Relevant bibliographies by topics / Phosphoprotein phosphatases

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'Phosphoprotein phosphatases'

Author: Grafiati
Published: 4 June 2021
Last updated: 30 July 2024

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Journal articles on the topic "Phosphoprotein phosphatases"

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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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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 L. Merr.), representing 3468 phosphoprotein groups, in which 2427 phosphoprotein groups were newly identified. These phosphoprotein groups contained 6326 unique high-probability phosphosites (UHPs), of which 77.2% were newly identified, increasing the current soybean phosphosite database size by 43.4%. Among the phosphopeptides found in this study, we determined 67 phosphopeptides (representing 63 phosphoprotein groups) from leaf tissue and 554 phosphopeptides (representing 487 phosphoprotein groups) from root tissue that showed significant changes in phosphorylation levels under sodium bicarbonate stress (fold change >1.2 or <0.83, respectively; p < 0.05). Localization prediction showed that most phosphoproteins localized in the nucleus for both leaf and root tissues. GO and KEGG enrichment analyses showed quite different enriched functional terms between leaf and root tissues, and more pathways were enriched in the root tissue than in the leaf tissue. Moreover, a total of 53 different protein kinases and 7 protein phosphatases were identified from the differentially expressed phosphoproteins (DEPs). A protein kinase/phosphatase interactor analysis showed that the interacting proteins were mainly involved in/with transporters/membrane trafficking, transcriptional level regulation, protein level regulation, signaling/stress response, and miscellaneous functions. The results presented in this study reveal insights into the function of post-translational modification in plant responses to sodium bicarbonate stress.
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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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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 homologue deleted on chromosome 10 (PTEN), Src homology 2-containing inositol 5′-phosphatase (SHIP), inositol polyphosphate 4-phosphatase type II (INPP4B), and protein phosphatase 2A (PP2A)—in different tissues with respect to regulation of cancer development. We will review the structures and functions of PTEN, SHIP, INPP4B, and PP2A phosphatases in suppressing cancer progression and their deregulation in cancer and highlight recent advances in our understanding of the PI3K/Akt signaling axis.
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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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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 that the serine/threonine specific enzymes are more ancient than the PTPs (protein tyrosine phosphatases). It is likely that the latter played a key role at the onset of metazoan evolution in conjunction with the tremendous expansion of tyrosine kinases and PTPs at this point. In the present review, we discuss the evolution of the PTPs, the serine/threonine specific PPP (phosphoprotein phosphatase) and PPM (metallo-dependent protein phosphatase) families and the more recently discovered phosphatases that utilize an aspartate-based catalytic mechanism. We will also highlight examples of convergent evolution and several phosphatases which are unique to plants.
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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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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 specificities to affect contraction and relaxation. Other members of the PP1 family that do not target myosin, as well as PP2A and PP2B, dephosphorylate a range of proteins that affect smooth muscle contraction. This review discusses the role of phosphatases in smooth muscle contractility with a focus on MYPT1 in uterine smooth muscle. Myometrium shares characteristics of vascular and other visceral smooth muscles yet, during healthy pregnancy, undergoes hypertrophy, hyperplasia, quiescence, and labor as physiological processes. Myometrium presents an accessible model for the study of normal and pathological smooth muscle function, and a better understanding of myometrial physiology may allow the development of novel therapeutics for the many disorders of myometrial physiology from preterm labor to dysmenorrhea.
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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 phosphorylation sites to control kinetochore function. Specificity is in part achieved by PPPs binding to short linear motifs (SLiMs) that guide their substrate specificity. SLiMs bind to conserved pockets on PPPs and are degenerate in nature, giving rise to a range of binding affinities. These SLiMs control the assembly of numerous substrate specifying complexes and their position and binding strength allow PPPs to target specific phosphorylation sites. In addition, the activity of PPPs is regulated by mitotic kinases and inhibitors, either directly at the activity level or through affecting PPP–SLiM interactions. Here, we discuss recent progress in understanding the regulation of PPP specificity and activity and how this controls kinetochore biology.
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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, present in the same liver extract, was not affected by cyanobacteria. Thus, experimental poisoning by hepatotoxic cyanobacteria resulted in an abnormally low ratio of phosphatase to lactate dehydrogenase activity in the liver extracts. These results indicate that specific inhibition of phosphatases 1 and 2A may provide a useful diagnostic tool to determine the early effects of cyanobacteria toxic peptides directly in liver samples from poisoned animals. Although this test was developed with rainbow trout, it should be possible to extend the analysis of liver phosphatase activity to other species, including sheep and cattle, which are frequently affected by hepatotoxic cyanobacteria.
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Dissertations / Theses on the topic "Phosphoprotein phosphatases"

