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Related Experiment Videos

The FHA domain mediates phosphoprotein interactions.

J Li1, G I Lee, S R Van Doren

  • 1Division of Biological Sciences and Department of Biochemistry, University of Missouri-Columbia, Columbia, MO 65211, USA.

Journal of Cell Science
|November 9, 2000
PubMed
Summary

The forkhead-associated (FHA) domain binds phosphopeptides and is crucial in diverse cellular processes like DNA repair and signaling. Its structure and binding capabilities highlight its broad biological significance.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • The forkhead-associated (FHA) domain is a conserved phosphopeptide-binding module.
  • Initially identified in forkhead transcription factors, FHA domains are now known to be present in diverse proteins across prokaryotes and eukaryotes.
  • FHA domain-containing proteins are implicated in critical cellular functions such as DNA repair, cell cycle regulation, and pre-mRNA processing in yeast and humans, and in plant receptor-like kinase signaling.

Purpose of the Study:

  • To elucidate the structural and functional characteristics of the forkhead-associated (FHA) domain.
  • To understand the binding specificities and cellular roles of FHA domains in various organisms.

Main Methods:

  • Structural analysis of FHA domains, focusing on secondary and tertiary structures.

Related Experiment Videos

  • Investigation of phosphopeptide-binding capabilities, including specificity for phosphothreonine, phosphoserine, and phosphotyrosine.

    • Main Results:

    • A functional FHA domain comprises 120-140 amino acid residues, larger than previously recognized.
    • Despite limited sequence similarity, FHA domains share a conserved structure of two anti-parallel beta-sheets.
    • FHA domains exhibit unique binding affinities for phosphothreonine, phosphoserine, and sometimes phosphotyrosine.

    Conclusions:

    • The FHA domain's conserved structure and diverse binding specificities indicate its role in coordinating a wide array of cellular processes.
    • The FHA domain represents a significant phosphoprotein-binding module with broad implications in molecular and cell biology.