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Journal articles on the topic 'Phosphoprotein phosphatases'

Author: Grafiati

Published: 4 June 2021

Last updated: 30 July 2024

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1

Shacter, Emily, Joseph A. McClure, Edward D. Korn, and P. Boon Chock. "Immunological characterization of phosphoprotein phosphatases." Archives of Biochemistry and Biophysics 242, no. 2 (November 1985): 523–31. http://dx.doi.org/10.1016/0003-9861(85)90239-5.

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2

Li, Qiang, Minglong Li, Huiying Ma, Man Xue, Tong Chen, Xiaodong Ding, Shuzhen Zhang, and Jialei Xiao. "Quantitative Phosphoproteomic Analysis Provides Insights into the Sodium Bicarbonate Responsiveness of Glycine max." Biomolecules 13, no. 10 (October 13, 2023): 1520. http://dx.doi.org/10.3390/biom13101520.

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Sodium bicarbonate stress caused by NaHCO3 is one of the most severe abiotic stresses affecting agricultural production worldwide. However, little attention has been given to the molecular mechanisms underlying plant responses to sodium bicarbonate stress. To understand phosphorylation events in signaling pathways triggered by sodium bicarbonate stress, TMT-labeling-based quantitative phosphoproteomic analyses were performed on soybean leaf and root tissues under 50 mM NaHCO3 treatment. In the present study, a total of 7856 phosphopeptides were identified from cultivated soybeans (Glycine max

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3

Vincent, John B., and Bruce A. Averill. "Sequence homology between purple acid phosphatases and phosphoprotein phosphatases." FEBS Letters 263, no. 2 (April 24, 1990): 265–68. http://dx.doi.org/10.1016/0014-5793(90)81389-6.

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4

Zhang, Qingxiu, and Francois X. Claret. "Phosphatases: The New Brakes for Cancer Development?" Enzyme Research 2012 (October 31, 2012): 1–11. http://dx.doi.org/10.1155/2012/659649.

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The phosphatidylinositol 3-kinase (PI3K) pathway plays a pivotal role in the maintenance of processes such as cell growth, proliferation, survival, and metabolism in all cells and tissues. Dysregulation of the PI3K/Akt signaling pathway occurs in patients with many cancers and other disorders. This aberrant activation of PI3K/Akt pathway is primarily caused by loss of function of all negative controllers known as inositol polyphosphate phosphatases and phosphoprotein phosphatases. Recent studies provided evidence of distinct functions of the four main phosphatases—phosphatase and tensin homolo

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5

Miller, W. Todd. "Tyrosine Phosphoprotein Phosphatases. Barry J. Goldstein." Quarterly Review of Biology 74, no. 4 (December 1999): 464–65. http://dx.doi.org/10.1086/394141.

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6

Moorhead, Greg B. G., Veerle De Wever, George Templeton, and David Kerk. "Evolution of protein phosphatases in plants and animals." Biochemical Journal 417, no. 2 (December 23, 2008): 401–9. http://dx.doi.org/10.1042/bj20081986.

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Protein phosphorylation appears to be a universal mechanism of protein regulation. Genomics has provided the means to compile inventories of protein phosphatases across a wide selection of organisms and this has supplied insights into the evolution of this group of enzymes. Protein phosphatases evolved independently several times yielding the groups we observe today. Starting from a core catalytic domain, phosphatases evolved by a series of gene duplication events and by adopting the use of regulatory subunits and/or fusion with novel functional modules or domains. Recent analyses also suggest

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7

Miskei, Márton, Csaba Ádám, László Kovács, Zsolt Karányi, and Viktor Dombrádi. "Molecular Evolution of Phosphoprotein Phosphatases in Drosophila." PLoS ONE 6, no. 7 (July 15, 2011): e22218. http://dx.doi.org/10.1371/journal.pone.0022218.

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8

Butler, Trent, Jonathan Paul, Nick Europe-Finner, Roger Smith, and Eng-Cheng Chan. "Role of serine-threonine phosphoprotein phosphatases in smooth muscle contractility." American Journal of Physiology-Cell Physiology 304, no. 6 (March 15, 2013): C485—C504. http://dx.doi.org/10.1152/ajpcell.00161.2012.

