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Journal articles on the topic 'Phosphatidylinositol 3-Kinases'

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Published: 4 June 2021

Last updated: 8 June 2024

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1

Abraham, Robert T. "Phosphatidylinositol 3-kinase related kinases." Current Opinion in Immunology 8, no. 3 (1996): 412–18. http://dx.doi.org/10.1016/s0952-7915(96)80132-4.

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2

Suzuki, Takahiro, Osamu Hazeki, and Michio Ui. "Phosphatidylinositol 3-Kinases." membrane 21, no. 3 (1996): 158–64. http://dx.doi.org/10.5360/membrane.21.158.

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3

Muftuoglu, Yagmur, Yi Xue, Xiang Gao, Dianqing Wu, and Ya Ha. "Mechanism of substrate specificity of phosphatidylinositol phosphate kinases." Proceedings of the National Academy of Sciences 113, no. 31 (2016): 8711–16. http://dx.doi.org/10.1073/pnas.1522112113.

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The phosphatidylinositol phosphate kinase (PIPK) family of enzymes is primarily responsible for converting singly phosphorylated phosphatidylinositol derivatives to phosphatidylinositol bisphosphates. As such, these kinases are central to many signaling and membrane trafficking processes in the eukaryotic cell. The three types of phosphatidylinositol phosphate kinases are homologous in sequence but differ in catalytic activities and biological functions. Type I and type II kinases generate phosphatidylinositol 4,5-bisphosphate from phosphatidylinositol 4-phosphate and phosphatidylinositol 5-ph

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4

Rane, M. J., S. L. Carrithers, J. M. Arthur, J. B. Klein, and K. R. McLeish. "Formyl peptide receptors are coupled to multiple mitogen-activated protein kinase cascades by distinct signal transduction pathways: role in activation of reduced nicotinamide adenine dinucleotide oxidase." Journal of Immunology 159, no. 10 (1997): 5070–78. http://dx.doi.org/10.4049/jimmunol.159.10.5070.

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Abstract Formyl peptide receptor activation of three mitogen-activated protein kinase (MAPK) cascades, extracellular signal-regulated kinases (ERKs), N-terminal kinases (JNKs), and p38 MAPK was examined in differentiated HL-60 granulocytes. FMLP stimulated a concentration- and time-dependent increase in ERK, JNK, and p38 MAPK activities, all of which were dependent on a pertussis toxin-sensitive G protein. Pharmacologic inhibitors were used to examine the roles of tyrosine kinases, phosphatidylinositol 3-kinase, protein kinase C, and phospholipase C. FMLP-stimulated ERK activity was dependent

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5

Roymans, Dirk, and Herman Slegers. "Phosphatidylinositol 3-kinases in tumor progression." European Journal of Biochemistry 268, no. 3 (2001): 487–98. http://dx.doi.org/10.1046/j.1432-1327.2001.01936.x.

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6

Imseng, Stefan, Christopher HS Aylett, and Timm Maier. "Architecture and activation of phosphatidylinositol 3-kinase related kinases." Current Opinion in Structural Biology 49 (April 2018): 177–89. http://dx.doi.org/10.1016/j.sbi.2018.03.010.

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7

Shibasaki, F., Y. Fukui, and T. Takenawa. "Different properties of monomer and heterodimer forms of phosphatidylinositol 3-kinases." Biochemical Journal 289, no. 1 (1993): 227–31. http://dx.doi.org/10.1042/bj2890227.

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Phosphatidylinositol (PI) 3-kinase plays an important role in the signalling of cell growth. We previously purified two types of PI 3-kinase from bovine thymus, a monomer from (PI 3-kinase I) and a heterodimer form (PI 3-kinase II) [Shibasaki, Homma and Takenawa (1991) J. Biol. Chem. 266, 8108-8114]. Here we examine the properties of these purified PI 3-kinases. Both PI 3-kinases were inhibited strongly by quercetin and isoquercetin. The inhibition of PI 3-kinase I and PI 3-kinase II by quercetin appears to be non-competitive, with apparent Ki values of 4 microM and 2.5 microM respectively. PI

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8

Yamboliev, Ilia A., Kevin M. Wiesmann, Cherie A. Singer, Jason C. Hedges, and William T. Gerthoffer. "Phosphatidylinositol 3-kinases regulate ERK and p38 MAP kinases in canine colonic smooth muscle." American Journal of Physiology-Cell Physiology 279, no. 2 (2000): C352—C360. http://dx.doi.org/10.1152/ajpcell.2000.279.2.c352.

