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Protein phosphatase 2, regulatory subunit B'', alpha

PR72, PR130, PPP2R3A
This gene encodes one of the regulatory subunits of the protein phosphatase 2. Protein phosphatase 2 (formerly named type 2A) is one of the four major Ser/Thr phosphatases and is implicated in the negative control of cell growth and division. Protein phosphatase 2 holoenzymes are heterotrimeric proteins composed of a structural subunit A, a catalytic subunit C, and a regulatory subunit B. The regulatory subunit is encoded by a diverse set of genes that have been grouped into the B/PR55, B'/PR61, and B''/PR72 families. These different regulatory subunits confer distinct enzymatic specificities and intracellular localizations to the holozenzyme. The product of this gene belongs to the B'' family. The B'' family has been further divided into subfamilies. The product of this gene belongs to the alpha subfamily of regulatory subunit B''. Alternative splicing results in multiple transcript variants encoding different isoforms.[provided by RefSeq, Jun 2010] (from NCBI)
Top mentioned proteins: PP2A, ACID, CAN, PCNA, KCNE1
Papers on PR72
Alteration of tight junction gene expression in celiac disease.
Bilbao et al., Barakaldo, Spain. In J Pediatr Gastroenterol Nutr, 2014
RESULTS: Nine genes showed altered expression levels in patients with active disease (CLDN2, PARD6A, ZAK, SYMPK, MYH14, and ACTB were upregulated, whereas MAGI1, TJP1, and PPP2R3A were downregulated).
Protein phosphatase 2A is regulated by protein kinase Cα (PKCα)-dependent phosphorylation of its targeting subunit B56α at Ser41.
Boknik et al., Münster, Germany. In J Biol Chem, 2014
The substrate and therefore the functional specificity of PP2A are determined by the assembly of the enzyme complex with the appropriate regulatory B subunit families, namely B55, B56, PR72, or PR93/PR110.
Structure of the Ca2+-dependent PP2A heterotrimer and insights into Cdc6 dephosphorylation.
Xing et al., Madison, United States. In Cell Res, 2013
The B″/PR72 family of protein phosphatase 2A (PP2A) is an important PP2A family involved in diverse cellular processes, and uniquely regulated by calcium binding to the regulatory subunit.
AMPK activity is regulated by calcium-mediated protein phosphatase 2A activity.
Gerrard et al., Suwŏn, South Korea. In Cell Calcium, 2013
Intracellular calcium mediates protein phosphatase 2A (PP2A), which is in a heterotrimeric complex with the PR72 subunit.
Identification of PP2A complexes and pathways involved in cell transformation.
Hahn et al., Boston, United States. In Cancer Res, 2011
Using a comprehensive loss-of-function approach, we identified 4 PP2A regulatory subunits [B56α, B56γ, PR72/PR130, and PTPA (protein phosphatase 2A activator)], which when suppressed replaced the expression of SV40ST in human cell transformation.
Protein phosphatase 2A PR130/B''alpha1 subunit binds to the SH2 domain-containing inositol polyphosphate 5-phosphatase 2 and prevents epidermal growth factor (EGF)-induced EGF receptor degradation sustaining EGF-mediated signaling.
Janssens et al., Leuven, Belgium. In Faseb J, 2010
To elucidate novel cell biological functions of specific protein phosphatase 2A (PP2A) holoenzymes, we identified and biochemically characterized a complex between the Src homology 2 (SH2) domain-containing inositol polyphosphate 5-phosphatase 2 (SHIP2) and a PP2A holoenzyme comprising PR130/B''alpha1 as a regulatory subunit (PP2A(T130)) in several mammalian cell lines.
Specific regulation of protein phosphatase 2A PR72/B'' subunits by calpain.
Goris et al., Leuven, Belgium. In Biochem Biophys Res Commun, 2009
Now we report partial degradation of PR72/B"alpha2 and PR130/B"alpha1 into a 45-48kDa proteolysis-resistant fragment ('PR45') by the Ca(2+)-dependent protease m-calpain.
