ProteinLounge
Citations
About Us
Contact Us
Login to Protein Lounge!

Calpain Protease Regulates Cellular Mechanics

This image is a scaled-down version of the actual pathway image. It does not contain any links to the protein information pages.
 

Description

Calpain is an evolutionary old family of soluble, neutral, calcium-dependent proteases, which have the unique property of using protein cleavage to modify the activity/function of their substrate proteins. There are two major calpain isoforms in the brain, calpain-1 and calpain-2. Calpain-1 and Calpain-2 exhibit opposite functions in both synaptic plasticity and neurodegeneration. Calpain-1 activation is required for the induction of long-term potentiation (LTP) and is generally neuroprotective, while calpain-2 activation limits the extent of potentiation and is neurodegenerative. Calpains release the link between the integrin-dependent FA complex and the actin cytoskeleton by proteolysis of talin, which allows proper cell migration. The activity of Calpains is tightly regulated by highly specific endogenous inhibitor Calpastatin. Inhibition of Calpain causes impaired retraction [...]

References:

1.Calpain-1 and Calpain-2: The Yin and Yang of Synaptic Plasticity and Neurodegeneration.
Baudry M, Bi X.
Trends Neurosci. 2016 Apr; 39(4):235-245. doi: 10.1016/j.tins.2016.01.007. Epub 2016 Feb 10. Review.
2.Calpains: Master Regulators of Synaptic Plasticity.
Briz V, Baudry M.
Neuroscientist. 2016 May 17. pii: 1073858416649178. [Epub ahead of print] Review.
You can get all the details on this pathway through subscription