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In canine colon, M2/M3 muscarinic receptors are coupled to extracellular signal-regulated kinase (ERK) and p38 mitogen-activated protein (MAP) kinases. We tested the hypothesis that this coupling is mediated by enzymes of the phosphatidylinositol (PI) 3-kinase family. RT-PCR and Western blotting demonstrated expression of two isoforms, PI 3-kinase-α and PI 3-kinase-γ. Muscarinic stimulation of intact muscle strips (10 μM ACh) activated PI 3-kinase-γ, ERK and p38 MAP kinases, and MAP kinase-activated protein kinase-2, whereas PI 3-kinase-α activation was not detected. Wortmannin (25 μM) abolish

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9

Choi, Suyong, Xander Houdek, and Richard A. Anderson. "Phosphoinositide 3-kinase pathways and autophagy require phosphatidylinositol phosphate kinases." Advances in Biological Regulation 68 (May 2018): 31–38. http://dx.doi.org/10.1016/j.jbior.2018.02.003.

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10

Christoforidis, Savvas, Marta Miaczynska, Keith Ashman, et al. "Phosphatidylinositol-3-OH kinases are Rab5 effectors." Nature Cell Biology 1, no. 4 (1999): 249–52. http://dx.doi.org/10.1038/12075.

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11

Takegawa, K., D. B. DeWald, and S. D. Emr. "Schizosaccharomyces pombe Vps34p, a phosphatidylinositol-specific PI 3-kinase essential for normal cell growth and vacuole morphology." Journal of Cell Science 108, no. 12 (1995): 3745–56. http://dx.doi.org/10.1242/jcs.108.12.3745.

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We have cloned the gene, vps34+, from the fission yeast Schizosaccharomyces pombe which encodes an 801 amino acid protein with phosphatidylinositol 3-kinase activity. The S. pombe Vps34 protein shares 43% amino acid sequence identity with the Saccharomyces cerevisiae Vps34 protein and 28% identity with the p110 catalytic subunit of the mammalian phosphatidylinositol 3-kinase. When the vps34+ gene is disrupted, S.pombe strains are temperature-sensitive for growth and the mutant cells contain enlarged vacuoles. Furthermore, while wild-type strains exhibit substantial levels of phosphatidylinosit

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12

Min, Sang H., and Charles S. Abrams. "Why do phosphatidylinositol kinases have so many isoforms?" Biochemical Journal 423, no. 1 (2009): e5-e8. http://dx.doi.org/10.1042/bj20091274.

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Macromolecules can be transported into the cells by endocytosis, either by phagocytosis or by pinocytosis. Typically, phagocytosis involves the uptake of solid large particles mediated by cell-surface receptors, whereas pinocytosis takes up fluid and solutes. The synthesis of PtdIns(4,5)P2 and PtdIns(3,4,5)P3 plays fundamental roles in all forms of endocytosis. Curiously, almost all eukaryotic cells have multiple isoforms of the kinases that synthesize these critical phosphatidylinositols. In this issue of the Biochemical Journal, Namiko Tamura, Osamu Hazeki and co-workers report that the subu

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13

Vieira, Otilia V., Roberto J. Botelho, Lucia Rameh, et al. "Distinct roles of class I and class III phosphatidylinositol 3-kinases in phagosome formation and maturation." Journal of Cell Biology 155, no. 1 (2001): 19–26. http://dx.doi.org/10.1083/jcb.200107069.

