Calcineurin associates with centrosomes and regulates cilia length maintenance.

Calcineurin, or protein phosphatase 2B (PP2B), the Ca2+ and calmodulin-activated phosphatase and target of immunosuppressants, has many substrates and functions that remain uncharacterized. By combining rapid proximity-dependent labeling with cell cycle synchronization, we mapped the spatial distribution of calcineurin in different cell cycle stages. While calcineurin-proximal proteins did not vary significantly between interphase and mitosis, calcineurin consistently associated with multiple centrosomal and/or ciliary proteins.

A cellular atlas of calcineurin signaling.

Intracellular Ca signals are temporally controlled and spatially restricted. Signaling occurs adjacent to sites of Ca entry and/or release, where Ca-dependent effectors and their substrates co-localize to form signaling microdomains. Here we review signaling by calcineurin, the Ca/calmodulin regulated protein phosphatase and target of immunosuppressant drugs, Cyclosporin A and FK506.

Palmitoylation targets the calcineurin phosphatase to the phosphatidylinositol 4-kinase complex at the plasma membrane.

Calcineurin, the conserved protein phosphatase and target of immunosuppressants, is a critical mediator of Ca signaling. Here, to discover calcineurin-regulated processes we examined an understudied isoform, CNAβ1. We show that unlike canonical cytosolic calcineurin, CNAβ1 localizes to the plasma membrane and Golgi due to palmitoylation of its divergent C-terminal tail, which is reversed by the ABHD17A depalmitoylase.