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Related Experiment Videos

Phosphorylation modulates keratin structure.

P L Yeagle1, J Frye, B S Eckert

  • 1Department of Biochemistry, State University of New York, Buffalo School of Medicine 14214.

Biochemistry
|February 13, 1990
PubMed
Summary
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Bovine hoof keratin structure changes upon phosphorylation by cAMP-dependent protein kinase, increasing protein rigidity and potentially altering intermediate filament organization. This phosphorylation impacts keratin

Area of Science:

  • Biochemistry
  • Structural Biology
  • Cell Biology

Background:

  • Keratin serves as a crucial structural protein in intermediate filaments.
  • Understanding keratin's structural dynamics is key to comprehending cellular organization.
  • Post-translational modifications like phosphorylation can significantly alter protein function.

Purpose of the Study:

  • To investigate the structural impact of cAMP-dependent protein kinase phosphorylation on bovine hoof keratin.
  • To elucidate how phosphorylation affects keratin's rigidity and alpha-helical content.
  • To explore the potential consequences of these structural changes on intermediate filament organization.

Main Methods:

  • Utilized [gamma-32P]ATP to phosphorylate bovine hoof keratin.

Related Experiment Videos

  • Employed natural-abundance cross-polarization magic-angle spinning (CP MAS) 13C NMR to assess structural changes.
  • Analyzed circular dichroism (CD) spectra to determine alterations in secondary structure.
  • Performed magic-angle spinning (MAS) 31P nuclear magnetic resonance (NMR) to identify phosphorylation sites.

    • Main Results:

    • Phosphorylation increased the motionally restricted portions of keratin, indicating enhanced rigidity.
    • Circular dichroism spectra suggested a potential increase in keratin's alpha-helical content post-phosphorylation.
    • 31P NMR revealed distinct phosphorylation sites, with evidence of both motionally restricted and less restricted classes.
    • The N-terminal region of keratin was identified as the likely site of structural alteration.

    Conclusions:

    • cAMP-dependent phosphorylation significantly alters bovine hoof keratin structure, increasing rigidity.
    • These structural changes may lead to modifications in the intracellular organization of intermediate filaments.
    • The study highlights the role of phosphorylation in regulating keratin's structural properties and cellular function.