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S100A7, S100A10, and S100A11 are transglutaminase substrates.

M Ruse1, A Lambert, N Robinson

  • 1Department of Physiology and Biophysics, Case Western Reserve University School of Medicine, 2109 Adelbert Road, Cleveland, Ohio 44106-4970, USA.

Biochemistry
|March 22, 2001
PubMed
Summary

Several S100 proteins can be covalently modified by transglutaminases, enzymes that regulate cellular signals. This modification occurs at the protein ends, suggesting a role in controlling S100 protein function.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • S100 proteins are calcium-binding proteins crucial for transmitting calcium-dependent cellular signals.
  • These proteins lack intrinsic enzymatic activity but modulate target protein function upon calcium binding.
  • Transglutaminases are enzymes catalyzing the formation of covalent bonds between glutamine and lysine residues in proteins.

Purpose of the Study:

  • To investigate whether S100 proteins undergo transglutaminase-dependent covalent modification.
  • To identify which types of transglutaminases can modify S100 proteins.
  • To determine the specific regions of S100 proteins targeted by transglutaminases.

Main Methods:

  • Assaying S100 protein modification by type I and type II transglutaminases.
  • Utilizing biochemical techniques to detect covalent bond formation.
  • Mapping the reactive sites on S100 proteins involved in transglutaminase modification.

Main Results:

  • Multiple S100 proteins were found to be substrates for transglutaminase-dependent covalent modification.
  • Both type I and type II transglutaminases were shown to modify S100 proteins.
  • Modification sites were identified at the solvent-exposed amino- and carboxyl-terminal ends of S100 proteins.

Conclusions:

  • Transglutaminase-dependent covalent modification is a shared property among several S100 proteins.
  • This modification mechanism, occurring at functionally important regions, likely serves to regulate S100 protein activity.
  • The findings suggest a general regulatory role for transglutaminases in controlling S100 protein signaling pathways.