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Phagosomes acquire their microbicidal properties by fusion with lysosomes. Products of phosphatidylinositol 3-kinase (PI 3-kinase) are required for phagosome formation, but their role in maturation is unknown. Using chimeric fluorescent proteins encoding tandem FYVE domains, we found that phosphatidylinositol 3-phosphate (PI[3]P) accumulates greatly but transiently on the phagosomal membrane. Unlike the 3′-phosphoinositides generated by class I PI 3-kinases which are evident in the nascent phagosomal cup, PI(3)P is only detectable after the phagosome has sealed. The class III PI 3-kinase VPS34

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14

Mitra, Prasenjit, Yingjie Zhang, Lucia E. Rameh, et al. "A novel phosphatidylinositol(3,4,5)P3 pathway in fission yeast." Journal of Cell Biology 166, no. 2 (2004): 205–11. http://dx.doi.org/10.1083/jcb.200404150.

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The mammalian tumor suppressor, phosphatase and tensin homologue deleted on chromosome 10 (PTEN), inhibits cell growth and survival by dephosphorylating phosphatidylinositol-(3,4,5)-trisphosphate (PI[3,4,5]P3). We have found a homologue of PTEN in the fission yeast, Schizosaccharomyces pombe (ptn1). This was an unexpected finding because yeast (S. pombe and Saccharomyces cerevisiae) lack the class I phosphoinositide 3-kinases that generate PI(3,4,5)P3 in higher eukaryotes. Indeed, PI(3,4,5)P3 has not been detected in yeast. Surprisingly, upon deletion of ptn1 in S. pombe, PI(3,4,5)P3 became de

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15

Tichý, Aleš, Kamila Ďurišová, Eva Novotná, et al. "PHOSPHATIDYLINOSITOL-3-KINASE RELATED KINASES (PIKKS) IN RADIATION-INDUCED DNA DAMAGE." Military Medical Science Letters 81, no. 4 (2012): 177–87. http://dx.doi.org/10.31482/mmsl.2012.025.

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16

Gutkind, J. S., P. M. Lacal, and K. C. Robbins. "Thrombin-dependent association of phosphatidylinositol-3 kinase with p60c-src and p59fyn in human platelets." Molecular and Cellular Biology 10, no. 7 (1990): 3806–9. http://dx.doi.org/10.1128/mcb.10.7.3806-3809.1990.

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Recent studies have shown that ligand-activated growth factor receptors as well as transforming versions of nonreceptor protein-tyrosine kinases physically associate with phosphatidylinositol-3 kinase (PI-3 kinase). Reasoning that PI-3 kinase might also play a role in the normal functions of nonreceptor kinases, we sought to determine whether association with PI-3 kinase might serve as a measure of nonreceptor protein-tyrosine kinase activation under physiological conditions. We found that p60c-src as well as p59fyn, the product of another member of the src family of proto-oncogenes, physicall

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17

Gutkind, J. S., P. M. Lacal, and K. C. Robbins. "Thrombin-dependent association of phosphatidylinositol-3 kinase with p60c-src and p59fyn in human platelets." Molecular and Cellular Biology 10, no. 7 (1990): 3806–9. http://dx.doi.org/10.1128/mcb.10.7.3806.

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Recent studies have shown that ligand-activated growth factor receptors as well as transforming versions of nonreceptor protein-tyrosine kinases physically associate with phosphatidylinositol-3 kinase (PI-3 kinase). Reasoning that PI-3 kinase might also play a role in the normal functions of nonreceptor kinases, we sought to determine whether association with PI-3 kinase might serve as a measure of nonreceptor protein-tyrosine kinase activation under physiological conditions. We found that p60c-src as well as p59fyn, the product of another member of the src family of proto-oncogenes, physicall

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18

Takeda, Kosuke, Atsuo T. Sasaki, Hyunjung Ha, Hyun-A. Seung, and Richard A. Firtel. "Role of Phosphatidylinositol 3-Kinases in Chemotaxis inDictyostelium." Journal of Biological Chemistry 282, no. 16 (2007): 11874–84. http://dx.doi.org/10.1074/jbc.m610984200.

