Phosphorylase kinase: The complexity of its regulation is reflected in the complexity of its structure

Brushia, Robert, J.

doi:10.2741/brushia

Cited by 174Glycogen Storage Diseases and MyoclonusMetabolism, Diabetes, and CancerProtein Kinase Regulation and GTPase Signaling

Phosphorylase kinase: The complexity of its regulation is reflected in the complexity of its structure

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Brushia, Robert, J.·1999·Frontiers in bioscience

DOI 10.2741/brushia

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Abstract

Intracellular glycogen stores are used to maintain blood-glucose homeostasis during fasting, are a source of energy for muscle contraction, and are used to support a broad range of cellular activities in most tissues. A diversity of signals accelerate glycogen degradation that are mediated by phosphorylase b kinase (Phk), which phosphorylates and thereby activates glycogen phosphorylase. Phk is among the most complex of the protein kinases so far elucidated. It has one catalytic (gamma) subunit and three different regulatory (alpha, beta, and delta) subunits, a molecular mass of 1.3 X 106 daltons, and each holoenzyme molecule is presumed to contain four molecules of each subunit. The three regulatory subunits inhibit the phosphotransferase activity of the gamma subunit. Ca2+ relieves inhibition via the delta subunit, which is identical to calmodulin but remains an integral component of the holoenzyme even when the [Ca2+] is lowered to nanomolar levels. Phosphorylation of the alpha and beta subunits by the 3',5'-cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) also relieves inhibition of the gamma subunit and thereby activates the enzyme. The stimulatory effects of Ca2+ and phosphorylation appear to be structurally coupled and are cooperative. In addition, Phk is activated in vitro by autophosphorylation, limited proteolysis of the regulatory subunits, and various allosteric effectors and these may also be mechanisms of physiological importance. The molecular mechanisms of regulation are currently poorly understood, but new insights are beginning to emerge. This review discusses current knowledge and concepts of the structure, function and regulation of Phk.

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Muscular contraction increases cytosolic Ca2+ release and an adrenaline-mediated increase in cAMP, thereby activating phosphorylase kinase and the resultant activation of glycogen phosphorylase.
“Muscular contraction also increases cytosolic calcium (Ca2+) release and an adrenaline-mediated increase in cyclic AMP (cAMP), thereby activating phosphorylase kinase (PK) and the resultant activation of glycogen phosphorylase [56,57].”
From Regulation of Energy Substrate Metabolism in Endurance Exercise (2021) · cites this paper as [56]
The Introduction (page unavailable) describes motor-nerve signals releasing Ca2+ in skeletal muscle, and explains that Ca2+ and cAMP-dependent signaling activate phosphorylase kinase, which in turn activates glycogen phosphorylase. It describes the hormonal and motor-nerve pathways separately; it does not identify adrenaline or say that muscle contraction itself increases cAMP. (LLM, conf=0.85)
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The multiphosphorylation domain of the phosphorylase kinase alpha M and alpha L subunits is a hotspot of differential mRNA processing and of molecular evolution.
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Molecular cloning and enzymatic analysis of the rat homolog of “PhK-gamma T,” an isoform of phosphorylase kinase catalytic subunit.
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Characterization of the Regulatory Domain of the γ-Subunit of Phosphorylase Kinase
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Phosphorylase kinase deficiency in I–strain mice is associated with a frameshift mutation in the α subunit muscle isoform
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Identification of the Substrate and Pseudosubstrate Binding Sites of Phosphorylase Kinase γ-Subunit
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Autosomal Recessive Liver Phosphorylase Kinase Deficiency Caused by a Novel Splice-Site Mutation in the Gene Encoding the Liver Gamma Subunit (PHKG2)
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Analysis by mutagenesis of the ATP binding site of the .gamma. subunit of skeletal muscle phosphorylase kinase expressed using a baculovirus system
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The association of phosphorylase kinase with rabbit muscle T-tubules
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X-ray analysis reveals conformational adaptation of the linker in functional calmodulin mutants
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Localization of a New Type of X-Linked Liver Glycogenosis to the Chromosomal Region Xp22 Containing the Liver α-Subunit of Phosphorylase Kinase (PHKA2)
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Motifs of protein phosphorylation and mechanisms of reversible covalent regulation
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Isolation of an autoinhibitory region from the regulatory beta-subunit of phosphorylase kinase.
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Nucleotide sequence of cDNA encoding the catalytic subunit of phosphorylase kinase from rat soleus muscle
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Evidence that phosphorylase kinase exhibits phosphatidylinositol kinase activity
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Phosphorylase b kinase deficiency glycogenosis with cirrhosis of the liver
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The interaction of calmodulin with regulatory peptides of phosphorylase kinase.
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X-linked liver glycogenosis: localization and isolation of a candidate gene
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A kinetic re-interpretation of the regulation of rabbit skeletal-muscle phosphorylase kinase activity by Ca2+ and phosphorylation
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Activation and Inhibition of Phosphorylase Kinase by Monospecific Antibodies Raised against Peptides from the Regulatory Domain of the γ-Subunit
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Phosphorylase Kinase Isoenzymes in Deficient ICR/IAn Mice
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LOCALIZATION OF CA2+‐DEPENDENT PROTEIN KINASES IN VARIOUS TISSUES BY THE IMMUNOFLUORESCENT TECHNIQUE*
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Postnatal development of phosphorylase kinase in mouse skeletal muscle
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Solution structure of phosphorylase kinase studied using small-angle x-ray and neutron scattering
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I/Lyn mouse phosphorylase kinase deficiency: mutation disrupts expression of the alpha/alpha'-subunit mRNAs.
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Expression of a cDNA for the catalytic subunit of skeletal-muscle phosphorylase kinase in transfected 3T3 cells
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Localization and Turnover of Phosphorylase Kinase in Rabbit Skeletal Muscle
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Ca2+-independent interaction of the γ subunit of phosphorylase kinase with dansyl-calmodulin
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DPhK-γ, a putative Drosophila kinase with homology to vertebrate phosphorylase kinase γ subunits: molecular characterisation of the gene and phenotypic analysis of loss of function mutants
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Genetic deficiencies of the glycogen phosphorylase system
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PHOSPHORYLASE B KINASE DEFICIENCY GLYCOGENOSIS WITH CIRRHOSIS OF LIVER
Kagalwalla, A., Kagalwalla, Y. A., Ajaji, S. A., Gorka, W., & Ashraf, A. (1995) · Journal of Pediatric Gastroenterology and Nutrition · doi:10.1002/j.1536-4801.1995.tb11818.x · Cited by 1 · see citing works

