Caspase-mediated cleavage of FADK 1

Stable Identifier
R-HSA-201634
Type
Reaction [transition]
Species
Homo sapiens
Compartment
cytosol
ReviewStatus
5/5
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Caspase-mediated cleavage of FADK 1
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FAK is a tyrosine kinase that localizes to focal adhesions and associates temporally and spatially with integrins (see references in Fischer et al., 2003 ). FAK is cleaved by caspases including caspase-7 (Wen et al., 1997). Caspases also cleave fodrin and components of the focal adhesion complex which links cortical actin filaments and membrane proteins to the extracellular matrix. Cleavage of these proteins is thought to promote cell shrinkage and cell detachment and disrupt antiapoptotic integrin signaling (see Fischer et al., 2003).
Literature References
PubMed ID Title Journal Year
9325343 Cleavage of focal adhesion kinase by caspases during apoptosis

Guan, JL, Wen, LP, Fahrni, JA, Rosen, GD, Troie, S, Orth, K

J Biol Chem 1997
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Catalyst Activity

cysteine-type endopeptidase activity of Caspase-7 [cytosol]

Physical Entity
Caspase-7 [cytosol] (Homo sapiens)
Activity
cysteine-type endopeptidase activity (GO:0004197)
Orthologous Events
Caspase-mediated cleavage of FADK 1 (Bos taurus)
Caspase-mediated cleavage of FADK 1 (Canis familiaris)
Caspase-mediated cleavage of FADK 1 (Gallus gallus)
Caspase-mediated cleavage of FADK 1 (Mus musculus)
Caspase-mediated cleavage of FADK 1 (Rattus norvegicus)
Authored
Schulze-Osthoff, K  (2007-09-03)
Reviewed
Ranganathan, S  (2007-11-23)
Created
Matthews, L  (2007-09-03)
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