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19

McNulty, Shannon, William Bornmann, Jill Schriewer, et al. "Multiple Phosphatidylinositol 3-Kinases Regulate Vaccinia Virus Morphogenesis." PLoS ONE 5, no. 5 (2010): e10884. http://dx.doi.org/10.1371/journal.pone.0010884.

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20

Li, Z., M. I. Wahl, A. Eguinoa, L. R. Stephens, P. T. Hawkins, and O. N. Witte. "Phosphatidylinositol 3-kinase- activates Bruton's tyrosine kinase in concert with Src family kinases." Proceedings of the National Academy of Sciences 94, no. 25 (1997): 13820–25. http://dx.doi.org/10.1073/pnas.94.25.13820.

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21

Gillooly, David J., Anne Simonsen, and Harald Stenmark. "Phosphoinositides and phagocytosis." Journal of Cell Biology 155, no. 1 (2001): 15–18. http://dx.doi.org/10.1083/jcb.200109001.

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Phosphoinositide 3 kinases (PI3Ks)**Abbreviation used in this paper: PI3K, phosphoinositide 3 kinase. are known as regulators of phagocytosis. Recent results demonstrate that class I and III PI3Ks act consecutively in phagosome formation and maturation, and that their respective products, phosphatidylinositol 3,4,5-trisphosphate (PI[3,4,5]P3) and phosphatidylinositol 3-phosphate (PI[3]P), accumulate transiently at different stages. Phagosomes containing Mycobacterium tuberculosis do not acquire the PI(3)P-binding protein EEA1, which is required for phagosome maturation. This suggests a possibl

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22

NAKAGAWA, Tamotsu, Kaoru GOTO, and Hisatake KONDO. "Cloning and characterization of a 92 kDa soluble phosphatidylinositol 4-kinase." Biochemical Journal 320, no. 2 (1996): 643–49. http://dx.doi.org/10.1042/bj3200643.

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A phosphatidylinositol (PtdIns) 4-kinase cDNA cloned from a rat brain cDNA library encoded a protein of 816 amino acids with a calculated molecular mass of 91654 Da. This molecule contained a lipid-kinase-unique domain and a presumed lipid/protein kinase homology domain that are found in other PtdIns 4-kinases and PtdIns 3-kinases. Furthermore, this kinase molecule had 43.3% shared identity with the presumed catalytic domain of yeast PtdIns 4-kinase, PtdInsK1, and the two molecules had a region of similarity that is not conserved in other lipid kinases. By examining PtdIns kinase activity in t

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23

Shin, Hye-Won, Mitsuko Hayashi, Savvas Christoforidis, et al. "An enzymatic cascade of Rab5 effectors regulates phosphoinositide turnover in the endocytic pathway." Journal of Cell Biology 170, no. 4 (2005): 607–18. http://dx.doi.org/10.1083/jcb.200505128.

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Generation and turnover of phosphoinositides (PIs) must be coordinated in a spatial- and temporal-restricted manner. The small GTPase Rab5 interacts with two PI 3-kinases, Vps34 and PI3Kβ, suggesting that it regulates the production of 3-PIs at various stages of the early endocytic pathway. Here, we discovered that Rab5 also interacts directly with PI 5- and PI 4-phosphatases and stimulates their activity. Rab5 regulates the production of phosphatidylinositol 3-phosphate (PtdIns[3]P) through a dual mechanism, by directly phosphorylating phosphatidylinositol via Vps34 and by a hierarchical enzy

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Thi, E. P., and N. E. Reiner. "Phosphatidylinositol 3-kinases and their roles in phagosome maturation." Journal of Leukocyte Biology 92, no. 3 (2012): 553–66. http://dx.doi.org/10.1189/jlb.0212053.

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25

Todorov, Alex G., Marcelo Einicker-Lamas, Solange L. de Castro, Mecia M. Oliveira, and Adilson Guilherme. "Activation of Host Cell Phosphatidylinositol 3-Kinases byTrypanosoma cruziInfection." Journal of Biological Chemistry 275, no. 41 (2000): 32182–86. http://dx.doi.org/10.1074/jbc.m909440199.