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The degree of phosphorylation of myosin light chain 20 (MLC20) is a major determinant of force generation in smooth muscle. Myosin phosphatases (MPs) contain protein phosphatase (PP) 1 as catalytic subunits and are the major enzymes that dephosphorylate MLC20. MP regulatory targeting subunit 1 (MYPT1), the main regulatory subunit of MP in all smooth muscles, is a key convergence point of contractile and relaxatory pathways. Combinations of regulatory mechanisms, including isoform splicing, multiple phosphorylation sites, and scaffolding proteins, modulate MYPT1 activity with tissue and agonist

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9

Garvanska, Dimitriya H., and Jakob Nilsson. "Specificity determinants of phosphoprotein phosphatases controlling kinetochore functions." Essays in Biochemistry 64, no. 2 (June 5, 2020): 325–36. http://dx.doi.org/10.1042/ebc20190065.

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Abstract Kinetochores are instrumental for accurate chromosome segregation by binding to microtubules in order to move chromosomes and by delaying anaphase onset through the spindle assembly checkpoint (SAC). Dynamic phosphorylation of kinetochore components is key to control these activities and is tightly regulated by temporal and spatial recruitment of kinases and phosphoprotein phosphatases (PPPs). Here we focus on PP1, PP2A-B56 and PP2A-B55, three PPPs that are important regulators of mitosis. Despite the fact that these PPPs share a very similar active site, they target unique ser/thr ph

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10

Sahin, Ali, Francesca G. Tencalla, Daniel R. Dietrich, Konstanze Mez, and Hanspeter Naegeli. "Enzymatic analysis of liver samples from rainbow trout for diagnosis of blue-green algae-induced toxicosis." American Journal of Veterinary Research 56, no. 8 (August 1, 1995): 1110–15. http://dx.doi.org/10.2460/ajvr.1995.56.08.1110.

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SUMMARY Microcystin and related toxic peptides produced by cyanobacteria (blue-green algae) are potent and selective inhibitors of protein phosphatases 1 and 2A. We adapted existing enzymatic techniques to analyze the liver of rainbow trout after oral administration of hepatotoxic cyanobacteria. Liver tissue was removed 3 and 12 hours after treatment, and phosphatase activity was determined in liver extracts, using a specific phosphoprotein substrate. In all samples from fish exposed to toxic cyanobacteria, phosphatase activity was suppressed, whereas the control enzyme, lactate dehydrogenase,

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11

MISTRY, Sucharita J., Heng-Chun LI, and George F. ATWEH. "Role for protein phosphatases in the cell-cycle-regulated phosphorylation of stathmin." Biochemical Journal 334, no. 1 (August 15, 1998): 23–29. http://dx.doi.org/10.1042/bj3340023.

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Stathmin is a major cytosolic phosphoprotein that regulates microtubule dynamics during the assembly of the mitotic spindle. The activity of stathmin itself is regulated by changes in its state of phosphorylation during the transition from interphase to metaphase. For a better understanding of the regulation of stathmin activity during the cell cycle, we explored the mechanism(s) responsible for the decrease in the level of phosphorylation of stathmin as cells complete mitosis and enter a new G1 phase. We show that stathmin mRNA and protein are expressed constitutively throughout the different

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12

Wheeler-Jones, Caroline P. D., Rebecca A. Houliston, and Jeremy D. Pearson. "Inhibitors of phosphoprotein phosphatases modulate p42mapk phosphorylation in endothelium." Blood Coagulation & Fibrinolysis 6, no. 2 (April 1995): 173. http://dx.doi.org/10.1097/00001721-199504000-00068.

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13

Burns, Chris J., Shân L. Gyles, Shanta J. Persaud, David Sugden, Barbara J. Whitehouse, and Peter M. Jones. "Phosphoprotein Phosphatases Regulate Steroidogenesis by Influencing StAR Gene Transcription." Biochemical and Biophysical Research Communications 273, no. 1 (June 2000): 35–39. http://dx.doi.org/10.1006/bbrc.2000.2890.

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14

Ford, S. L., D. R. E. Abayasekara, S. J. Persaud, and P. M. Jones. "Role of phosphoprotein phosphatases in the corpus luteum: I Identification and characterisation of serine/threonine phosphoprotein phosphatases in isolated rat luteal cells." Journal of Endocrinology 150, no. 2 (August 1996): 205–11. http://dx.doi.org/10.1677/joe.0.1500205.