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Tan, Yves S. H. "Regulation of the type 1 protein phosphatase in saccharomyces cerevisiae." free to MU campus, to others for purchase, 2001. http://wwwlib.umi.com/cr/mo/fullcit?p3013031.

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Wadham, Carol. "Protein Tyrosine Phosphatase Pez : its role in the regulation of cell-cell adhesions." Title page, abstract and table of contents only, 2003. http://web4.library.adelaide.edu.au/theses/09PH/09phw122.pdf.

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"March 2003" Bibliography: leaves 206-233. The experimental data presented in this thesis provide evidence that PTP-Pez is an active phosphatase that interacts with and dephosphorylates the adherens junction protein ℓ-catenin. PTP-Pez also associates with proteins that form part of the tight junction complex, the scaffolding protein ZO-1 and the transmembrane protein occludin.
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Wallis, Lise J., and n/a. "Regulation of Bub1b phosphorylation by protein phosphatase 2A." University of Otago. Dunedin School of Medicine, 2006. http://adt.otago.ac.nz./public/adt-NZDU20070502.114819.

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The mitotic spindle checkpoint plays a critical role during the cell cycle by protecting the faithful transmission of chromosomes during mitosis. If chromosomes are improperly bound to the spindle microtubules the checkpoint will prevent progress to anaphase by temporarily arresting cells in metaphase until all the chromosomes are correctly aligned. Bub1b is an essential component of the mitotic spindle checkpoint that transiently localises to kinetochores during mitosis and becomes phosphorylated, a response that is sustained during mitotic arrest. Bub1b has been implicated in other processes related to mitotic progression and is thought to regulate mitotic timing and have a role in caspase mediated cell death after prolonged mitotic arrest. The development of aneuploidy and cancer has been associated with mutations in the BUB1B gene and reduction in the level of Bub1b protein. To further our understanding of Bub1b function in the spindle checkpoint and mitosis, new protein interactions involving Bub1b were identified. This thesis describes the search for alternative proteins that interact with Bub1b, and their function in the mitotic spindle checkpoint and regulation of Bub1b activity. Using a yeast two-hybrid approach, members of the B56 family of regulatory subunits of serine-threonine protein phosphatase (PP2A) were identified as novel interacting partners of Bub1b. Substrate specificity of PP2A is determined by the regulatory subunits. There are five characterised isoforms of the B56 family, each encoded by separate genes. In addition, some isoforms have several recognised splice variants. Confirmation of interactions by alternative methods demonstrated that the isoforms B56γ and B56[epsilon] preferentially interact with phosphorylated Bub1b, whereas the interaction of the remaining B56 isoforms (α, β and [delta]) occurs at a lower affinity with no specificity for the phosphorylated form. It was further demonstrated that B56γ1 associated with phosphorylated Bub1b in vivo. Induced overexpression of splice variants of B56γ1 and B56γ2 demonstrated a significant reduction in levels of phosphorylated Bub1b during mitotic spindle checkpoint activation. In addition, an associated lower mitotic index was evident in cells with B56γ1 overexpression. Specific inhibition of PP2A activity with okadaic acid was shown to prolong Bub1b phosphorylation during normal mitosis and to restore the levels of phosphorylated Bub1b in arrested cells over expressing B56γ. These findings suggest a role for PP2A activity in regulation of Bub1b function that is mediated through substrate recognition by B56 regulatory subunits.
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Cheng, Lina. "Regulation of protein phosphatase 1, PP1 [gamma] 2, in testis/spermatozoa by PPP1R11, PPP1R7 and PPP1R2." [Kent, Ohio] : Kent State University, 2008. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=kent1208813693.

