Flexibility is a defining feature of AKAP kinase-phosphatase assemblies and points toward a mechanism whereby combinatorial recruitment of binding partners tailors the overall conformation of the macromolecular assembly, allowing customized physiological roles.
EPO/JAK2/PKA signaling cascade via AKAP10 relocalization to the outer mitochondrial membrane results in the phosphorylation of the terminal heme synthesis enzyme ferrochelatase, which contributes to heme production in red cells.
A potassium channel, as a nonconducting function, organizes compartmentalized neuronal calcium signaling microdomains via structural and functional coupling of plasma membrane and endoplasmic reticulum calcium channels.
Biochemical and cell biological analyses reveal that the Astrin-SKAP complex acts to stabilize kinetochore-microtubule interactions through its intrinsic microtubule binding activity and its association with the Ndc80 complex, the core component of the kinetochore-microtubule interface.
XIAP/TRIP-Br1-mediated degradation of multiple adenylyl cyclase isoforms is a previously unrecognised general mechanism for controlling adenylyl cyclase expression and the homeostasis of cAMP signalling.