Epigenetic analysis of childhood acute lymphoblastic leukemia.
Latif et al., Birmingham, United Kingdom. In Epigenetics, 2009
PPP2R3A (protein phosphatase 2, regulatory subunit B", alpha) was frequently methylated in T (69%) and B (82%)-ALL.
Protein phosphatase 2A is targeted to cell division control protein 6 by a calcium-binding regulatory subunit.
Mumby et al., Dallas, United States. In J Biol Chem, 2008
PP2A can be targeted in a calcium-regulated manner to Cdc6 via the PR70 subunit, where it plays a role in regulating protein phosphorylation and stability.
Diversity in genomic organisation, developmental regulation and distribution of the murine PR72/B" subunits of protein phosphatase 2A.
Janssens et al., Leuven, Belgium. In Bmc Genomics, 2007
Immunohistochemical analysis revealed a striated expression pattern of PR72 and PR130 in heart and skeletal muscle, but not in bladder smooth muscle.
Selection of protein phosphatase 2A regulatory subunits is mediated by the C terminus of the catalytic Subunit.
Janssens et al., Leuven, Belgium. In J Biol Chem, 2007
In this study, we show that PP2A C subunit methylation was not absolutely required for binding the PR61/B' and PR72/B'' subunit families, whereas binding of the PR55/B subunit family was determined by methylation and the nature of the C-terminal amino acid side chain.
The B''/PR72 subunit mediates Ca2+-dependent dephosphorylation of DARPP-32 by protein phosphatase 2A.
Nairn et al., New York City, United States. In Proc Natl Acad Sci U S A, 2007
The B''/PR72 subunit mediates Ca2+-dependent dephosphorylation of DARPP-32 by protein phosphatase 2A.
Identification of novel substrates for human checkpoint kinase Chk1 and Chk2 through genome-wide screening using a consensus Chk phosphorylation motif.
Yun et al., Pusan, South Korea. In Exp Mol Med, 2007
ST5, HDAC5, PGC-1alpha, PP2A PR130, FANCG, GATA3, cyclin G, Rad51D and MAD1a were newly identified as in vitro substrates for Chk1 and/or Chk2.
Characterization of a 3;6 translocation associated with renal cell carcinoma.
Maher et al., Birmingham, United Kingdom. In Genes Chromosomes Cancer, 2007
No known genes were disrupted by the translocation breakpoints but several candidate TSGs (e.g., EPHB1, EPHA7, PPP2R3A RNF184, and STAG1) map within close proximity to the breakpoints.
Wnt/beta-catenin/CBP signaling maintains long-term murine embryonic stem cell pluripotency.
Kahn et al., Shizuoka, Japan. In Proc Natl Acad Sci U S A, 2007
We demonstrate that IQ-1, by targeting the PR72/130 subunit of the serine/threonine phosphatase PP2A, prevents beta-catenin from switching coactivator usage from CBP to p300.
PR72, a novel regulator of Wnt signaling required for Naked cuticle function.
Bernards et al., Amsterdam, Netherlands. In Genes Dev, 2005
PR72 interacts physically and functionally with Naked cuticle. PR72, like Naked cuticle, acts as a negative regulator of the classical Wnt signaling cascade.
Macromolecular complexes regulating cardiac ryanodine receptor function.
Bers, Maywood, United States. In J Mol Cell Cardiol, 2004
calmodulin (CaM), FK-506-binding proteins, protein kinase A, Ca-CaM-dependent protein kinase, phosphatases 1 and 2A, mAKAP, spinophilin, PR130, sorcin, triadin, junctin, calsequestrin and Homer).
Identification and functional analysis of two Ca2+-binding EF-hand motifs in the B"/PR72 subunit of protein phosphatase 2A.
Goris et al., Leuven, Belgium. In J Biol Chem, 2003
two Ca2+-binding EF-hand motifs in the B"/PR72 subunit of protein phosphatase 2A demonstrating the ability or calcium ions to interact with and regulate PP2A
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