Growth factor receptor levels are aberrantly high in diverse cancers, driving the proliferation and survival of tumor cells. Understanding the molecular basis for this aberrant elevation has profound clinical implications. Here we show that the pleckstrin homology domain leucine-rich repeat protein phosphatase (PHLPP) suppresses receptor tyrosine kinase (RTK) signaling output by a previously unidentified epigenetic mechanism unrelated to its previously described function as the hydrophobic motif phosphatase for the protein kinase AKT, protein kinase C, and S6 kinase. Specifically, we show that nuclear-localized PHLPP suppresses histone phosphorylation and acetylation, in turn suppressing the transcription of diverse growth factor receptors, including the EGF receptor. These data uncover a much broader role for PHLPP in regulation of growth factor signaling beyond its direct inactivation of AKT: By suppressing RTK levels, PHLPP dampens the downstream signaling output of two major oncogenic pathways, the
The dephosphorylation of the modulator subunit is an essential step in the kinase FA-mediated activation of the ATP,Mg-dependent protein phosphatase. Mg2+ is implicated in this autocatalytic dephosphorylation which is not effected by the addition of phosphoinhibitor-1. Dephosphorylation of free modulator by the catalytic subunit is also largely Mg2+-dependent but can be abolished by phosphoinhibitor-1 in concentrations comparable to the amount of modulator used as substrate (micromolar). The phosphorylase phosphatase activity of the catalytic subunit is inhibited by nanomolar concentrations of phosphoinhibitor-1 and is completely independent of divalent cations ...
Protein serine/threonine phosphatase (PSP)[1] is a form of phosphoprotein phosphatase that acts upon phosphorylated serine/threonine residues. Serine and threonine phosphates are stable under physiological conditions, so a phosphatase enzyme has to remove the phosphate to reverse the regulation signal. Ser/Thr-specific protein phosphatases are regulated partly by their location within the cell and by specific inhibitor proteins. Serine and threonine are amino acids which have similar side-chain compositions that contain a hydroxyl group and thus can be phosphorylated by enzymes called serine/threonine protein kinases. The addition of the phosphate group can be reversed by enzymes called serine/threonine phosphatases. The addition and removal of phosphate groups regulates many cellular pathways involved in cell proliferation, programmed cell death (apoptosis), embryonic development, and cell differentiation. ...
Paclitaxel and docetaxel (taxoids) are chemotherapy agents whose mode of action is through an effect on cellular microtubules. Several studies have investigated their potential in the treatment of myeloid malignancies. The aim of our study was to investigate the potential role of the serine/threonine protein phosphatase system in docetaxel/paclitaxel induced cytotoxicity on HL 60 cells. The IC50 dose of paclitaxel and docetaxel were found as 20 and 5 nM respectively using trypan blue dye exclusion and XTT assays. Treating HL 60 cells with docetaxel and paclitaxel resulted in dose and time dependent cytotoxicity. Docetaxel induced the decrease in the activity of protein phosphatase 1 (PP1) and increase in the activity of PP2 subgroups, while paclitaxel induced the increase in the activity of PP1 and decrease in the activity of PP2 subgroups. Potential use of specific protein phosphatase inhibitors or activators in combination with taxoids will open new windows in the treatment of myeloid ...
Calyculins, highly cytotoxic polyketides, originally isolated from the marine sponge Discodermia calyx by Fusetani and co-workers, belong to the lithistid sponges group. These molecules have become interesting targets for cell biologists and synthetic organic chemists. The serine/threonine protein phosphatases play an essential role in the cellular signalling, metabolism, and cell cycle control. Calyculins express potent protein phosphatase 1 and 2A inhibitory activity, and have therefore become valuable tools for cellular biologists studying intracellular processes and their control by reversible phosphorylation. Calyculins might also play an important role in the development of several diseases such as cancer, neurodegenerative diseases, and type 2-diabetes mellitus. The fascinating structures of calyculins have inspired various groups of synthetic organic chemists to develop total syntheses of the most abundant calyculins A and C. However, with fifteen chiral centres, a cyano-capped tetraene unit, a
plasma membrane, magnesium-dependent protein serine/threonine phosphatase activity, protein serine/threonine phosphatase activity, drought recovery, microtubule cytoskeleton organization, negative regulation of growth, protein dephosphorylation
plasma membrane, magnesium-dependent protein serine/threonine phosphatase activity, protein serine/threonine phosphatase activity
EC 3.1.3.16; recommended name: phosphoprotein phosphatase; other names: protein phosphatase‐1; protein phosphatase‐2A; protein phosphatase‐2B; protein phosphatase‐2C. This name includes enzymes that hydrolyse the serine‐ or threonine‐bound phosphate group from phosphoproteins.. [...] ...
