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.
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.
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.