaryotes and bacteria.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cellular Regulation

Background:

  • The forkhead-associated (FHA) domain is a conserved protein module.
  • FHA domains are known to bind phosphothreonine residues on target proteins.
  • These domains are found in various proteins involved in cellular processes.

Purpose of the Study:

  • To highlight the significance of the FHA domain in molecular recognition.
  • To underscore the role of FHA domains in protein-protein interactions.
  • To emphasize the evolutionary conservation and widespread distribution of FHA domains.

Main Methods:

  • Literature review of studies on FHA domain function.
  • Bioinformatic analysis of FHA domain distribution in protein databases.

Related Experiment Videos

  • Comparative analysis of FHA domain-containing proteins across different organisms.

    • Main Results:

    • FHA domains specifically recognize phosphothreonine epitopes.
    • FHA domains are present in diverse eukaryotic proteins, including kinases, phosphatases, and transcription factors.
    • FHA domains are also found in bacterial proteins, indicating ancient origins.

    Conclusions:

    • FHA domain-mediated recognition of phosphothreonine is a fundamental regulatory mechanism.
    • The widespread presence of FHA domains suggests their critical role in ancient cellular pathways.
    • Phospho-dependent protein complex assembly via FHA domains is a conserved biological process.