TY - JOUR. T1 - Cloning, Expression, and Catalytic Mechanism of the Low Molecular Weight Phosphotyrosyl Protein Phosphatase from Bovine Heart. AU - Wo, Yu Yuan P.. AU - Zhou, Ming Ming. AU - Stevis, Panayiotis. AU - Davis, June P.. AU - Zhang, Zhong Yin. AU - Van Etten, Robert L.. PY - 1992/2/1. Y1 - 1992/2/1. N2 - The first representative of a group of mammalian, low molecular weight phosphotyrosyl protein phosphatases was cloned, sequenced and expressed in Escherichia coli. Using a 61-mer oligonucleotide probe based on the amino acid sequence of the purified enzyme, several overlapping cDNA clones were isolated from a bovine heart cDNA library. A full-length clone was obtained consisting of a 27-bp 5ʹ3ʹ noncoding region, an open reading frame encoding the expected 157 amino acid protein, and an extensive 3 nontranslated sequence. The identification of the clone as full length was consistent with results obtained in mRNA blotting experiments using poly(A)+ mRNA from bovine heart. The coding ...
Supplementary MaterialsSupplementary Table 1: Venn diagram list in term and preterm labor cerm-2019-03013-suppl1. in placentas with swelling. We also proven that many miRNAs (miR-371a-5p, miR-3065-3p, miR-519b-3p, and miR-373-3p) straight targeted their focus on genes (and had not been modified by LPS treatment. Summary These results offer applicant miRNAs and their focus on genes that may be Ganetespib price utilized as placental biomarkers of swelling. These applicants may be helpful for additional miRNA-based biomarker development. research. The cells had been taken care of at 37C in 5% CO2. The tradition moderate was RPMI-1640 (Gibco, Grand Isle, NY, USA) supplemented with 5% fetal bovine serum (FBS; Gibco) and 1% penicillin-streptomycin (Gibco). HeLa cells (a cervical tumor cell range) had been cultured with Dulbeccos customized Eagle medium (Gibco) containing 5% FBS (Gibco) and 1% penicillin-streptomycin (Gibco). 3. Lipopolysaccharide treatment and miRNA transfection The HTR-8/SVneo ...
The Saccharomyces Genome Database (SGD) provides comprehensive integrated biological information for the budding yeast Saccharomyces cerevisiae.
The catalytic subunit of type 1 protein phosphatase (PP1C) interacts with a large number of polypeptides in eukaryotic cells from yeast to man and these regulatory subunits can both modulate the activ
Phosphoprotein phosphatases, which hydrolyze the phosphoester bonds of phosphoserines, phosphothreonines or phosphotyrosines, play an essential role in signal transduction and actively contribute to the regulation of protein phosphorylation. On the basis of their substrate specificity they are usually divided into phosphoserine and phosphothreonine phosphatases on the one hand, and phosphotyrosine and dual-specificity phosphatases, on the other hand. This division corresponds also to different families of enzymes with different catalytic mechanisms. Genes coding for phosphoserine/threonine phosphatases are less numerous in vertebrate genomes than those for serine /threonine kinases, and the complexity of phosphatases function arises in part from the interactions of catalytic subunits with other proteins.. Prior to the knowledge of their sequence, phosphoserine/threonine phosphatases were classified on the basis of their substrate preference and inhibitor sensitivity. Type 1 protein phosphatases ...
Protein Phosphatase 1: A eukayrotic protein serine-threonine phosphatase subtype that dephosphorylates a wide variety of cellular proteins. The enzyme is comprised of a catalytic subunit and regulatory subunit. Several isoforms of the protein phosphatase catalytic subunit exist due to the presence of multiple genes and the alternative splicing of their mRNAs. A large number of proteins have been shown to act as regulatory subunits for this enzyme. Many of the regulatory subunits have additional cellular functions.
