The PKA anchoring protein, AKAP7, localizes PKA in dentate granule mossy fibers and this localization plays an important role in contextual discrimination and cAMP-induced synaptic plasticity.
Structural analysis of an AKAP18-protein kinase A complex reveals that regions of intrinsic disorder impact the phosphorylation of preferred substrates.
Fibrolamellar carcinoma results from a genetic lesion that produces the DNAJ-PKAc fusion kinase, which is recruited into macromolecular complexes and is sensitive to combinations of signal transduction inhibitor drugs.
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.
During intestinal development, apical PAR complex proteins keep apical domains and junctions continuous between cells as they divide and elongate, and ultimately build a continuous functional tube.
The protein-lipid modification palmitoylation targets the kinase LIMK1 to dendritic spines to ensure precise control of the size of individual spines in response to synaptic activation.
A novel synthetic DNA cassette of CTCF-binding sites combined with the drug-controllable induction system of heterochromatin enabled switchable blocking of chromatin conformation and gene-enhancer interaction.
Plasma membrane clusters of the Parkinson's disease protein α-synuclein colocalize with negatively charged phospholipids involved in endocytosis and exocytosis.
Vibrator and PI4KIIIα that stimulate the synthesis of PI(4)P anchor non-muscle myosin II RLC (Sqh) to the plasma membrane and conversely Sqh associates with PI(4)P and facilitates its membrane localization during asymmetric division of neuroblasts.
