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Phosphorylase kinase, beta

PHKB
Phosphorylase kinase is a polymer of 16 subunits, four each of alpha, beta, gamma and delta. The alpha subunit includes the skeletal muscle and hepatic isoforms, encoded by two different genes. The beta subunit is the same in both the muscle and hepatic isoforms, encoded by this gene, which is a member of the phosphorylase b kinase regulatory subunit family. The gamma subunit also includes the skeletal muscle and hepatic isoforms, encoded by two different genes. The delta subunit is a calmodulin and can be encoded by three different genes. The gamma subunits contain the active site of the enzyme, whereas the alpha and beta subunits have regulatory functions controlled by phosphorylation. The delta subunit mediates the dependence of the enzyme on calcium concentration. Mutations in this gene cause glycogen storage disease type 9B, also known as phosphorylase kinase deficiency of liver and muscle. Alternatively spliced transcript variants encoding different isoforms have been identified in this gene. Two pseudogenes have been found on chromosomes 14 and 20, respectively.[provided by RefSeq, Feb 2010] (from NCBI)
Top mentioned proteins: PHKA2, PHKG2, CAN, PHKA1, HAD
Papers on PHKB
Clinical, Biochemical, and Genetic Characterization of Glycogen Storage Type IX in a Child with Asymptomatic Hepatomegaly.
New
Kim et al., Seoul, South Korea. In Pediatr Gastroenterol Hepatol Nutr, Jun 2015
Glycogen storage disease type IX (GSD IX) is caused by a defect in phosphorylase b kinase (PhK) that results from mutations in the PHKA2, PHKB, and PHKG2 genes.
The natural history of glycogen storage disease types VI and IX: Long-term outcome from the largest metabolic center in Canada.
Mercimek-Mahmutoglu et al., Toronto, Canada. In Mol Genet Metab, 2014
RESULTS: We report on the natural history and treatment outcomes of the 21 patients with GSD-VI and -IX and 16 novel pathogenic mutations in the PHKA2, PHKB, PHKG2 and PYGL genes.
KIAA1199 interacts with glycogen phosphorylase kinase β-subunit (PHKB) to promote glycogen breakdown and cancer cell survival.
Nishio et al., Ōsaka, Japan. In Oncotarget, 2014
A pull-down analysis showed that the glycogen phosphorylase kinase β-subunit (PHKB) interacted with the C-terminal region of KIAA1199 protein.
Variability of disease spectrum in children with liver phosphorylase kinase deficiency caused by mutations in the PHKG2 gene.
Kishnani et al., Durham, United States. In Mol Genet Metab, 2014
Liver phosphorylase b kinase (PhK) deficiency (glycogen storage disease type IX), one of the most common causes of glycogen storage disease, is caused by mutations in the PHKA2, PHKB, and PHKG2 genes.
Liver glycogen storage diseases due to phosphorylase system deficiencies: diagnosis thanks to non invasive blood enzymatic and molecular studies.
Baussan et al., Paris, France. In Mol Genet Metab, 2011
Causative mutations were found either in the PYGL (11 patients), PHKA2 (26 patients), PHKG2 (three patients) or in the PHKB (three patients) genes.
Phosphorylase Kinase Deficiency
Review
Bali et al., Seattle, United States. In Unknown Journal, 2011
Mutations in PHKA1, encoding subunit α, cause the rare X-linked disorder muscle PhK deficiency; mutations in PHKA2, also encoding subunit α, cause the most common form, liver PhK deficiency (X-linked liver glycogenosis); mutations in PHKB, encoding subunit β, cause autosomal recessive PhK deficiency in both liver and muscle; and mutations in PHKG2, encoding subunit γ, cause autosomal recessive liver PhK deficiency.
The regulatory beta subunit of phosphorylase kinase interacts with glyceraldehyde-3-phosphate dehydrogenase.
GeneRIF
Carlson et al., Kansas City, United States. In Biochemistry, 2008
The interactions described herein between the beta subunit of PhK and GAPDH provide a possible mechanism for the direct linkage of glycogenolysis and glycolysis in skeletal muscle.
Glycogen storage disease type IX: High variability in clinical phenotype.
Sharrard et al., Cambridge, United Kingdom. In Mol Genet Metab, 2007
The liver isoforms of the alpha-, beta- and gamma-subunits are encoded by PHKA2, PHKB and PHKG2, respectively.
Severe phenotype of phosphorylase kinase-deficient liver glycogenosis with mutations in the PHKG2 gene.
Kilimann et al., Bochum, Germany. In Pediatr Res, 2003
It can be caused by mutations in three different genes of phosphorylase kinase subunits: PHKA2, PHKB, and PHKG2.
Glucoamylase-like domains in the alpha- and beta-subunits of phosphorylase kinase.
GeneRIF
Pallen, Birmingham, United Kingdom. In Protein Sci, 2003
alpha- and beta-subunits possess amino-terminal glucoamylase-like domains and suggests that they might possess a previously overlooked amylase activity
Muscle glycogenosis with low phosphorylase kinase activity: mutations in PHKA1, PHKG1 or six other candidate genes explain only a minority of cases.
Kilimann et al., Bochum, Germany. In Eur J Hum Genet, 2003
The coding sequences of all six genes that contribute to Phk in muscle were analysed: PHKA1, PHKB, PHKG1, CALM1, CALM2 and CALM3.
A mutation in GLUT2, not in phosphorylase kinase subunits, in hepato-renal glycogenosis with Fanconi syndrome and low phosphorylase kinase activity.
Kilimann et al., Bochum, Germany. In Hum Genet, 1999
We have analyzed this family for mutations in the GLUT2 gene and in the three Phk subunit genes that can cause liver glycogenosis (PHKA2, PHKB, and PHKG2).
Unequal homologous recombination between LINE-1 elements as a mutational mechanism in human genetic disease.
Kilimann et al., Bochum, Germany. In J Mol Biol, 1998
We have characterized a homologous recombination event between two neighboring LINE-1 sequences in the human gene encoding the beta subunit of phosphorylase kinase (PHKB).
Liver glycogenosis due to phosphorylase kinase deficiency: PHKG2 gene structure and mutations associated with cirrhosis.
Kilimann et al., Bochum, Germany. In Hum Mol Genet, 1998
Mutations in three different genes of phosphorylase kinase (Phk) subunits, PHKA2, PHKB and PHKG2, can give rise to glycogen storage disease of the liver.
Phosphorylase-kinase-deficient liver glycogenosis with an unusual biochemical phenotype in blood cells associated with a missense mutation in the beta subunit gene (PHKB).
Kilimann et al., Bochum, Germany. In Hum Genet, 1997
His alpha L and gamma TL coding sequences are normal, whereas he is compound-heterozygous for two mutations in the beta subunit gene, PHKB.
Autosomal recessive phosphorylase kinase deficiency in liver, caused by mutations in the gene encoding the beta subunit (PHKB).
Berger et al., Utrecht, Netherlands. In Am J Hum Genet, 1997
The association of autosomal recessive phosphorylase kinase deficiency in liver of a 3 1/2-year-old female child with mutations in the gene encoding the common part of the beta subunit of phosphorylase kinase is reported.
Autosomal glycogenosis of liver and muscle due to phosphorylase kinase deficiency is caused by mutations in the phosphorylase kinase beta subunit (PHKB).
Kilimann et al., Bochum, Germany. In Hum Mol Genet, 1997
The gene of the ubiquitously expressed beta subunit, PHKB, was a candidate for involvement in autosomally transmitted phosphorylase kinase deficiency of liver and muscle.
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