BIOMAT Database Logo BIOMAT Database Logo

Type II regulatory subunits are not required for the anchoring-dependent modulation of Ca2+ channel activity by cAMP-dependent protein kinase. 1997

K A Burton, and B D Johnson, and Z E Hausken, and R E Westenbroek, and R L Idzerda, and T Scheuer, and J D Scott, and W A Catterall, and G S McKnight
Department of Pharmacology, University of Washington School of Medicine, Box 357750, Seattle, WA 98195-7750, USA.

Preferential phosphorylation of specific proteins by cAMP-dependent protein kinase (PKA) may be mediated in part by the anchoring of PKA to a family of A-kinase anchor proteins (AKAPs) positioned in close proximity to target proteins. This interaction is thought to depend on binding of the type II regulatory (RII) subunits to AKAPs and is essential for PKA-dependent modulation of the alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid/kainate receptor, the L-type Ca2+ channel, and the KCa channel. We hypothesized that the targeted disruption of the gene for the ubiquitously expressed RIIalpha subunit would reveal those tissues and signaling events that require anchored PKA. RIIalpha knockout mice appear normal and healthy. In adult skeletal muscle, RIalpha protein levels increased to partially compensate for the loss of RIIalpha. Nonetheless, a reduction in both catalytic (C) subunit protein levels and total kinase activity was observed. Surprisingly, the anchored PKA-dependent potentiation of the L-type Ca2+ channel in RIIalpha knockout skeletal muscle was unchanged compared with wild type although it was more sensitive to inhibitors of PKA-AKAP interactions. The C subunit colocalized with the L-type Ca2+ channel in transverse tubules in wild-type skeletal muscle and retained this localization in knockout muscle. The RIalpha subunit was shown to bind AKAPs, although with a 500-fold lower affinity than the RIIalpha subunit. The potentiation of the L-type Ca2+ channel in RIIalpha knockout mouse skeletal muscle suggests that, despite a lower affinity for AKAP binding, RIalpha is capable of physiologically relevant anchoring interactions.

