Caspase mediated cleavage of alpha-II-Fodrin

Stable Identifier
R-HSA-202967
Type
Reaction [transition]
Species
Homo sapiens
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Apoptosis induced caspases cleave cortical actin network components including fodrin and components of the focal adhesion complex components which links membrane proteins and cortical actin filaments to the extracellular matrix (Janicke et al.,1998). Cleavage of these proteins results in disruption of the cortical cytoskeleton and may contribute to membrane blebbing (see Fischer et al., 2003). The full length 240 kDa alpha-fodrin protein can be cleaved at several sites within its sequence by activated caspases to yield amino-terminal 150 kDa, carboxy-terminal 120 kDa and 35 kDa major products. Cleavage of alpha-II fodrin leads to membrane malfunction and cell shrinkage (Janicke et al., 1998).

Literature References
PubMed ID Title Journal Year
9624143 Caspase-3 is required for alpha-fodrin cleavage but dispensable for cleavage of other death substrates in apoptosis

Janicke, RU, Ng, P, Sprengart, ML, Porter, AG

J Biol Chem 1998
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Catalyst Activity
Title
cysteine-type endopeptidase activity of Caspase-3 [cytosol]
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Activity
Orthologous Events
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