GSK3β-driven phosphorylation of ABLIM1 regulates its interactions with titin cardiac muscle.

The heart adapts to cardiac demand via chemical modifications of contractile myofilament proteins. Many of these modifications, such as phosphorylation, occur in proteins' intrinsically disordered regions (IDRs). These IDRs, though challenging to study, are recognized as dynamic, tunable regulators of protein function.

Molecular mechanisms of GSK3 -driven modulation of ABLIM1 and titin interactions in cardiac muscle.

1 The heart adapts to cardiac demand through various mechanisms, including chemical modifications of myofilament proteins responsible for cell contraction. Many of these modifications, such as phosphorylation, occur in unstructured, or intrinsically disordered, regions (IDRs) of proteins. Although often challenging to study, these IDRs are increasingly recognized as dynamic, tunable regulators of protein function.