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Abstract Although the role of protein kinases and phosphorylation in steroidogenesis has received much attention, very little is known about the activities of phosphoprotein phosphatases (PP) and dephosphorylation in steroidogenic tissues. The aims of the present study were therefore to identify which of those serine/threonine PPs more commonly involved in intracellular signalling are expressed in rat luteal cells; to quantify, in vitro, the effects of inhibitors on PP activity extracted from purified rat luteal cells; and to measure the effects of PP inhibitors on the phosphorylation of endog

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15

Moradi, Atieh, Shuaijian Dai, Emily Oi Ying Wong, Guang Zhu, Fengchao Yu, Hon-Ming Lam, Zhiyong Wang, et al. "Isotopically Dimethyl Labeling-Based Quantitative Proteomic Analysis of Phosphoproteomes of Soybean Cultivars." Biomolecules 11, no. 8 (August 16, 2021): 1218. http://dx.doi.org/10.3390/biom11081218.

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Isotopically dimethyl labeling was applied in a quantitative post-translational modification (PTM) proteomic study of phosphoproteomic changes in the drought responses of two contrasting soybean cultivars. A total of 9457 phosphopeptides were identified subsequently, corresponding to 4571 phosphoprotein groups and 3889 leading phosphoproteins, which contained nine kinase families consisting of 279 kinases. These phosphoproteins contained a total of 8087 phosphosites, 6106 of which were newly identified and constituted 54% of the current soybean phosphosite repository. These phosphosites were c

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16

Abbasian, Nima, James O. Burton, Karl E. Herbert, Barbara-Emily Tregunna, Jeremy R. Brown, Maryam Ghaderi-Najafabadi, Nigel J. Brunskill, Alison H. Goodall, and Alan Bevington. "Hyperphosphatemia, Phosphoprotein Phosphatases, and Microparticle Release in Vascular Endothelial Cells." Journal of the American Society of Nephrology 26, no. 9 (March 5, 2015): 2152–62. http://dx.doi.org/10.1681/asn.2014070642.

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17

Rietz, A., and JP Spiers. "The relationship between the MMP system, adrenoceptors and phosphoprotein phosphatases." British Journal of Pharmacology 166, no. 4 (May 17, 2012): 1225–43. http://dx.doi.org/10.1111/j.1476-5381.2012.01917.x.

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18

Taylor, William P., and Theodore S. Widlanski. "Charged with meaning: the structure and mechanism of phosphoprotein phosphatases." Chemistry & Biology 2, no. 11 (November 1995): 713–18. http://dx.doi.org/10.1016/1074-5521(95)90098-5.

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19

Mivechi, N. F., L. D. Trainor, and G. M. Hahn. "Purified Mammalian HSP-70 kDa Activates Phosphoprotein Phosphatases in Vitro." Biochemical and Biophysical Research Communications 192, no. 2 (April 1993): 954–63. http://dx.doi.org/10.1006/bbrc.1993.1508.

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20

Smith, Robert D., and John C. Walker. "Expression of multiple type 1 phosphoprotein phosphatases in Arabidopsis thaliana." Plant Molecular Biology 21, no. 2 (January 1993): 307–16. http://dx.doi.org/10.1007/bf00019946.

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21

Pereira, Susana R., Vítor M. Vasconcelos, and Agostinho Antunes. "The phosphoprotein phosphatase family of Ser/Thr phosphatases as principal targets of naturally occurring toxins." Critical Reviews in Toxicology 41, no. 2 (February 2011): 83–110. http://dx.doi.org/10.3109/10408444.2010.515564.

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22

DESDOUITS, Frédéric, C. Julio SICILIANO, C. Angus NAIRN, Paul GREENGARD, and Jean-Antoine GIRAULT. "Dephosphorylation of Ser-137 in DARPP-32 by protein phosphatases 2A and 2C: different roles in vitro and in striatonigral neurons." Biochemical Journal 330, no. 1 (February 15, 1998): 211–16. http://dx.doi.org/10.1042/bj3300211.