Background: SNF1-related protein kinases 2 (SnRK2s) are key regulators of the plant response to osmotic stress. They are transiently activated in response to drought and salinity. Based on a phylogenetic analysis SnRK2s are divided into three groups. The classification correlates with their response to abscisic acid (ABA); group 1 consists SnRK2s non-activated in response to ABA, group 2, kinases non-activated or weakly activated (depending on the plant species) by ABA treatment, and group 3, ABA-activated kinases. The activity of all SnRK2s is regulated by phosphorylation. It is well established that clade A phosphoprotein phosphatases 2C (PP2Cs) are negative regulators of ABA-activated SnRK2s, whereas regulators of SnRK2s from group 1 remain unidentified. Results: Here, we show that ABI1, a PP2C clade A phosphatase, interacts with SnRK2.4, member of group 1 of the SnRK2 family, dephosphorylates Ser158, whose phosphorylation is needed for the kinase activity, and inhibits the kinase, both in ...
Reversible protein phosphorylation is widely accepted as a major mechanism for the control of biological processes in eukaryotic cells. In plants, reversible protein phosphorylation is involved in processes such as hormonal, pathogenic, or environmental stress responses (Mumby and Walter, 1993; Smith and Walker, 1993; Garbers et al., 1996; Schöntal, 1998;Janssens and Goris, 2001). In this context, Ser/Thr protein phosphatases (PPs) are important regulatory components of many signal transduction pathways (Ingebritsen and Cohen, 1983a; Schöntal, 1998). Several Ser/Thr phosphatases, grouped into different categories, have been identified in a variety of plant species. Specifically, homologs of the 1, 2A, and 2C types of animal PPs have been described in plants (Rodrı́guez, 1998; Lin et al., 1999; Meek et al., 1999). All these types of PPs are distinguished by their different sensitivity to inhibitors and their divalent cation requirements, and are structurally different (for review, see Mumby ...
By reversing the phosphorylation of key regulatory proteins mediated by protein kinases, phosphatases serve as an important complement to kinases and attenuate activated signal transduction pathways. Important classes of phosphatases include both receptor and nonreceptor protein tyrosine phosphatases (PTPs), dual specificity phosphatases (DUSPs), cell cycle regulatory phosphatases, the 4 major serine/threonine protein phosphatase gene families (PP1, PP2A, PP2B, and PP2C), and other increasingly important gene families (PP4, PP5, PP6, and PP7). PTPs regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. DUSPs can dephosphorylate serine and threonine as well as tyrosine residues, primarily targeting MAP kinases. PP1 family members regulate of a variety of cellular processes, such as cell division, glycogen metabolism, muscle contractility, protein synthesis, and HIV-1 viral transcription. PP2A family members negatively regulate ...
Type 1 serine/threonine protein phosphatase catalytic subunit; involved in various processes including glycogen metabolism, sporulation, mitosis; accumulates at mating projections by interaction with Afr1p; interacts with many regulatory subunits; involved in regulation of the nucleocytoplasmic shuttling of Hxk2p; import into nucleus is inhibited during spindle assembly checkpoint arrest ...
About one-third of all proteins in eukaryotic cells are usually phosphorylated at anybody time. various mobile processes was the main topic of an EMBO meeting that was arranged in De Panne Belgium (Sept 19-24 1999 by M.Bollen D.S and Barford.Klumpp. This Europhosphatase meeting attracted 170 individuals from 25 different countries. Book proteins phosphatase (regulators) Proteins phosphatases are categorized into three households predicated on the framework of their catalytic domains. The PPP family members BMS-509744 contains the phosphoserine/phosphothreonine-specific proteins phosphatases PP1 PP2A PP2B (calcineurin) PP4 and PP5. BMS-509744 The PPM family members comprises Mg2+-activated proteins phosphatases such as for example PP2C which also dephosphorylate phosphoserine and phosphothreonine residues. Protein-tyrosine phosphatases and dual-specificity proteins phosphatases which dephosphorylate all three phosphoamino acids participate in the PTP family members. S.Klumpp (Marburg Germany) ...
Protein Phosphatase Inhibitor-2 (I-2) specifically and instantaneously inhibits the catalytic subunit of type I protein phosphatase (PP1) at nanomolar concentrations. In contrast, the inhibition of native forms of PP1
Read "Direct interactions of ABA-insensitive(ABI)-clade protein phosphatase(PP)2Cs with calcium-dependent protein kinases and ABA response element-binding bZIPs may contribute to turning off ABA response, Plant Molecular Biology" on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
Background The malarial parasite, Plasmodium falciparum(Pf), is responsible for nearly 2 million deaths worldwide. However, the mechanisms of cellular signaling in the parasite remain largely...