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26

Zhou, Q. L., J. G. Park, Z. Y. Jiang, et al. "Analysis of insulin signalling by RNAi-based gene silencing." Biochemical Society Transactions 32, no. 5 (2004): 817–21. http://dx.doi.org/10.1042/bst0320817.

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Using siRNA-mediated gene silencing in cultured adipocytes, we have dissected the insulin-signalling pathway leading to translocation of GLUT4 glucose transporters to the plasma membrane. RNAi (RNA interference)-based depletion of components in the putative TC10 pathway (CAP, CrkII and c-Cbl plus Cbl-b) or the phospholipase Cγ pathway failed to diminish insulin signalling to GLUT4. Within the phosphoinositide 3-kinase pathway, loss of the 5′-phosphatidylinositol 3,4,5-trisphosphate phosphatase SHIP2 was also without effect, whereas depletion of the 3′-phosphatase PTEN significantly enhanced in

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27

Jeschke, Andreas, Nicole Zehethofer, Buko Lindner, et al. "Phosphatidylinositol 4-phosphate and phosphatidylinositol 3-phosphate regulate phagolysosome biogenesis." Proceedings of the National Academy of Sciences 112, no. 15 (2015): 4636–41. http://dx.doi.org/10.1073/pnas.1423456112.

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Professional phagocytic cells ingest microbial intruders by engulfing them into phagosomes, which subsequently mature into microbicidal phagolysosomes. Phagosome maturation requires sequential fusion of the phagosome with early endosomes, late endosomes, and lysosomes. Although various phosphoinositides (PIPs) have been detected on phagosomes, it remained unclear which PIPs actually govern phagosome maturation. Here, we analyzed the involvement of PIPs in fusion of phagosomes with various endocytic compartments and identified phosphatidylinositol 4-phosphate [PI(4)P], phosphatidylinositol 3-ph

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28

Yamboliev, Ilia A., Jennifer Chen, and William T. Gerthoffer. "PI 3-kinases and Src kinases regulate spreading and migration of cultured VSMCs." American Journal of Physiology-Cell Physiology 281, no. 2 (2001): C709—C718. http://dx.doi.org/10.1152/ajpcell.2001.281.2.c709.

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Pulmonary artery smooth muscle cell (PASMC) adhesion, spreading, and migration depend on matrix-stimulated reorganization of focal adhesions. Platelet-derived growth factor (PDGF) activates intracellular signal transduction cascades that also regulate adhesion, spreading, and migration, but the signaling molecules involved in these events are poorly defined. We hypothesized that phosphatidylinositol (PI) 3-kinases and Src tyrosine kinases translate matrix and PDGF-initiated signals into cell motility. In experiments with cultured canine PASMCs, inhibition of PI 3-kinases with wortmannin (0.3 μ

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29

Graziani, A., L. E. Ling, G. Endemann, C. L. Carpenter, and L. C. Cantley. "Purification and characterization of human erythrocyte phosphatidylinositol 4-kinase. Phosphatidylinositol 4-kinase and phosphatidylinositol 3-monophosphate 4-kinase are distinct enzymes." Biochemical Journal 284, no. 1 (1992): 39–45. http://dx.doi.org/10.1042/bj2840039.

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PtdIns 4-kinase has been purified 83,000-fold from human erythrocyte membranes. The major protein detected by SDS/PAGE is of molecular mass 56 kDa, and enzymic activity can be renatured from this band of the gel. The characteristics of this enzyme are similar to other type II PtdIns kinases previously described: PtdIns presented in Triton X-100 micelles is preferred as a substrate over PtdIns vesicles, the enzyme possesses a relatively low Km for ATP (20 microM), and adenosine is an effective inhibitor. A monoclonal antibody raised against bovine brain type II PtdIns 4-kinase is an effective i

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30

Liu, X., L. E. Marengere, C. A. Koch, and T. Pawson. "The v-Src SH3 domain binds phosphatidylinositol 3'-kinase." Molecular and Cellular Biology 13, no. 9 (1993): 5225–32. http://dx.doi.org/10.1128/mcb.13.9.5225-5232.1993.