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Sheppard, Vonda Chantal. "Identification and characterization of diatom kinases catalyzing the phosphorylation of biomineral forming proteins." Diss., Georgia Institute of Technology, 2010. http://hdl.handle.net/1853/37227.

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Diatoms are unicellular photosynthetic algae that display intricately patterned cell walls made of amorphous silicon dioxide (silica). Long-chain polyamines and highly phosphorylated proteins, silaffins and silacidins, are believed to play an important role in biosilica formation. The phosphate moieties on silaffins and silacidins play a significant role in biomineral formation, yet no kinase has been identified that phosphorylates these biomineral forming proteins. This dissertation describes the characterization of a novel kinase from the diatom Thalassiosira pseudonana, tpSTK1, which is upregulated during silica formation. A recombinantly expressed histidine-tagged version of tpSTK1 was capable of phosphorylating recombinant silaffins but not recombinant silacidin in vitro. Through establishing methods for subcellular fraction of T. pseudonana membranes in combination with antibody inhibition assay, it was discovered that native tpSTK1 phosphorylates silaffins but not silacidins in vitro (i.e. it exhibits the same substrate specificity as recombinant tpSTK1). As tpSTK1 is an abundant protein in the ER lumen (~ 0.5 % of total ER protein) it seems highly likely to function as a silaffin kinase in vivo. TpSTK1 lacks clear sequence homologs in non-diatom organisms and is the first molecularly characterized kinase that appears to be involved in biomineralization. The predicted kinase domain (KD) of tpSTK2, the only T. pseudonana homolog of tpSTK1, was recombinantly expressed and tested for phosphorylation activity. Recombinant tpSTK2-KD and native tpSTK2 exhibited detectable activity with myelin basic protein, but did not phosphorylate silaffins or silacidins in vitro. Western blot analysis demonstrated that native tpSTK2 was not present in the ER, but associated with the cytosol and Golgi membrane containing subcellular fractions.
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Lee, Gui-in. "Structure and dynamics of the receptor kinase interacting FHA domain of kinase associated protein kinase from arabidopsis." Free to MU campus, others may purchase, 2003. http://wwwlib.umi.com/cr/mo/fullcit?p3100058.

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Saraf, Amit Strack Stefan. "Regulation of tyrosine hydroxylase by protein phosphatase 2A." [Iowa City, Iowa] : University of Iowa, 2008. http://ir.uiowa.edu/etd/429.

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Chakrabarti, Rumela. "Role for PP1 [gamma] 2 in spermatogenesis and sperm morphogenesis." [Kent, Ohio] : Kent State University, 2007. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=kent1176430377.

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Thesis (Ph.D.)--Kent State University, 2007.
Title from PDF t.p. (viewed Mar. 12, 2009). Advisor: Srinivasan Vijayaraghavan. Keywords: sperm, testes, spermatogenesis, protein phosphatase, knock out, spermatid. Includes bibliographical references (p. 115-129).
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Sayed, Saba Bilquis. "Studies of the role of phosphoprotein phosphatases in the adrenal cortex." Thesis, King's College London (University of London), 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.300432.

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Szapiel, Nicolas. "Glc7-E101Q is a novel tool for integrated genomic and proteomic analysis of PP1Glc7 phosphatase functional networks in Saccharomyces cerevisiae." Thesis, McGill University, 2007. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=101656.

