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Protein phosphatase 2, regulatory subunit B', delta

The product of this gene belongs to the phosphatase 2A regulatory subunit B family. Protein phosphatase 2A is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell growth and division. It consists of a common heteromeric core enzyme, which is composed of a catalytic subunit and a constant regulatory subunit, that associates with a variety of regulatory subunits. The B regulatory subunit might modulate substrate selectivity and catalytic activity. This gene encodes a delta isoform of the regulatory subunit B56 subfamily. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: PP2A, Akt, ACID, OUT, Cyclin-Dependent Kinase 5
Papers on Ppp2r5d
De novo missense variants in PPP2R5D are associated with intellectual disability, macrocephaly, hypotonia, and autism.
Chung et al., New York City, United States. In Neurogenetics, Jan 2016
PPP2R5D is a regulatory B subunit of PP2A and plays an important role in regulating key neuronal and developmental regulation processes such as PI3K/AKT and glycogen synthase kinase 3 beta (GSK3β)-mediated cell growth, chromatin remodeling, and gene transcriptional regulation.
Mutations in the PP2A regulatory subunit B family genes PPP2R5B, PPP2R5C and PPP2R5D cause human overgrowth.
Rahman et al., Wellington, New Zealand. In Hum Mol Genet, Oct 2015
Prioritisation of functionally relevant genes with multiple unique de novo mutations revealed four mutations in protein phosphatase 2A (PP2A) regulatory subunit B family genes protein phosphatase 2, regulatory Subunit B', beta (PPP2R5B); protein phosphatase 2, regulatory Subunit B', gamma (PPP2R5C); and protein phosphatase 2, regulatory Subunit B', delta (PPP2R5D).
B56δ-related protein phosphatase 2A dysfunction identified in patients with intellectual disability.
Janssens et al., In J Clin Invest, Sep 2015
Ten patients had mutations within a highly conserved acidic loop of the PPP2R5D-encoded B56δ regulatory subunit, with the same E198K mutation present in 6 individuals.
Regulatory B Subunits of Protein Phosphatase 2A Are Involved in Site-specific Regulation of Tau Protein Phosphorylation.
Ahn et al., Seoul, South Korea. In Korean J Physiol Pharmacol, 2014
Down-regulation of PPP2R5D expression decreased tau phosphorylation at Ser-202/Thr-205, Thr-231, and Ser-422, which indicates activation of the tau kinase glycogen synthase kinase 3 beta (GSK3β) by PP2A with PPP2R5D subunit.
Identification of transcriptional and phosphatase regulators as interaction partners of human ADA3, a component of histone acetyltransferase complexes.
Topcu et al., Denizli, Turkey. In Biochem J, 2013
We identified three novel hADA3-interacting partners, a transcriptional regulator, AATF (apoptosis-antagonizing transcription factor), and regulatory subunits of the PP1 (protein phosphatase 1) and PP2A (protein phosphatase 2A) [PPP1R7 (PP1 regulatory subunit 7) and PPP2R5D (PP2A 56 kDa regulatory subunit δ isoform) respectively].
Nuclear life of the voltage-gated Cacnb4 subunit and its role in gene transcription regulation.
Mori et al., Grenoble, France. In Channels (austin), 2013
This re-localization of β 4 is promoted by its interaction with Ppp2r5d a regulatory subunit of PP2A in complex with PP2A itself.
Cacnb4 directly couples electrical activity to gene expression, a process defective in juvenile epilepsy.
De Waard et al., Grenoble, France. In Embo J, 2012
Electrical activity induces Cacnb4 association to Ppp2r5d, a regulatory subunit of PP2A phosphatase, followed by (i) nuclear translocation of Cacnb4/Ppp2r5d/PP2A, (ii) association with the tyrosine hydroxylase (TH) gene promoter through the nuclear transcription factor thyroid hormone receptor alpha (TRα), and (iii) histone binding through association of Cacnb4 with HP1γ concomitantly with Ser(10) histone H3 dephosphorylation by PP2A.
Identification and association analysis of several hundred single nucleotide polymorphisms within candidate genes for back fat thickness in Italian Large White pigs using a selective genotyping approach.
Russo et al., Bologna, Italy. In J Anim Sci, 2012
The list of significant markers also included SNP in additional genes (ABHD16A, ABHD5, ACP2, ALMS1, APOA2, ATP1A2, CALR, COL14A1, CTSF, DARS, DECR1, ENPP1, ESR1, GH1, GHRL, GNMT, IKBKB, JAK3, MTTP, NFKBIA, NT5E, PLAT, PPARG, PPP2R5D, PRLR, RRAGD, RFC2, SDHD, SERPINF1, UBE2H, VCAM1, and WAT).
