kinaseinteracting

Kinase-interacting refers to proteins or factors that bind to protein kinases, influencing their activity, localization, or substrate specificity. These interactions form part of cellular signaling networks by modulating kinase function rather than serving as substrates themselves.

Interactors can be direct binders to catalytic or regulatory domains, or indirect partners that assemble signaling complexes or scaffolds that bring kinases into proximity with substrates. Interaction can be regulated by phosphorylation, calcium, or other second messengers, enabling context-dependent signaling and precise control over when and where signals are transmitted.

Well-known examples include 14-3-3 proteins, which bind phosphorylated motifs on kinases and regulate activity and localization; SH2-domain-containing adaptors such as Grb2 that recruit kinases to activated receptors; and A-kinase anchoring proteins (AKAPs) that localize PKA to specific cellular compartments. This category also includes calmodulin interaction with CaMKII and other calcium-sensitive kinases, as well as various regulator proteins that modulate kinase docking and substrate presentation.

Researchers study kinase interactors using methods such as co-immunoprecipitation, yeast two-hybrid screening, pull-down assays, and proximity-based labeling approaches followed by mass spectrometry, which help map interaction networks and binding dependencies in different cellular contexts.

Biologically, kinase-interacting proteins shape signaling networks governing cell growth, differentiation, immune responses, and stress adaptation. Aberrations in these interactions can contribute to cancer, neurodegenerative and metabolic disorders, making them potential targets for therapeutic intervention. Approaches to modulate kinase interactions—by disrupting or stabilizing specific contacts—offer avenues for selective therapeutic modulation beyond traditional ATP-competitive inhibitors.