Emerging functions of the calpain superfamily of cysteine proteases in neuroendocrine secretory pathways.
The first calpain protease was discovered over 40 years ago now, yet despite the vast amount of literature that has subsequently emerged detailing their involvement in the pathophysiology of a variety of human diseases, it is only in the last decade that calpain-mediated actions along the secretory pathway have begun to emerge. However, the number of secretory pathway substrates identified and their diversity of function continues to grow. This review summarizes our current knowledge of calpain-mediated mechanisms of action that are pertinent to synaptic vesicle assembly and budding, cytoskeletal organization, endosomal recycling, and exocytotic membrane fusion.
Evans
Joanne S
JS
Centre for Diabetes and Metabolic Medicine, Institute of Cell and Molecular Science, London, UK.
Turner
Mark D
MD
D000818:Animals; D002154:Calpain / Q000378:metabolism*; D003599:Cytoskeleton / Q000201:enzymology / Q000648:ultrastructure; D011992:Endosomes / Q000201:enzymology / Q000648:ultrastructure; D005089:Exocytosis / Q000502:physiology; D006801:Humans; D009490:Neurosecretory Systems / Q000201:enzymology*; D022142:Secretory Vesicles / Q000201:enzymology / Q000648:ultrastructure; D009435:Synaptic Transmission / Q000502:physiology; D013572:Synaptic Vesicles / Q000201:enzymology / Q000648:ultrastructure
D002154:Calpain