This gene encodes a serine/threonine phosphatase which is a member of the protein phosphatase catalytic subunit family. Proteins in this family participate in pathways regulated by reversible phosphorylation at serine and threonine residues; many of these pathways are involved in the regulation of cell growth and differentiation. The product of this gene has been shown to participate in signaling pathways in response to hormones or cellular stress, and elevated levels of this protein may be associated with breast cancer development. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2011 ...
Protein phosphatase involved in regulation of Akt and PKC signaling. Mediates dephosphorylation in the C-terminal domain hydrophobic motif of members of the AGC Ser/Thr protein kinase family; specifically acts on Ser-473 of AKT2 and AKT3, Ser-660 of PRKCB and Ser-657 of PRKCA (PubMed:15808505, PubMed:17386267, PubMed:18162466). Isoform 2 seems to have a major role in regulating Akt signaling in hippocampal neurons (By similarity). Akt regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of Ser-473 of Akt triggers apoptosis and suppression of tumor growth. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation (PubMed:18162466). Dephosphorylates STK4 on Thr-387 leading to STK4 activation and apoptosis (PubMed:20513427). Dephosphorylates RPS6KB1 and is involved in regulation of cap-dependent translation ...
To elucidate the roles of protein phosphatases type 1 (PP1) and type 2A (PP2A) in 1,25-dihydroxy-cholecalciferol [1,25(OH)2D3]-induced differentiation of HL-60 cells into monocytes, we examined the enzyme activity and the protein and gene expressions of PP1 and PP2A in these cells. Calyculin-A augmented the 1,25(OH)2D3-induced differentiation of the cells. Treatment of the cells with 1,25(OH)2D3 led to a decrease in PP1-like activity in the cytosol fraction, with a concomitant increase in the membrane and nuclear PP1-like activity, as determined when protein phosphatase activity was assayed using myosin light chain as substrate in the presence of 5 nm okadaic acid. Western blot analysis with antibodies specific for PP1 catalytic subunit isozymes (PP1α, PP1γ, and PP1δ) showed that all three PP1 isozymes were expressed but were differentially distributed in each cellular fraction. Subcellular redistribution of PP1-like activity during 1,25(OH)2D3-induced differentiation was mainly attributed to ...
Aromatase inhibitors (AIs) are effective endocrine therapeutics for postmenopausal women with estrogen receptor (ER)α‑positive breast cancer. However, the efficacy of the treatment is often limited by the onset of AI resistance, owing to the phosphorylation of ERα serine 167 (Ser167). Previous studies have indicated that hyperactivation of the phosphoinositide‑3 kinase/RAC serine/threonine‑protein kinase signaling pathway occurs in AI‑resistant breast cancer models, which coincides with elevated levels of ERα phosphorylation at Ser167. The tumor suppressor serine/threonine‑protein phosphatase 2A (PP2A) regulates the phosphatidylinositol 3‑kinase/RAC serine/threonine‑protein kinase signaling pathway. A previous study indicated that PP2A inhibition decreased ERα Ser167 phosphorylation and estradiol (E2)‑independent cell growth. The present study investigated the potential relevance of PP2A in E2 deprivation‑resistant MCF‑7 cells. E2 depletion reduced the susceptibility of ...
The present series of studies has analyzed two paradoxical observations on the action of H2O2 in neural plasticity: As seen previously (Gahtan et al., 1998), slices of Tg-SOD mice, which apparently overproduce H2O2, expressed lower LTP in response to the tetanic stimulation of afferent pathways than slices from normal mice. Surprisingly, this impairment could be overcome by the addition of H2O2 at a concentration that impaired LTP in the control wt mice. Conversely, aged tg-SOD mice exhibited larger LTP than that produced by wt slices. The effects of H2O2 were reversed in the aged mice; LTP in tg-SOD slices was impaired by the addition of H2O2, whereas LTP of wt slices was enhanced by H2O2.. In an attempt to resolve these paradoxical observations, we found that the young tg-SOD mice and the aged wt mice exhibited elevated levels of endogenous H2O2 and had different protein phosphatase activity with or without exogenous H2O2. Although protein phosphatases are considered to be facilitators of ...