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Fibroblasts transformed by v-src or by related oncogenes encoding activated tyrosine kinases contain elevated levels of polyphosphoinositides with phosphate at the D-3 position of the inositol ring, as a result of the activation of phosphatidylinositol (PI) 3'-kinase. v-src-transformed cells also contain increased levels of PI 3'-kinase activity immunoprecipitable with anti-phosphotyrosine antibodies; furthermore, PI 3'-kinase can be detected in association with the v-Src tyrosine kinase. To identify regions of v-Src that can interact with PI 3'-kinase, the v-Src SH2 and SH3 domains were expre

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Liu, X., L. E. Marengere, C. A. Koch, and T. Pawson. "The v-Src SH3 domain binds phosphatidylinositol 3'-kinase." Molecular and Cellular Biology 13, no. 9 (1993): 5225–32. http://dx.doi.org/10.1128/mcb.13.9.5225.

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Fibroblasts transformed by v-src or by related oncogenes encoding activated tyrosine kinases contain elevated levels of polyphosphoinositides with phosphate at the D-3 position of the inositol ring, as a result of the activation of phosphatidylinositol (PI) 3'-kinase. v-src-transformed cells also contain increased levels of PI 3'-kinase activity immunoprecipitable with anti-phosphotyrosine antibodies; furthermore, PI 3'-kinase can be detected in association with the v-Src tyrosine kinase. To identify regions of v-Src that can interact with PI 3'-kinase, the v-Src SH2 and SH3 domains were expre

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SCHNYDER, Bruno, Paul C. MEUNIER, and Bruce D. CAR. "Inhibition of kinases impairs neutrophil activation and killing of Staphylococcus aureus." Biochemical Journal 331, no. 2 (1998): 489–95. http://dx.doi.org/10.1042/bj3310489.

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Intracellular phosphorylations polymorphonuclear neutrophils are mediated by kinases, including mitogen activated-protein (MAP) kinases and phosphatidylinositol 3-kinase. In the present study we demonstrate their effector functions upon both ligation of cell-surface seven-transmembrane-spanning receptors by bacterial peptide formylmethionyl-leucylphenylalanine as well as in the process of destruction of Staphylococcus aureus. To regulate neutrophil MAP kinases p38 and p44/42, specifically, we made use of their specific inhibitors 10 µM SK&F 86002 (for p38) and PD 098059 (for activating kin

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33

Velnati, Suresh, Sara Centonze, Federico Girivetto, et al. "Identification of Key Phospholipids That Bind and Activate Atypical PKCs." Biomedicines 9, no. 1 (2021): 45. http://dx.doi.org/10.3390/biomedicines9010045.

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PKCζ and PKCι/λ form the atypical protein kinase C subgroup, characterised by a lack of regulation by calcium and the neutral lipid diacylglycerol. To better understand the regulation of these kinases, we systematically explored their interactions with various purified phospholipids using the lipid overlay assays, followed by kinase activity assays to evaluate the lipid effects on their enzymatic activity. We observed that both PKCζ and PKCι interact with phosphatidic acid and phosphatidylserine. Conversely, PKCι is unique in binding also to phosphatidylinositol-monophosphates (e.g., phosphati

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Lingaraj, Trupti, John Donovan, Zhi Li, et al. "A High-Throughput Liposome Substrate Assay with Automated Lipid Extraction Process for PI 3-Kinase." Journal of Biomolecular Screening 13, no. 9 (2008): 906–11. http://dx.doi.org/10.1177/1087057108324498.

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The signaling pathways involving lipid kinase class I phosphatidylinositol 3-kinases (PI 3-kinases) regulate cell growth, proliferation, and survival. Class I PI 3-kinases catalyze the conversion of PI (4,5)P2 to PI (3,4,5)P3, which acts as a lipid second messenger to activate mitogenic signaling cascades. Recently, p110α, a class IA PI 3-kinase, was found to be mutated frequently in many human cancers. Therefore, it is increasingly studied as an anticancer drug target. Traditionally, PI 3-kinase activities have been studied using liposome substrates. This method, however, is hampered signific

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KRISTIANSEN, S⊘ren, Toolsie RAMLAL, and Amira KLIP. "Phosphatidylinositol 4-kinase, but not phosphatidylinositol 3-kinase, is present in GLUT4-containing vesicles isolated from rat skeletal muscle." Biochemical Journal 335, no. 2 (1998): 351–56. http://dx.doi.org/10.1042/bj3350351.