Mice lacking phosphatase PP2A subunit PR61/B'delta (Ppp2r5d) develop spatially restricted tauopathy by deregulation of CDK5 and GSK3beta.
Janssens et al., Leuven, Belgium. In Proc Natl Acad Sci U S A, 2011
Functional diversity of protein phosphatase 2A (PP2A) enzymes mainly results from their association with distinct regulatory subunits.
Acute regulation of renal Na+/H+ exchanger NHE3 by dopamine: role of protein phosphatase 2A.
Moe et al., Dallas, United States. In Am J Physiol Renal Physiol, 2010
The PP2A regulatory subunit B56δ (coded by the Ppp2r5d gene) directly associates with more than one region of the carboxy-terminal hydrophilic putative cytoplasmic domain of NHE3 (NHE3-cyto), as demonstrated by yeast-two-hybrid, coimmunoprecipitation, blot overlay, and in vitro pull-down assays.
Phosphorylation on the PPP2R5D B regulatory subunit modulates the biochemical properties of protein phosphatase 2A.
Ahn et al., Seoul, South Korea. In Bmb Rep, 2010
Protein kinase A mediated activation of protein phosphatase 2A is enabled by PPP2R5D phosphorylation, which modulates the affinity of the protein phosphatase 2A holoenzyme to its physiological substrates.
The Balpha and Bdelta regulatory subunits of PP2A are necessary for assembly of the CaMKIV.PP2A signaling complex.
Wadzinski et al., Nashville, United States. In Biochem Biophys Res Commun, 2009
these data indicate that the B subunits alpha and delta are essential for the interaction of PP2A with CaMKIV.
Detection of target genes of FOXA transcription factors involved in proliferation control.
Merkulova et al., Novosibirsk, Russia. In Biochemistry (mosc), 2008
Six genes containing clusters of confirmed binding sites--Cul2, Cdc73, Ptk, Pdcd, Creb, and Ppp2r5d--were selected.
Control of mitotic exit by PP2A regulation of Cdc25C and Cdk1.
Virshup et al., Salt Lake City, United States. In Proc Natl Acad Sci U S A, 2008
PP2A:B56delta as a key upstream regulator of Cdk1 activity upon exit from mitosis
An advanced sheep (Ovis aries, 2n = 54) cytogenetic map and assignment of 88 new autosomal loci by fluorescence in situ hybridization and R-banding.
Iannuzzi et al., Napoli, Italy. In Anim Genet, 2007
Eleven loci that were FISH-mapped in sheep (B3GAT2, ASCC3, RARSL, BRD2, POLR1C, PPP2R5D, TNRC5, BAT2, BAT4, CDC5L and OLA-DRA) are unassigned in cattle and goat.
Protein kinase A activates protein phosphatase 2A by phosphorylation of the B56delta subunit.
Nairn et al., New York City, United States. In Proc Natl Acad Sci U S A, 2007
We have found that the A/C subunits of PP2A, in association with the B56delta (or PPP2R5D) regulatory subunit, is an active DARPP-32 phosphatase.
Positive regulation of Raf1-MEK1/2-ERK1/2 signaling by protein serine/threonine phosphatase 2A holoenzymes.
Wadzinski et al., Nashville, United States. In J Biol Chem, 2006
PP2A ABalphaC and ABdeltaC holoenzymes function as positive regulators of Raf1-MEK1/2-ERK1/2 signaling by targeting Raf1
Gonadotropin-releasing hormone retards doxorubicin-induced apoptosis and serine/threonine phosphatase inhibition in ovarian cancer cells.
Tamaya et al., Gifu, Japan. In Oncol Rep, 2005
Gonadotropin-releasing hormone (GnRH) affects the membrane protein phosphatase 2A-associated apoptosis and the enzyme activity in ovarian cancer cells.
Peas-Mea1-Ppp2r5d overlapping gene complex: a transposon mediated-gene formation in mammals.
Mitsui et al., Tsukuba, Japan. In Dna Res, 2003
Human and mouse MEA1/Mea1 is flanked by two overlapping genes, a novel PEAS/Peas in a head-to-head orientation and PPP2R5D/Ppp2r5d in a tail-to-tail orientation making a Peas-Mea1-Ppp2r5d overlapping gene complex (PMP-complex).
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