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DARPP-32 (dopamine- and cAMP-regulated phosphoprotein, Mr = 32000) is highly expressed in striatonigral neurons in which its phosphorylation is regulated by several neurotransmitters including dopamine and glutamate. DARPP-32 becomes a potent inhibitor of protein phosphatase 1 when it is phosphorylated on Thr-34 by cAMP- or cGMP-dependent protein kinases. DARPP-32 is also phosphorylated on Ser-137 by protein kinase CK1 (CK1), in vitro and in vivo. This phosphorylation has an important regulatory role since it inhibits the dephosphorylation of Thr-34 by calcineurin in vitro and in striatonigral

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23

Palmer, Frederick B. St C. "Identification of the phosphomonoesterases that hydrolyze lysopolyphosphoinositides in rat brain and liver." Biochemistry and Cell Biology 65, no. 10 (October 1, 1987): 890–98. http://dx.doi.org/10.1139/o87-115.

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The phosphatase activities responsible for the sequential dephosphorylation of lysophosphatidylinositol 4,5-bisphosphate (lysoPtdIns(4,5)P2) to lysophosphatidylinositol that precedes reacylation in rat brain and liver microsomes were characterized. LysoPtdIns(4,5)P2 and the intermediate lysophosphatidylinositol 4-phosphate (lysoPtdIns4P) were hydrolyzed by two distinct phosphatase activities which were distinguishable by their substrate and cation requirements. The lysoPtdIns(4,5)P2 phosphatase activity was Mg2+ dependent and partially inhibited by Ca2+, excess Mg2+, and cationic detergent (ce

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24

Ohno, J., K. Fukuyama, A. Hara, and W. L. Epstein. "Immuno- and enzyme-histochemical detection of phosphoprotein phosphatase in rat epidermis." Journal of Histochemistry & Cytochemistry 37, no. 5 (May 1989): 629–34. http://dx.doi.org/10.1177/37.5.2539408.

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A phosphoprotein phosphatase (PPase: EC 3.1.3.2) was recently purified from rat epidermis. The enzyme dephosphorylates phosphoprotein, and its properties, such as pH optimum, inhibitor spectrum, and Fe2+ activation, differ from those of other soluble phosphatases. We investigated in 2-day-old rat skin the distribution of immunologically detectable PPase and intracellular localization of PPase activity. The reaction of rabbit monospecific anti-PPase IgG was identified in granular and cornified cells by the avidin-biotin complex method. For activity staining, basic principles of the Gomori lead-

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25

Pazy, Y., M. A. Motaleb, M. T. Guarnieri, N. W. Charon, R. Zhao, and R. E. Silversmith. "Identical phosphatase mechanisms achieved through distinct modes of binding phosphoprotein substrate." Proceedings of the National Academy of Sciences 107, no. 5 (January 14, 2010): 1924–29. http://dx.doi.org/10.1073/pnas.0911185107.

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Two-component signal transduction systems are widespread in prokaryotes and control numerous cellular processes. Extensive investigation of sensor kinase and response regulator proteins from many two-component systems has established conserved sequence, structural, and mechanistic features within each family. In contrast, the phosphatases which catalyze hydrolysis of the response regulator phosphoryl group to terminate signal transduction are poorly understood. Here we present structural and functional characterization of a representative of the CheC/CheX/FliY phosphatase family. The X-ray cry

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26

Mukhopadhyay, Subhendu, Vinayak Kapatral, Wenbin Xu, and A. M. Chakrabarty. "Characterization of a Hank’s Type Serine/Threonine Kinase and Serine/Threonine Phosphoprotein Phosphatase inPseudomonas aeruginosa." Journal of Bacteriology 181, no. 21 (November 1, 1999): 6615–22. http://dx.doi.org/10.1128/jb.181.21.6615-6622.1999.

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ABSTRACT Pseudomonas aeruginosa is an opportunistic pathogen that causes infections in eye, urinary tract, burn, and immunocompromised patients. We have cloned and characterized a serine/threonine (Ser/Thr) kinase and its cognate phosphoprotein phosphatase. By using oligonucleotides from the conserved regions of Ser/Thr kinases of mycobacteria, an 800-bp probe was used to screenP. aeruginosa PAO1 genomic library. A 20-kb cosmid clone was isolated, from which a 4.5-kb DNA with two open reading frames (ORFs) were subcloned. ORF1 was shown to encode Ser/Thr phosphatase (Stp1), which belongs to th

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27

Perry, M. D., and G. I. Sandle. "Regulation of colonic apical potassium (BK) channels by cAMP and somatostatin." American Journal of Physiology-Gastrointestinal and Liver Physiology 297, no. 1 (July 2009): G159—G167. http://dx.doi.org/10.1152/ajpgi.00132.2009.