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Reversible phosphorylation is a major mechanism for regulating the activity, localization and stability of proteins required for vital cellular processes such as glucose metabolism, gene expression, establishment of polarity, mitosis and cytokinesis. Phospho-regulation is driven by the activities of kinases and phosphatases. Together, these enzymes account for ∼3% of eukaryotic genomes and it is estimated that 30% of the eukaryotic proteome is composed of phospho-proteins. Protein kinases (PKs) have been studied extensively, however relatively little is known regarding the signaling networks of protein phosphatases (PPases). The identification of PPase functional networks has been slow due to the redundant nature of the majority of PPases, the complexity of their substrate recognition in vivo, and the lack of large-scale analyses that would facilitate network analysis. We hypothesized that large-scale analysis of genetic interactions using the Synthetic Genetic Array (SGA) and proteomic analyses using 2D-PAGE Difference Gel Electrophoresis (DiGE) could reveal PPase functional networks. Here, we apply this approach to the essential and conserved PP1 PPase Glc7 as it regulates numerous cellular processes in budding yeast. For this study, we created a glc7 hypomorphic mutant (glc7-E101Q) suited for both SGA and DiGE analyses. SGA analysis of glc7-E101Q revealed a broad network of 147 synthetic sick/lethal (SSL) and 178 synthetic rescue (SR) interactions. DiGE comparison of the glc7-E101Q proteome relative to wild-type at medium-resolution (∼1000 proteins) revealed alterations in 39 proteins that changed as a consequence of both the mutation and growth conditions. One of the proteins identified in this analysis was Eno1, a non-essential enolase that is mis-regulated in the presence of glucose and identified a SR mutation in the glc7-E101Q SGA. Subsequent phenotypic analysis suggests a novel, non-metabolic role for Eno1 in the Glc7 interaction network. Our results reveal that parallel analysis, using SGA and DIGE, can reveal novel functions and networks that a single analysis may not detect.
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Books on the topic "Phosphoprotein phosphatases"

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Goldstein, Barry J. Phosphoprotein phosphatases 1: tyrosine phosphatases. London: Academic Press, 1995.

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Goldstein, Barry J. Tyrosine phosphoprotein phosphatases. 2nd ed. Oxford: Oxford University Press, 1998.

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W, Ludlow John, ed. Protein phosphatase protocols. Totowa, N.J: Humana Press, 1998.

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Salvo, Joseph Di. Advances in protein phosphatases: Proceedings of the first international symposium, held at the Koninklijke Academie voor Geneeskunde van België August 20-23, 1985. Leuven, Belgium: Lueven University Press, 1985.

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International Conference on Second Messengers and Phosphoproteins (12th 2004 Montréal, Québec). Second messengers and phosphoprotein signaling: Proceedings of the 12th International Conference on Second Messengers and Phosphoproteins : Montreal, Canada, August 3-7, 2004. Edited by Anand-Srivastava Madhu B, Tremblay Michel, and Srivastava Ashok K. Bologna: Medimond International Proceedings, 2004.

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Millan, Jose Luis. Phosphatase modulators. New York: Humana Press, 2013.

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service), ScienceDirect (Online, ed. Mitochondrial function: Mitochondrial protein kinases, protein phosphatases and mitochondrial diseases. San Diego, Calif: Academic Press/Elsevier, 2009.

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G, Hardie D., ed. Protein phosphorylation: A practical approach. Oxford: Oxford University Press, 1993.

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NATO Advanced Study Institute on Cellular Regulation by Protein Phosphorylation (1990 La Londe les Maures, France). Cellular regulation by protein phosphorylation. Berlin: Springer-Verlag, 1991.

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(Editor), Joaquín Arino, and Denis R. Alexander (Editor), eds. Protein Phosphatases (Topics in Current Genetics). Springer, 2004.

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Book chapters on the topic "Phosphoprotein phosphatases"

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Ghahremani, Mina, and William C. Plaxton. "Phosphoprotein Phosphatase Function of Secreted Purple Acid Phosphatases." In Protein Phosphatases and Stress Management in Plants, 11–28. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-48733-1_2.

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Abe, S., L. C. Huang, and J. Larner. "Dephosphorylation of PDH by phosphoprotein phosphatases and its allosteric regulation by inositol glycans." In Alpha-Keto Acid Dehydrogenase Complexes, 187–95. Basel: Birkhäuser Basel, 1996. http://dx.doi.org/10.1007/978-3-0348-8981-0_14.

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Schomburg, Dietmar, and Margit Salzmann. "Phosphoprotein phosphatase." In Enzyme Handbook 3, 362–70. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76463-9_77.

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Schomburg, Dietmar, and Margit Salzmann. "Phosphoprotein phosphatase." In Enzyme Handbook 3, 371–76. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76463-9_78.

