3.4.22.52	phosphoprotein	brain-derived neurotrophic factor does not stimulate mu-calpain serine phosphorylation	709641	
3.4.22.52	phosphoprotein	protein phosphatase 2A functions as a physiological calpain phosphatase to directly dephosphorylate mu-calpain, which leads to decreased calpain activity and suppression of migration and invasion of human lung cancer cells	680713	
3.4.22.52	proteolytic modification	autolysis of both mu-calpain and calpain-3 is tightly regulated by Ca2+ concentration in skeletal muscle across a range close to but evidently above that reached during normal activity	663588	
3.4.22.52	proteolytic modification	calpains are autolyzed in the early stage of skeletal muscle atrophy. This autolysis is specific to the particulate fraction for calpain 1 and to the soluble fraction for calpain 2, indicating specific microlocalization of calpain autolysis regulation. Calpain 1 autolysis occurs without any modification in the total amount. Calpain autolysis is only seen in the slow soleus muscle, while the fast plantaris muscle is not affected. Calpain autolysis and caspase 3 activation found in the soleus muscle could explain a more atrophied condition of this muscle compared with the plantaris muscle	677455