UI MeSH Term Description Entries
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D015220 Calcium Channels Voltage-dependent cell membrane glycoproteins selectively permeable to calcium ions. They are categorized as L-, T-, N-, P-, Q-, and R-types based on the activation and inactivation kinetics, ion specificity, and sensitivity to drugs and toxins. The L- and T-types are present throughout the cardiovascular and central nervous systems and the N-, P-, Q-, & R-types are located in neuronal tissue. Ion Channels, Calcium,Receptors, Calcium Channel Blocker,Voltage-Dependent Calcium Channel,Calcium Channel,Calcium Channel Antagonist Receptor,Calcium Channel Antagonist Receptors,Calcium Channel Blocker Receptor,Calcium Channel Blocker Receptors,Ion Channel, Calcium,Receptors, Calcium Channel Antagonist,VDCC,Voltage-Dependent Calcium Channels,Calcium Channel, Voltage-Dependent,Calcium Channels, Voltage-Dependent,Calcium Ion Channel,Calcium Ion Channels,Channel, Voltage-Dependent Calcium,Channels, Voltage-Dependent Calcium,Voltage Dependent Calcium Channel,Voltage Dependent Calcium Channels
D015640 Ion Channel Gating The opening and closing of ion channels due to a stimulus. The stimulus can be a change in membrane potential (voltage-gated), drugs or chemical transmitters (ligand-gated), or a mechanical deformation. Gating is thought to involve conformational changes of the ion channel which alters selective permeability. Gating, Ion Channel,Gatings, Ion Channel,Ion Channel Gatings
D051379 Mice The common name for the genus Mus. Mice, House,Mus,Mus musculus,Mice, Laboratory,Mouse,Mouse, House,Mouse, Laboratory,Mouse, Swiss,Mus domesticus,Mus musculus domesticus,Swiss Mice,House Mice,House Mouse,Laboratory Mice,Laboratory Mouse,Mice, Swiss,Swiss Mouse,domesticus, Mus musculus
D054746 Cyclic AMP-Dependent Protein Kinase Type II A cyclic AMP-dependent protein kinase subtype primarily found in particulate subcellular fractions. They are tetrameric proteins that contain two catalytic subunits and two type II-specific regulatory subunits. Protein Kinase A, Type II,Protein Kinase Type II, Cyclic AMP-Dependent,Cyclic AMP Dependent Protein Kinase Type II,Protein Kinase Type II, Cyclic AMP Dependent
D054754 Cyclic AMP-Dependent Protein Kinase RIIalpha Subunit A type II cAMP-dependent protein kinase regulatory subunit that plays a role in confering CYCLIC AMP activation of protein kinase activity. It has a higher affinity for cAMP than that of the CYCLIC-AMP-DEPENDENT PROTEIN KINASE RIIBETA SUBUNIT. Binding of this subunit by A KINASE ANCHOR PROTEINS may play a role in the cellular localization of type II protein kinase A. Protein Kinase A, RII alpha Subunit,Cyclic-AMP-Dependent Protein Kinase RIIalpha Subunit,RII alpha, cAMP Protein Kinase,RIIalpha, cAMP Protein Kinase,Regulatory Subunit RIIalpha, Cyclic-AMP-Dependent Protein Kinase,cAMP Protein Kinase RIIalpha,cAMP-Dependent Protein Kinase type II-alpha Regulatory Subunit,cAMP-Dependent Protein Kinase, Type 2alpha-Regulatory Subunit,Cyclic AMP Dependent Protein Kinase RIIalpha Subunit,Regulatory Subunit RIIalpha, Cyclic AMP Dependent Protein Kinase,cAMP Dependent Protein Kinase type II alpha Regulatory Subunit,cAMP Dependent Protein Kinase, Type 2alpha Regulatory Subunit
D054756 Cyclic AMP-Dependent Protein Kinase RIalpha Subunit A type I cAMP-dependent protein kinase regulatory subunit that plays a role in confering CYCLIC AMP activation of protein kinase activity. It has a lower affinity for cAMP than the CYCLIC-AMP-DEPENDENT PROTEIN KINASE RIBETA SUBUNIT. Protein Kinase A, RIalpha Subunit,Cyclic-AMP-Dependent Protein Kinase RIalpha Subunit,RI alpha, cAMP Protein Kinase,RIalpha, PKA,RIalpha, Protein Kinase A,RIalpha, cAMP Protein Kinase,Regulatory Subunit RIalpha, Cyclic-AMP-Dependent Protein Kinase,Cyclic AMP Dependent Protein Kinase RIalpha Subunit,PKA RIalpha,Regulatory Subunit RIalpha, Cyclic AMP Dependent Protein Kinase
D017868 Cyclic AMP-Dependent Protein Kinases A group of enzymes that are dependent on CYCLIC AMP and catalyze the phosphorylation of SERINE or THREONINE residues on proteins. Included under this category are two cyclic-AMP-dependent protein kinase subtypes, each of which is defined by its subunit composition. Adenosine Cyclic Monophosphate-Dependent Protein Kinases,Protein Kinase A,cAMP Protein Kinase,cAMP-Dependent Protein Kinases,Cyclic AMP-Dependent Protein Kinase,cAMP-Dependent Protein Kinase,Adenosine Cyclic Monophosphate Dependent Protein Kinases,Cyclic AMP Dependent Protein Kinase,Cyclic AMP Dependent Protein Kinases,Protein Kinase, cAMP,Protein Kinase, cAMP-Dependent,Protein Kinases, cAMP-Dependent,cAMP Dependent Protein Kinase,cAMP Dependent Protein Kinases
D018345 Mice, Knockout Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes. Knockout Mice,Mice, Knock-out,Mouse, Knockout,Knock-out Mice,Knockout Mouse,Mice, Knock out
D018482 Muscle, Skeletal A subtype of striated muscle, attached by TENDONS to the SKELETON. Skeletal muscles are innervated and their movement can be consciously controlled. They are also called voluntary muscles. Anterior Tibial Muscle,Gastrocnemius Muscle,Muscle, Voluntary,Plantaris Muscle,Skeletal Muscle,Soleus Muscle,Muscle, Anterior Tibial,Muscle, Gastrocnemius,Muscle, Plantaris,Muscle, Soleus,Muscles, Skeletal,Muscles, Voluntary,Skeletal Muscles,Tibial Muscle, Anterior,Voluntary Muscle,Voluntary Muscles

