N-terminal cleavage of GSK-3 by calpain: a new form of GSK-3 regulation
P Goñi-Oliver, JJ Lucas, J Avila, F Hernández - Journal of Biological …, 2007 - ASBMB
Although GSK-3 activity can be regulated by phosphorylation and through interaction with
GSK-3-binding proteins, here we describe N-terminal proteolysis as a novel way to regulate
GSK-3. When brain extracts were exposed to calcium, GSK-3 was truncated, generating two
fragments of∼ 40 and 30 kDa, a proteolytic process that was inhibited by specific calpain
inhibitors. Interestingly, instead of inhibiting this enzyme, GSK-3 truncation augmented its
kinase activity. When we digested recombinant GSK-3α and GSK-3β protein with calpain …
GSK-3-binding proteins, here we describe N-terminal proteolysis as a novel way to regulate
GSK-3. When brain extracts were exposed to calcium, GSK-3 was truncated, generating two
fragments of∼ 40 and 30 kDa, a proteolytic process that was inhibited by specific calpain
inhibitors. Interestingly, instead of inhibiting this enzyme, GSK-3 truncation augmented its
kinase activity. When we digested recombinant GSK-3α and GSK-3β protein with calpain …
