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Effect of caspase cleavage-site phosphorylation on proteolysis

  1. Author:
    Tozser, J.
    Bagossi, N.
    Zahuczky, G.
    Specht, S. I.
    Majerova, E.
    Copeland, T. D.

  2. Author Address

    Debrecen Univ Med, Fac Med, Dept Biochem & Mol Biol, H-4012 Debrecen, Hungary Debrecen Univ Med, Fac Med, Dept Biochem & Mol Biol, H-4012 Debrecen, Hungary NCI, Basic Res Lab, Canc Res Ctr, Frederick, MD 21701 USA SAIC Frederick, Frederick, MD 21701 USA Tozser J Debrecen Univ Med, Fac Med, Dept Biochem & Mol Biol, H-4012 Debrecen, Hungary
    1. Year: 2003
  2. Journal: Biochemical Journal
    1. 372
    2. Part 1
    3. Pages: 137-143
  4. Type of Article: Article
  1. Abstract:

    Caspases are important mediators of apoptotic cell death. Several cellular protein substrates of caspases contain potential phosphorylation site(s) at the cleavage-site region, and some of these sites have been verified to be phosphorylated. Since phosphorylation may affect substantially the substrate susceptibility towards proteolysis, phosphorylated, non-phosphorylated and substituted oligopeptides representing such cleavage sites were studied as substrates of apoptotic caspases 3, 7 and 8. Peptides containing phosphorylated serine residues at P4 and P1' positions were found to be substantially less susceptible towards proteolysis as compared with the serine-containing analogues, while phosphoserine at P3 did not have a substantial effect. PI serine as well as P1-phosphorylated, serine- containing analogues of an oligopeptide representing the poly(ADP-ribose) polymerase cleavage site of caspase-3 were not hydrolysed by any of these enzymes, whereas the P I aspartate- containing peptides were efficiently hydrolysed. These findings were interpreted with the aid of molecular modelling. Our results suggest that cleavage-site phosphorylation in certain positions could be disadvantageous or detrimental with respect to cleavability by caspases. Cleavage-site phosphorylation may therefore provide a regulatory mechanism to protect substrates from caspase-mediated degradation.

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