Related Publications

K A Burton, and B D Johnson, and Z E Hausken, and R E Westenbroek, and R L Idzerda, and T Scheuer, and J D Scott, and W A Catterall, and G S McKnight
The cAMP-binding proteins of Leishmania are not the regulatory subunits of cAMP-dependent protein kinase.
September 2001, Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology,
K A Burton, and B D Johnson, and Z E Hausken, and R E Westenbroek, and R L Idzerda, and T Scheuer, and J D Scott, and W A Catterall, and G S McKnight
Modulation of the cloned skeletal muscle L-type Ca2+ channel by anchored cAMP-dependent protein kinase.
February 1997, The Journal of neuroscience : the official journal of the Society for Neuroscience,
K A Burton, and B D Johnson, and Z E Hausken, and R E Westenbroek, and R L Idzerda, and T Scheuer, and J D Scott, and W A Catterall, and G S McKnight
Coelution of the type II holoenzyme form of cAMP-dependent protein kinase with regulatory subunits of the type I form of cAMP-dependent protein kinase.
October 1985, The Journal of biological chemistry,
K A Burton, and B D Johnson, and Z E Hausken, and R E Westenbroek, and R L Idzerda, and T Scheuer, and J D Scott, and W A Catterall, and G S McKnight
Alpha4 integrins are type I cAMP-dependent protein kinase-anchoring proteins.
April 2007, Nature cell biology,
K A Burton, and B D Johnson, and Z E Hausken, and R E Westenbroek, and R L Idzerda, and T Scheuer, and J D Scott, and W A Catterall, and G S McKnight
Predicted structures of cAMP binding domains of type I and II regulatory subunits of cAMP-dependent protein kinase.
January 1987, Biochemistry,
K A Burton, and B D Johnson, and Z E Hausken, and R E Westenbroek, and R L Idzerda, and T Scheuer, and J D Scott, and W A Catterall, and G S McKnight
Type II cAMP-dependent protein kinase regulatory subunit-binding proteins.
January 1988, Methods in enzymology,
K A Burton, and B D Johnson, and Z E Hausken, and R E Westenbroek, and R L Idzerda, and T Scheuer, and J D Scott, and W A Catterall, and G S McKnight
Bidirectional control of phospholipase A2 activity by Ca2+/calmodulin-dependent protein kinase II, cAMP-dependent protein kinase, and casein kinase II.
August 1991, Proceedings of the National Academy of Sciences of the United States of America,
K A Burton, and B D Johnson, and Z E Hausken, and R E Westenbroek, and R L Idzerda, and T Scheuer, and J D Scott, and W A Catterall, and G S McKnight
Modulation of inositol 1,4,5-trisphosphate receptor type 2 channel activity by Ca2+/calmodulin-dependent protein kinase II (CaMKII)-mediated phosphorylation.
November 2012, The Journal of biological chemistry,
K A Burton, and B D Johnson, and Z E Hausken, and R E Westenbroek, and R L Idzerda, and T Scheuer, and J D Scott, and W A Catterall, and G S McKnight
Immunochemical studies on human, bovine and pig brain regulatory subunits of cAMP-dependent protein kinase type II.
August 1996, Biochemistry and molecular biology international,
K A Burton, and B D Johnson, and Z E Hausken, and R E Westenbroek, and R L Idzerda, and T Scheuer, and J D Scott, and W A Catterall, and G S McKnight
Conserved phosphorylation of the intracellular domains of GABA(A) receptor beta2 and beta3 subunits by cAMP-dependent protein kinase, cGMP-dependent protein kinase protein kinase C and Ca2+/calmodulin type II-dependent protein kinase.
October 1997, Neuropharmacology,
Copied contents to your clipboard!