3E7A: Crystal structures of protein phosphatase-1 bound to nodularin-R and tautomycin: a novel scaffold for structure-based drug design of serine/threonine phosphatase inhibitors
Protein phosphatase 5 (PP5) is a novel human protein serine/threonine phosphatase of molecular weight of 58 kDa. It is made up of a C-terminal…
A resource on protein phosphatases, a key class of regulatory proteins. Includes genomic and evolutionary analyses (phosphatomes), classification, disease associationa and an extensive database of protein phosphatase genes.
Staphylococcus aureus; strain: USA300_FPR3757; locus tag: SAUSA300_1112 (SAUSA300_RS06020); symbol: stp1; product: protein phosphatase 2C domain-containing protein
15:30 But Ed didnt realize that the following year while my English didnt improve very much his deteriorated completely LOL. ...
A resource on protein phosphatases, a key class of regulatory proteins. Includes genomic and evolutionary analyses (phosphatomes), classification, disease associationa and an extensive database of protein phosphatase genes.
Type 2A-related Serine-threonine Phosphatase; Functions In The G1/S Transition Of The Mitotic Cycle; Regulator Of COPII Coat Dephosphorylation; Required For ER To Golgi Traffic; Interacts With Hrr25p Kinase; Cytoplasmic And Nuclear Protein That Modulates Functions Mediated By Pkc1p Including Cell Wall And Actin Cytoskeleton Organization; Similar To Human PP6
We are primarily concerned with the development of novel pharmaceuticals to regulate signal transduction pathways that underlie chronic diseases associated with inflammation and aging. The activities of approximately a third of the proteins in vertebrate cells are regulated by reversible phosphorylation at serine and threonine resides. There are almost a thousand different protein kinases, each of which catalyzes the transfer of phosphoryl groups from ATP to a specific set of protein substrates in response to a regulatory input. In contrast, there are just a few phosphoprotein phosphatases to catalyze the removal of these groups. Our research over the past several years has focused on the molecular mechanisms that underlie the regulation of these phosphatases. Through these efforts we have identified potential pharmaceutical targets for the global regulation of phosphatase activity, developed screens for useful therapeutic agents, and characterized pharmaceutical leads that provide a basis for ...
摘要 野生型p53诱导的磷酸酶1(Wild-type p53-induced phosphatase1,Wip1)是PP2C(The type 2C family of protein phosphatases)磷酸酶家族中的一员。在DNA损伤修复中起重要作用,并作为原癌基因受到越来越多的关注。Wip1敲除小鼠虽然能够存活,但寿命缩短,并出现多系统异常,包括生殖系统、免疫体系、内分泌系统、神经系统等,具体表现:雄性生殖器官萎缩及雄性不育、对病原体敏感、T细胞和B细胞功能受损、胰岛素抵抗、体重增长受限、脂肪量减少、焦虑和抑郁样行为增加等。相关机制研究发现,Wip1通过去磷酸化不同蛋白底物而在多种生理和病理过程中发挥重要作用。本文旨在对小鼠Wip1基因缺失所致表型及其初步的分子机制进行综述,为进一步研究Wip1的生物学功能以及哺乳动物体内生理和病理过程的发生机制提供参考。. ...
Antonioli, J.A.; Baer, A.; Vannotti, A., 1965: Alkaline and acide leukocyte phosphatases: pathologic variations, humoral regulation and relation to plasma phosphatases
GSK690693 is a pan-Akt inhibitor targeting Akt1, 2, 3 with IC50 values of 2, 13 and 9 nM, respectively [1, 2]. In addition, it also inhibits AMPK (IC50=50 nM), DAPK3 (IC50=81 nM), PAK4, 5, and 6 (IC50=10, 52, 6 nM), as well as the members of AGC kinase fa
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JPT Peptide Technologies is a DIN ISO 9001:2015 certified and GCLP compliant integrated provider of innovative peptide based catalog products and custom services.
Data Availability StatementThe datasets generated and/or analyzed during the current research are available for the GenBank repository, https://www. BcsZ had been 8.86?mg/mL and 0.3?M/minmg, respectively.. ...
dict.cc | Übersetzungen für leukocyte phosphatase im Englisch-Deutsch-Wörterbuch, mit echten Sprachaufnahmen, Illustrationen, Beugungsformen, ...
