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Characterisation of Mcl‐1 cleavage during apoptosis of haematopoietic cells

Mcl‐1 is essential for normal haematopoiesis, being required for lymphocyte development and maintenance. Its role in haematopoietic differentiation and development is associated with its function as an anti‐apoptotic member of the Bcl‐2 family of proteins although the underlining mechanism is poorly understood. We have characterized caspase cleavage of the Mcl‐1 protein during apoptosis. Caspase cleavage resulted in the removal of the PEST regions from the protein and generation of a fragment containing the BH‐1, ‐2 and ‐3 homology domains. Removal of the PEST regions did not appear to alter Mcl‐1 stability, suggesting that these regions are not responsible for Mcl‐1's short half‐life. In addition, unlike cleavage of Bcl‐2 and Bcl‐XL, which resulted in pro‐apoptotic fragments, cleaved forms of Mcl‐1 were unable to induce apoptosis. This novel regulation of Mcl‐1 may have important implications not only for its role in apoptosis but also for the essential role it plays in the differentiation and development of haematopoietic cells.