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Pickett-Gies C & D. Walsh: Phosphorylase kinase. In: The Enzymes. Academic Press, NY (1986)

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“Muscular contraction also increases cytosolic calcium (Ca2+) release and an adrenaline-mediated increase in cyclic AMP (cAMP), thereby activating phosphorylase kinase (PK) and the resultant activation of glycogen phosphorylase [56,57].”
Background
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KIAA1199 interacts with glycogen phosphorylase kinase β-subunit (PHKB) to promote glycogen breakdown and cancer cell survival
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Calmodulin binding to M‐type K+channels assayed by TIRF/FRET in living cells
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Cre recombinase-dependent expression of a constitutively active mutant allele of the catalytic subunit of protein kinase A
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Role of β-Adrenoceptor Signaling and AMP-Activated Protein Kinase in Glycolysis of Postmortem Skeletal Muscle
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Effect of molecular crowding on the enzymes of glycogenolysis
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Authors: Brushia, R.
Venue: Frontiers in bioscience
Publisher: IMR Press
Published: 1999
Volume: 4
Issue: 1-3
Pages: d618
ISSN: 1093-4715 (ISSN-L)
1093-9946
DOI: 10.2741/brushia
OpenAlex: W150287726
Cited by: 174
References: 119
Citations by year: 2026: 1 · 2025: 9 · 2024: 6 · 2023: 10 · 2022: 13 · 2021: 6 · 2020: 5 · 2019: 8 · 2018: 8 · 2017: 6 · 2016: 7 · 2015: 3 · 2014: 7 · 2013: 7 · 2012: 6
FWCI: 0.64
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Frontiers in bioscience (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Rheumatology › Glycogen Storage Diseases and Myoclonus
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords: phosphorylase kinase, glycogen phosphorylase, enzyme regulation, protein kinase structure, regulatory subunit, calmodulin, calcium signaling, protein kinase A, autophosphorylation, allosteric regulation, glycogenolysis, blood glucose homeostasis
MeSH terms: Amino Acid Sequence, Animals, Calcium, Enzyme Activation, Humans, Hydrogen-Ion Concentration, Isoenzymes, Molecular Sequence Data, Mutation, Phosphorylase Kinase, Phosphorylation, Protein Binding, Structure-Activity Relationship, Substrate Specificity, Consensus Sequence, Protein Structure, Tertiary, Cyclic AMP-Dependent Protein Kinases, Holoenzymes

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Phosphorylase kinase: The complexity of its regulation is reflected in the complexity of its structure

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