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High-conductance apical K+(BK) channels are present in surface colonocytes of mammalian (including human) colon. Their location makes them well fitted to contribute to the excessive intestinal K+losses often associated with infective diarrhea. Since many channel proteins are regulated by phosphorylation, we evaluated the roles of protein kinase A (PKA) and phosphatases in the modulation of apical BK channel activity in surface colonocytes from rat distal colon using patch-clamp techniques, having first increased channel abundance by chronic dietary K+enrichment. We found that PKA activation us

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28

Lajarín-Cuesta, Rocío, Raquel L. Arribas, and Cristóbal De Los Ríos. "Ligands for Ser/Thr phosphoprotein phosphatases: a patent review (2005-2015)." Expert Opinion on Therapeutic Patents 26, no. 3 (February 7, 2016): 389–407. http://dx.doi.org/10.1517/13543776.2016.1135903.

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29

Ádám, Csaba, László Henn, Márton Miskei, Miklós Erdélyi, Péter Friedrich, and Viktor Dombrádi. "Conservation of male-specific expression of novel phosphoprotein phosphatases in Drosophila." Development Genes and Evolution 220, no. 3-4 (July 15, 2010): 123–28. http://dx.doi.org/10.1007/s00427-010-0332-6.

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30

Pidoux, Guillaume, and Kjetil Taskén. "Specificity and spatial dynamics of protein kinase A signaling organized by A-kinase-anchoring proteins." Journal of Molecular Endocrinology 44, no. 5 (February 11, 2010): 271–84. http://dx.doi.org/10.1677/jme-10-0010.

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Protein phosphorylation is the most common post-translational modification observed in cell signaling and is controlled by the balance between protein kinase and phosphatase activities. The cAMP–protein kinase A (PKA) pathway is one of the most studied and well-known signal pathways. To maintain a high level of specificity, the cAMP–PKA pathway is tightly regulated in space and time. A-kinase-anchoring proteins (AKAPs) target PKA to specific substrates and distinct subcellular compartments providing spatial and temporal specificity in the mediation of biological effects controlled by the cAMP–

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31

Turowski, Patric, Timothy Myles, Brian A. Hemmings, Anne Fernandez, and Ned J. C. Lamb. "Vimentin Dephosphorylation by Protein Phosphatase 2A Is Modulated by the Targeting Subunit B55." Molecular Biology of the Cell 10, no. 6 (June 1999): 1997–2015. http://dx.doi.org/10.1091/mbc.10.6.1997.

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The intermediate filament protein vimentin is a major phosphoprotein in mammalian fibroblasts, and reversible phosphorylation plays a key role in its dynamic rearrangement. Selective inhibition of type 2A but not type 1 protein phosphatases led to hyperphosphorylation and concomitant disassembly of vimentin, characterized by a collapse into bundles around the nucleus. We have analyzed the potential role of one of the major protein phosphatase 2A (PP2A) regulatory subunits, B55, in vimentin dephosphorylation. In mammalian fibroblasts, B55 protein was distributed ubiquitously throughout the cyto

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32

Seok, Seung-Hyeon. "Structural Insights into Protein Regulation by Phosphorylation and Substrate Recognition of Protein Kinases/Phosphatases." Life 11, no. 9 (September 13, 2021): 957. http://dx.doi.org/10.3390/life11090957.

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Protein phosphorylation is one of the most widely observed and important post-translational modification (PTM) processes. Protein phosphorylation is regulated by protein kinases, each of which covalently attaches a phosphate group to an amino acid side chain on a serine (Ser), threonine (Thr), or tyrosine (Tyr) residue of a protein, and by protein phosphatases, each of which, conversely, removes a phosphate group from a phosphoprotein. These reversible enzyme activities provide a regulatory mechanism by activating or deactivating many diverse functions of proteins in various cellular processes

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33

Whalley, T., I. Crossley, and M. Whitaker. "Phosphoprotein inhibition of calcium-stimulated exocytosis in sea urchin eggs." Journal of Cell Biology 113, no. 4 (May 15, 1991): 769–78. http://dx.doi.org/10.1083/jcb.113.4.769.

