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Fig. 3. Motility-related processes known to be affected by calpains and the substrates or binding partners acting as effectors. Calpain 2 can cleave adhesion complex proteins such as FAK, paxillin and talin 1, possibly resulting in integrin activation, adhesion complex turnover or detachment of the cell rear. Proteolysis of the actin-regulating protein cortactin might lead to inhibition of membrane protrusion. Cleavage of integrin ß-tails might be important for the formation of small integrin clusters during the early stages of cell spreading, whereas proteolysis of the small GTPase RhoA negatively regulates cell spreading. Interaction of 
PIX with calpain small subunit 1 (CSS1) can also mediate cell spreading. Proteolysis of the adaptor protein MARCKS might also regulate cell migration in myoblasts, possibly by promoting adhesion formation. The isoforms required for proteolysis of integrins, RhoA and MARCKS remain to be determined, as do the processes affected by proteolysis of nearly 100 other calpain substrates.
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