SBI-425 是一种有效的,选择性和口服生物可利用的 TNAP 抑制剂。长期施用 SBI-425 可有效地达到并抑制脉管系统中的 TNAP,改善心血管参数和存活,并且其剂量不会引起骨的可检测变化。- 高纯度,全球文献引用。
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Signal transductionRegulatory functionsProtein interactionsPhr family secreted Rap phosphatase inhibitor (TIGR04429; HMM-score: 12.4) ...
TY - JOUR. T1 - A ceramide-activated protein phosphatase mediates ceramide-induced G1 arrest of Saccharomyces cerevisiae. AU - Nickels, Joseph T.. AU - Broach, James R.. PY - 1996/2/15. Y1 - 1996/2/15. N2 - Certain mammalian growth modulators, such as tumor necrosis factor α, interleukin-1β, and γ-interferon, induce an antiproliferative response-terminal differentiation, apoptosisis, or cell cycle arrest-through a novel signal transduction pathway mediated by the lipid ceramide as a second messenger. Both a ceramide-activated protein phosphatase and a ceramide-activated protein kinase have been implicated in transmitting the signals elicited by ceramide. We have determined that ceramide addition to the yeast Saccharomyces causes a similar antiproliferative response, resulting in arrest of cells in the G1 phase of the cell cycle. We have also determined that yeast cells contain a ceramide-activated protein phosphatase composed of regulatory subunits encoded by TPD3 and CDC55 and a catalytic ...
Phosphodiesterase type 3B (PDE3B) has been shown to be activated and phosphorylated in response to insulin and hormones that increase cAMP. In order to study serine/threonine protein phosphatases involved in the regulation of rat adipocyte PDE3B, we investigated the phosphorylation and activation of PDE3B in vivoin response to phosphatase inhibitors and the dephosphorylation and deactivation of PDE3B in vitroby phosphatases purified from rat adipocyte homogenates. Okadaic acid and calyculin A induced dose- and time-dependent activation of PDE3B. Maximal effects were obtained after 30 min using 1 μM okadaic acid (1.8-fold activation) and 300 nM calyculin A (4-fold activation), respectively. Tautomycin and cyclosporin A did not induce activation of PDE3B. Incubation of adipocytes with 300 nM calyculin A inhibited protein phosphatase (PP) 1 and PP2A completely. Okadaic acid (1 μM) reduced PP2A activity by approx. 50% but did not affect PP1 activity, and 1 μM tautomycin reduced PP1 activity by ...
Apoptosis is important for tissue homeostasis and is the mechanism of cell death induced by many anticancer agents. The apoptotic machinery is present in all cells, such that tight regulation must exist to prevent untimely cell and tissue death. To avert apoptotic death, cells utilize survival signaling pathways including the PI3 kinase/Akt and MEK/ERK pathways. Inhibitors of serine/threonine protein phosphatases can inhibit drug-induced apoptosis, implicating these phosphatases in regulation of apoptotic pathways. Here, we determined which protein phosphatases (PP) are critical for this protection from apoptosis, and investigated the relationship between phosphatases and survival pathways. An apoptotic signal can be delivered through a receptor pathway or via drug-induced stress that triggers death via mitochondrial events. Chemical inhibitors of protein phosphatases, calyculin A, okadaic acid and tautomycin, prevented anisomycin-induced apoptosis, a model of the latter pathway. Concentrations ...
Apoptosis is important for tissue homeostasis and is the mechanism of cell death induced by many anticancer agents. The apoptotic machinery is present in all cells, such that tight regulation must exist to prevent untimely cell and tissue death. To avert apoptotic death, cells utilize survival signaling pathways including the PI3 kinase/Akt and MEK/ERK pathways. Inhibitors of serine/threonine protein phosphatases can inhibit drug-induced apoptosis, implicating these phosphatases in regulation of apoptotic pathways. Here, we determined which protein phosphatases (PP) are critical for this protection from apoptosis, and investigated the relationship between phosphatases and survival pathways. An apoptotic signal can be delivered through a receptor pathway or via drug-induced stress that triggers death via mitochondrial events. Chemical inhibitors of protein phosphatases, calyculin A, okadaic acid and tautomycin, prevented anisomycin-induced apoptosis, a model of the latter pathway. Concentrations ...
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