Role of polyglycine repeats in the regulation of glycogen synthase kinase activity

Abstract

Glycogen synthase kinase (GSK3) activity present in one cell is the consequence of the sum of the activities of two different proteins called GSK3α and GSK3β. These isoenzymes are coded by two different genes and share an almost identical sequence at their catalytic domain, but differ in the sequence of putative regulatory regions. In this review, we propose that glycine repeats present only in GSK3α may result in the different cleavage of both isoenzymes by the protease calpain, a cleavage that modifies GSK3 activity.