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Mohandas, D. V., and S. Dales. "In Vivo and In Vitro Models of Demyelinating Disease: A Phosphoprotein Phosphatase in Host Cell Endosomes Dephosphorylating the Nucleocapsid Protein of Coronavirus JHM." In Advances in Experimental Medicine and Biology, 255–60. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4684-5823-7_35.

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Goldstein, Barry J. "Protein-tyrosine phosphatases." In Tyrosine Phosphoprotein Phosphatases, 3–37. Oxford University PressOxford, 1998. http://dx.doi.org/10.1093/oso/9780198502470.003.0002.

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Abstract The first descriptions of PTPases in cell and tissue extracts provided evidence that they were distinct from other protein phosphatases because of their substrate specificity, neutral pH optimum, resistance to EDT A, and unique inhibition by low concentrations of zinc or vanadate [33]. Biochemical studies have since provided evidence that PTPases are found ubiquitously in cytosolic and particulate fractions of cells not only in mammals, but in diverse organisms including invertebrates and lower organisms such as yeast, viruses and bacteria.
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Goldstein, Barry J. "Biochemical studies of PTPase catalytic activity." In Tyrosine Phosphoprotein Phosphatases, 80–123. Oxford University PressOxford, 1998. http://dx.doi.org/10.1093/oso/9780198502470.003.0004.

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Abstract In attempts to gain insight into the nature of the PTPase catalytic reaction, as well as possible physiological substrates for the various PTPase homologues, a number of studies have utilized [32P]-labelled phosphorylated peptide and protein substrates for direct comparison of the activities of recombinant PTPase enzymes (Table 7). As expected, differences in kinetic parameters towards these substrates have been demonstrated, although this analysis has been hampered by the relatively low stoichiometry of the labelled substrate and the difficulty in evaluating true initial rates of dephosphorylation and relative substrate affinities [245, 540]. These types of studies have also been helpful in mapping the residues involved in the catalytic reaction, and to distinguish between differences in the potential enzyme activity of the two domains of the tandem-domain transmembrane PTPases.
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Goldstein, Barry J. "Interactions of PTPases with other proteins, peptides and macromolecules." In Tyrosine Phosphoprotein Phosphatases, 140–55. Oxford University PressOxford, 1998. http://dx.doi.org/10.1093/oso/9780198502470.003.0007.

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Abstract Some of the most exciting work in cell signalling has been in the characterization of protein-protein intermolecular reactions. PTPases have been shown to be involved in a variety of interactions that hold promise in identifying associated cellular proteins, potential substrate targets and eventually to help elucidate the physiological roles of the various PTPase homologues (Table 12). The initial sequence characterization of several transmembrane PTPases revealed structural similarity in the extracellular domains to the NCAM family of cell adhesion molecules and to repeats of fibronectin type III (Fn-III) motifs [756, 891] suggesting that these domains might be regulated by homotypic cell-cell interactions [605, 901]. This hypothesis has been demonstrated to be true at least in the case of two of the receptor-type PTPases, RPTP-µ and RPTP-K;, where recombinant domains on inert spheres as well as in the surface of overexpressing eukaryotic cells have been shown to engage in homotypic aggregation [412, 421, 447, 1089].
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Goldstein, Barry J. "Introduction." In Tyrosine Phosphoprotein Phosphatases, 1–2. Oxford University PressOxford, 1998. http://dx.doi.org/10.1093/oso/9780198502470.003.0001.

