S100A7, S100A10, and S100A11 are transglutaminase substrates

Biochemistry. 2001 Mar 13;40(10):3167-73. doi: 10.1021/bi0019747.

Abstract

S100 proteins are a family of 10-14 kDa EF-hand-containing calcium binding proteins that function to transmit calcium-dependent cell regulatory signals. S100 proteins have no intrinsic enzyme activity but bind in a calcium-dependent manner to target proteins to modulate target protein function. Transglutaminases are enzymes that catalyze the formation of covalent epsilon-(gamma-glutamyl)lysine bonds between protein-bound glutamine and lysine residues. In the present study we show that transglutaminase-dependent covalent modification is a property shared by several S100 proteins and that both type I and type II transglutaminases can modify S100 proteins. We further show that the reactive regions are at the solvent-exposed amino- and carboxyl-terminal ends of the protein, regions that specify S100 protein function. We suggest that transglutaminase-dependent modification is a general mechanism designed to regulate S100 protein function.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 3T3 Cells
  • Animals
  • Annexins / metabolism*
  • Calcium / metabolism
  • Calcium-Binding Proteins / metabolism*
  • Cells, Cultured
  • Epidermis / enzymology
  • Epidermis / metabolism
  • GTP-Binding Proteins / metabolism
  • Glutamine / metabolism
  • Humans
  • Keratinocytes / enzymology
  • Keratinocytes / metabolism
  • Lysine / metabolism
  • Mice
  • Psoriasis / enzymology
  • Psoriasis / metabolism
  • Putrescine / metabolism
  • S100 Calcium Binding Protein A7
  • S100 Proteins / metabolism*
  • Substrate Specificity
  • Swine
  • Transglutaminases / metabolism*

Substances

  • Annexins
  • Calcium-Binding Proteins
  • S100 Calcium Binding Protein A7
  • S100 Proteins
  • S100A7 protein, human
  • Glutamine
  • S100A11 protein, human
  • transglutaminase 2
  • Transglutaminases
  • GTP-Binding Proteins
  • Lysine
  • Calcium
  • Putrescine