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Proteolytic cleavage of β‐catenin by caspases: an in vitro analysis
Author(s) -
Van de Craen Marc,
Berx Geert,
Van den Brande Ilse,
Fiers Walter,
Declercq Wim,
Vandenabeele Peter
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01153-9
Subject(s) - cleavage (geology) , caspase , chemistry , in vitro , microbiology and biotechnology , catenin , apoptosis , biochemistry , biology , signal transduction , programmed cell death , wnt signaling pathway , paleontology , fracture (geology)
Cleavage of structural proteins by caspases has been associated with the severe morphological changes occurring during the apoptotic process. One of the proteins regulating the connection of the actin filament with cadherins in a cell‐cell adhesion complex is β‐catenin. During apoptosis, both an N‐terminal and a small C‐terminal part are removed from β‐catenin. Removal of the N‐terminal part may result in a disconnection of the actin filament from a cadherin cell‐cell adhesion complex. We demonstrate that caspase‐8, ‐3 and ‐6 directly proteolyse β‐catenin in vitro. However, the β‐catenin cleavage products generated by caspase‐8 were different from those generated by caspase‐3 or caspase‐6. Caspase‐1, ‐2, ‐4/11 and ‐7 did not or only very inefficiently cleave β‐catenin. These data suggest that activation of procaspase‐3, ‐6 or ‐8 by different stimuli in the cell might result in a differential proteolysis of β‐catenin.