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Abstract Covalent modification of proteins by phosphorylation and déphosphorylation has long been appreciated to be an essential physiological mechanism for the control of cellular function. The extensive molecular and biochemical characterisation of tyrosine kinases that has taken place through the 1980s has now been followed by studies on a rapidly emerging super - family of complementary enzymes, the protein-tyrosine phosphatases (P TP ases; EC 3.1.4.38), which reverse the effect of the kinases and serve to dephosphorylate protein-tyrosine residues of cellular substrate proteins [16, 26]. Work on reversible protein phosphorylation was highlighted by the awarding of the 1992 Nobel Prize in Physiology or Medicine to Drs Edmond Fischer and Edwin Krebs for their fundamental contributions in this area. Although the phosphorylation of protein-tyrosine residues represents only a small fraction of the overall modification of cellular proteins by phosphorylation, which occurs primarily on serine and threonine residues, this reversible protein alteration has been demonstrated to be involved in many critical aspects of cellular physiology. Reversible tyrosine phosphorylation mediates the regulation of cell growth, cell division and differentiation as well as responses to tyrosine kinases that are expressed in cells as plasma membrane receptors or as non-receptor tyrosine kinases. PTPases have been considered to balance the steady-state phosphorylation of a variety of cellular tyrosine kinase substrates and influence cellular signal transduction by attenuating the activity of activated (autophosphorylated) tyrosine receptor kinases or by participating in an on–off switching mechanism mediated by reversible tyrosine phosphorylation of substrate proteins involved in downstream signalling.
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Goldstein, Barry J. "Covalent modification of PTPases." In Tyrosine Phosphoprotein Phosphatases, 124–38. Oxford University PressOxford, 1998. http://dx.doi.org/10.1093/oso/9780198502470.003.0005.

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Abstract The large, transmembrane PTPases have been shown in several cases to undergo proteolytic processing of a proprotein that produces protein subunits, including LAR, RPTP-k and RPTP-σ. The site and determinants of LAR proprotein cleavage have recently been evaluated [105, 110, 116]. LAR is synthesized initially as a ∼200 kDa proprotein that is processed into a complex of two non-covalently associated subunits. The E-subunit (150 kDa) contains the cell adhesion molecule domains, the P-subunit (85 kDa) contains a short segment of extracellular region and the transmembrane and cytoplasmic domains. Cleavage occurs at a pentabasic (RRRRR) motif at residues 1148-1152, and is catalysed by a subtilisinlike endogenous enzyme. The unprocessed enzyme can also be detected at the cell surface. Studies in transfected HeLa cells have shown that the E-subunit is shed during cell growth; whether this is a mechanism for regulating PTPase function remains to be determined [110].
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Conference papers on the topic "Phosphoprotein phosphatases"

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Enouf, J., R. Bredoux, A. Giraud, N. Bourdeau, and S. Levy-Toledano. "POSSIBLE RELATIONSHIP BETWEEN THE 23-kDa PHOSPHOPROTEIN AND THE IP3 -INDUCED Ca2+RELEASE IN HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644516.

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Abstract:
The regulation of Ca2+ concentration in human platelets involves intracellular membranes i.e. dense tubular system (DTS). Agonist-induced platelet activation generates inositol 1,4,5 trisphosphate (IP3) which is responsible for Ca2+ mobilization from DTS. However, its mechanism of action is still unknown. cAMP has been shown to regulate Ca2+ transport by isolated membrane vesicles. This effect was correlated with the phosphorylation of a 23 kDa protein. We investigated whether this phosphorylation could play a role in the mechanism of IP3-induced Ca release.We isolated a membrane fraction enriched in intracellular membranes, which actively sequesters Ca2++. The Ca2+ uptake was mediated by a characterized (Ca2+ + Mg2+)-ATPase of a molecular weight 120 kDa. As well, the characterization of the 23-kDa protein phosphorylation by the catalytic subunit of the cAMP dependent protein kinase (C. Sub.) has been achieved. IP^-induced Ca release was tested on our membrane preparations. The transient effect was maximal at one minute and a dose-response curve was obtained.The cAMP dependent phosphorylation of the 23-kDa protein increased the Ca2+ liberation induced by IP by two fold whatever the IP3 concentration. The addition on the protein kinase inhibitor inhibited the IP3 -induced Ca2+ release.The effect of IP3 on the cAMP-mediated phosphorylation of the 23-kDa protein has been examinated.A dose dependent stimu-ulation of the 23-kDa protein phosphorylation in the presence of C. Sub. was initiated by IP3. The maximal effect was observed after 1-2 min and obtained with an IP3 concentration similar to that producing the maximal calcium release. The stimulation of the phosphorylation by IP3 was detected in the absence of Ca2+ and in the presence of phosphatase inhibitors.Therefore, we suggest a possible correlation between cAMP dependent phosphorylation of the 23-kDa protein and the IP3-induced Ca2+ release in human platelet membrane vesicles.
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