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We have investigated the role of protein phosphorylation in the control of exocytosis in sea urchin eggs by treating eggs with a thio-analogue of ATP. ATP gamma S (adenosine 5'-O-3-thiotriphosphate) is a compound which can be used as a phosphoryl donor by protein kinases, leading to irreversible protein thiophosphorylation (Gratecos, D., and E.H. Fischer. 1974. Biochem. Biophys. Res. Commun. 58:960-967). Microinjection of ATP gamma S inhibits cortical granule exocytosis, but has no effect on the sperm-egg signal transduction mechanisms which normally cause exocytosis by generating an increase

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34

Al-Nedawi, K. N., Z. Pawłowska, and C. S. Cierniewski. "Interferon gamma bound to endothelial cells is phosphorylated by ecto-protein kinases." Acta Biochimica Polonica 46, no. 3 (September 30, 1999): 693–702. http://dx.doi.org/10.18388/abp.1999_4141.

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The presence of protein kinase activity and its phosphorylated products has been demonstrated on the outer surface of the plasma membrane of endothelial cells. Extracellular phosphorylation was detected by incubation of primary endothelial cells (HUVEC's) and endothelial cell line EA.hy 926 with [gamma-32P]ATP. The reaction products were subjected to SDS/PAGE, autoradiography and scanning densitometry. Under the experimental conditions, five proteins with apparent molecular masses of 19, 23, 55, 88, and 110 kDa were prominently phosphorylated in both types of cells. Phosphorylation of the 19 k

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35

Comolli, J., W. Taylor, J. Rehman, and J. W. Hastings. "Inhibitors of Serine/Threonine Phosphoprotein Phosphatases Alter Circadian Properties in Gonyaulax polyedra." Plant Physiology 111, no. 1 (May 1, 1996): 285–91. http://dx.doi.org/10.1104/pp.111.1.285.

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36

Macaulay, S. L., Julie D. Newman, J. D. Mc Armstrong, and J. Bornstein. "Activation of phosphoprotein phosphatases by growth hormone sequences with insulin-like activity." Molecular and Cellular Biochemistry 74, no. 1 (March 1987): 95–101. http://dx.doi.org/10.1007/bf00221916.

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37

Wasserman, Jason S., Felicity Feiser, Seren Palacio, Kishan Patel, Joy Gonzalez, Holly Fowle, and Xavier Graña. "Protocol to assess substrate dephosphorylation by serine/threonine phosphoprotein phosphatases in vitro." STAR Protocols 4, no. 2 (June 2023): 102148. http://dx.doi.org/10.1016/j.xpro.2023.102148.

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38

Polanowska-Grabowska, Renata, Carl G. Simon, Rocco Falchetto, Jeffrey Shabanowitz, Donald F. Hunt, and Adrian R. L. Gear. "Platelet Adhesion to Collagen Under Flow Causes Dissociation of a Phosphoprotein Complex of Heat-Shock Proteins and Protein Phosphatase 1." Blood 90, no. 4 (August 15, 1997): 1516–26. http://dx.doi.org/10.1182/blood.v90.4.1516.

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AbstractPhosphorylation/dephosphorylation events in human blood platelets were investigated during their adhesion to collagen under flow conditions. Using 32P-labeled platelets and one-dimensional gel electrophoresis, we found that adhesion to collagen mediated primarily by the α2β1 integrin resulted in a strong dephosphorylation of several protein bands. Neither adhesion to polylysine nor thrombin-induced aggregation caused similar protein dephosphorylation. In addition, treatment with okadaic acid (OA), an inhibitor of serine/threonine protein phosphatases type 1 (PP1) and 2A (PP2A), caused

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39

Polanowska-Grabowska, Renata, Carl G. Simon, Rocco Falchetto, Jeffrey Shabanowitz, Donald F. Hunt, and Adrian R. L. Gear. "Platelet Adhesion to Collagen Under Flow Causes Dissociation of a Phosphoprotein Complex of Heat-Shock Proteins and Protein Phosphatase 1." Blood 90, no. 4 (August 15, 1997): 1516–26. http://dx.doi.org/10.1182/blood.v90.4.1516.1516_1516_1526.

