Emerging functions of the calpain superfamily of cysteine proteases in neuroendocrine secretory pathways
Article first published online: 11 JUL 2007
Journal of Neurochemistry
Volume 103, Issue 3, pages 849–859, November 2007
How to Cite
Evans, J. S. and Turner, M. D. (2007), Emerging functions of the calpain superfamily of cysteine proteases in neuroendocrine secretory pathways. Journal of Neurochemistry, 103: 849–859. doi: 10.1111/j.1471-4159.2007.04815.x
- Issue published online: 11 JUL 2007
- Article first published online: 11 JUL 2007
- Received April 16, 2007; revised manuscript received June 5, 2007; accepted June 19, 2007.
- synaptic vesicle
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.