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Phosphorylation/dephosphorylation events in human blood platelets were investigated during their adhesion to collagen under flow conditions. Using 32P-labeled platelets and one-dimensional gel electrophoresis, we found that adhesion to collagen mediated primarily by the α2β1 integrin resulted in a strong dephosphorylation of several protein bands. Neither adhesion to polylysine nor thrombin-induced aggregation caused similar protein dephosphorylation. In addition, treatment with okadaic acid (OA), an inhibitor of serine/threonine protein phosphatases type 1 (PP1) and 2A (PP2A), caused signific

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40

Nilsson, Jakob. "Protein phosphatases in the regulation of mitosis." Journal of Cell Biology 218, no. 2 (November 16, 2018): 395–409. http://dx.doi.org/10.1083/jcb.201809138.

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The accurate segregation of genetic material to daughter cells during mitosis depends on the precise coordination and regulation of hundreds of proteins by dynamic phosphorylation. Mitotic kinases are major regulators of protein function, but equally important are protein phosphatases that balance their actions, their coordinated activity being essential for accurate chromosome segregation. Phosphoprotein phosphatases (PPPs) that dephosphorylate phosphoserine and phosphothreonine residues are increasingly understood as essential regulators of mitosis. In contrast to kinases, the lack of a pron

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41

Zgajnar, Nadia R., Cristina Daneri-Becerra, Ana Cauerhff, and Mario D. Galigniana. "The Scaffold Immunophilin FKBP51 Is a Phosphoprotein That Undergoes Dynamic Mitochondrial-Nuclear Shuttling." Cells 11, no. 23 (November 25, 2022): 3771. http://dx.doi.org/10.3390/cells11233771.

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The immunophilin FKBP51 forms heterocomplexes with molecular chaperones, protein-kinases, protein-phosphatases, autophagy-related factors, and transcription factors. Like most scaffold proteins, FKBP51 can use a simple tethering mechanism to favor the efficiency of interactions with partner molecules, but it can also exert more complex allosteric controls over client factors, the immunophilin itself being a putative regulation target. One of the simplest strategies for regulating pathways and subcellular localization of proteins is phosphorylation. In this study, it is shown that scaffold immu

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Wagner, Volker, Gunther Geßner, Ines Heiland, Marc Kaminski, Susan Hawat, Kai Scheffler, and Maria Mittag. "Analysis of the Phosphoproteome of Chlamydomonas reinhardtii Provides New Insights into Various Cellular Pathways." Eukaryotic Cell 5, no. 3 (March 2006): 457–68. http://dx.doi.org/10.1128/ec.5.3.457-468.2006.

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ABSTRACT The unicellular flagellated green alga Chlamydomonas reinhardtii has emerged as a model organism for the study of a variety of cellular processes. Posttranslational control via protein phosphorylation plays a key role in signal transduction, regulation of gene expression, and control of metabolism. Thus, analysis of the phosphoproteome of C. reinhardtii can significantly enhance our understanding of various regulatory pathways. In this study, we have grown C. reinhardtii cultures in the presence of an inhibitor of Ser/Thr phosphatases to increase the phosphoprotein pool. Phosphopeptid

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Chen, Lei, Qingling He, Yamin Liu, Yafei Wu, Dongsheng Ni, Jianing Liu, Yanxia Hu, et al. "PPP3CB Inhibits Migration of G401 Cells via Regulating Epithelial-to-Mesenchymal Transition and Promotes G401 Cells Growth." International Journal of Molecular Sciences 20, no. 2 (January 11, 2019): 275. http://dx.doi.org/10.3390/ijms20020275.

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PPP3CB belongs to the phosphoprotein phosphatases (PPPs) group. Although the majority of the PPP family play important roles in the epithelial-to-mesenchymal transition (EMT) of tumor cells, little is known about the function of PPP3CB in the EMT process. Here, we found PPP3CB had high expression in kidney mesenchymal-like cells compared with kidney epithelial-like cells. Knock-down of PPP3CB downregulated epithelial marker E-cadherin and upregulated mesenchymal marker Vimentin, promoting the transition of cell states from epithelial to mesenchymal and reorganizing the actin cytoskeleton which

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Lu, D. J., A. Takai, T. L. Leto, and S. Grinstein. "Modulation of neutrophil activation by okadaic acid, a protein phosphatase inhibitor." American Journal of Physiology-Cell Physiology 262, no. 1 (January 1, 1992): C39—C49. http://dx.doi.org/10.1152/ajpcell.1992.262.1.c39.

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We determined the effects of okadaic acid (OA), a specific inhibitor of protein phosphatases 1 (PP1) and 2A (PP2A), on protein phosphorylation and on the activation of the NADPH oxidase in human neutrophils. In otherwise unstimulated cells, OA induced phosphoprotein accumulation, revealing the presence of constitutively active protein kinases. Pulse-chase experiments in electropermeabilized cells confirmed that this effect was due, at least in part, to inhibition of dephosphorylation. OA potentiated phosphoprotein accumulation induced by phorbol esters and by the chemotactic peptide N-formyl-m

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Kochinyan, Samvel, Luo Sun, Inca Ghosh, Tanya Barshevsky, Jie Xu, and Ming-Qun Xu. "Use of intein-mediated phosphoprotein arrays to study substrate specificity of protein phosphatases." BioTechniques 42, no. 1 (January 2007): 63–69. http://dx.doi.org/10.2144/000112311.

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Lyons, Scott P., Nicole P. Jenkins, Isha Nasa, Meng S. Choy, Mark E. Adamo, Rebecca Page, Wolfgang Peti, Greg B. Moorhead, and Arminja N. Kettenbach. "A Quantitative Chemical Proteomic Strategy for Profiling Phosphoprotein Phosphatases from Yeast to Humans." Molecular & Cellular Proteomics 17, no. 12 (September 18, 2018): 2448–61. http://dx.doi.org/10.1074/mcp.ra118.000822.

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Vickroy, Thomas W., Wendi L. Malphurs, and Marie L. Carriger. "Regulation of stimulus-dependent hippocampal acetylcholine release by okadaic acid-sensitive phosphoprotein phosphatases." Neuroscience Letters 191, no. 3 (May 1995): 200–204. http://dx.doi.org/10.1016/0304-3940(95)11576-i.

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Matta, Csaba, Ali Mobasheri, Pál Gergely, and Róza Zákány. "Ser/Thr-phosphoprotein phosphatases in chondrogenesis: neglected components of a two-player game." Cellular Signalling 26, no. 10 (October 2014): 2175–85. http://dx.doi.org/10.1016/j.cellsig.2014.06.013.

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Nasa, Isha, Lauren E. Cressey, Thomas Kruse, Emil P. T. Hertz, Jiang Gui, Lee M. Graves, Jakob Nilsson, and Arminja N. Kettenbach. "Quantitative kinase and phosphatase profiling reveal that CDK1 phosphorylates PP2Ac to promote mitotic entry." Science Signaling 13, no. 648 (September 8, 2020): eaba7823. http://dx.doi.org/10.1126/scisignal.aba7823.

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The reciprocal regulation of phosphoprotein phosphatases (PPPs) by protein kinases is essential to cell cycle progression and control, particularly during mitosis for which the role of kinases has been extensively studied. PPPs perform much of the serine/threonine dephosphorylation in eukaryotic cells and achieve substrate selectivity and specificity through the interaction of distinct regulatory subunits with conserved catalytic subunits in holoenzyme complexes. Using a mass spectrometry–based chemical proteomics approach to enrich, identify, and quantify endogenous PPP holoenzyme complexes c

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Nasa, Isha, and Arminja N. Kettenbach. "Effects of carboxyl-terminal methylation on holoenzyme function of the PP2A subfamily." Biochemical Society Transactions 48, no. 5 (October 14, 2020): 2015–27. http://dx.doi.org/10.1042/bst20200177.

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Phosphoprotein Phosphatases (PPPs) are enzymes highly conserved from yeast and human and catalyze the majority of the serine and threonine dephosphorylation in cells. To achieve substrate specificity and selectivity, PPPs form multimeric holoenzymes consisting of catalytic, structural/scaffolding, and regulatory subunits. For the Protein Phosphatase 2A (PP2A)-subfamily of PPPs, holoenzyme assembly is at least in part regulated by an unusual carboxyl-terminal methyl-esterification, commonly referred to as ‘methylation’. Carboxyl-terminal methylation is catalyzed by Leucine carboxyl methyltransf

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