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Insulin stimulates the rate of glucose transport into muscle and adipose cells by translocation of glucose transporter (GLUT4)-containing vesicles from an intracellular storage pool to the surface membrane. This event is mediated through the insulin receptor substrates (IRSs), which in turn activate phosphatidylinositol (PI) 3-kinase isoforms. It has been suggested that insulin causes attachment of PI 3-kinases to the intracellular GLUT4-containing vesicles in rat adipose cells. Furthermore, it has also been shown that GLUT4-containing vesicles in adipose cells contain a PI 4-kinase. In the pr

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Sugimoto, Katsunori. "Branching the Tel2 pathway for exact fit on phosphatidylinositol 3-kinase-related kinases." Current Genetics 64, no. 5 (2018): 965–70. http://dx.doi.org/10.1007/s00294-018-0817-9.

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Bony, Claire, Serge Roche, Ueno Shuichi та ін. "A Specific Role of Phosphatidylinositol 3–Kinase γ". Journal of Cell Biology 152, № 4 (2001): 717–28. http://dx.doi.org/10.1083/jcb.152.4.717.

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Purinergic stimulation of cardiomyocytes turns on a Src family tyrosine kinase–dependent pathway that stimulates PLCγ and generates IP3, a breakdown product of phosphatidylinositol 4,5–bisphosphate (PIP2). This signaling pathway closely regulates cardiac cell autonomic activity (i.e., spontaneous cell Ca2+ spiking). PIP2 is phosphorylated on 3′ by phosphoinositide 3–kinases (PI3Ks) that belong to a broad family of kinase isoforms. The product of PI3K, phosphatidylinositol 3,4,5–trisphosphate, regulates activity of PLCγ. PI3Ks have emerged as crucial regulators of many cell functions including

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Endemann, G. C., A. Graziani, and L. C. Cantley. "A monoclonal antibody distinguishes two types of phosphatidylinositol 4-kinase." Biochemical Journal 273, no. 1 (1991): 63–66. http://dx.doi.org/10.1042/bj2730063.

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A monoclonal antibody has been developed against the type II PtdIns 4-kinase from bovine brain. This antibody, 4C5G, causes greater than 90% inhibition of the type II PtdIns 4-kinase from bovine brain, rat brain and human erythrocytes. However, it fails to inhibit type III PtdIns 4-kinase from bovine brain or PtdIns 3-kinase from rat liver. These results suggest that type II and type III PtdIns 4-kinases are distinct gene products, and that 4C5G will be useful in studying the function of the type II PtdIns 4-kinase.

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Yoshioka, Kazuaki. "Class II phosphatidylinositol 3-kinase isoforms in vesicular trafficking." Biochemical Society Transactions 49, no. 2 (2021): 893–901. http://dx.doi.org/10.1042/bst20200835.

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Phosphatidylinositol 3-kinases (PI3Ks) are critical regulators of many cellular processes including cell survival, proliferation, migration, cytoskeletal reorganization, and intracellular vesicular trafficking. They are a family of lipid kinases that phosphorylate membrane phosphoinositide lipids at the 3′ position of their inositol rings, and in mammals they are divided into three classes. The role of the class III PI3K Vps34 is well-established, but recent evidence suggests the physiological significance of class II PI3K isoforms in vesicular trafficking. This review focuses on the recently

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Boronenkov, Igor V., Joost C. Loijens, Masato Umeda, and Richard A. Anderson. "Phosphoinositide Signaling Pathways in Nuclei Are Associated with Nuclear Speckles Containing Pre-mRNA Processing Factors." Molecular Biology of the Cell 9, no. 12 (1998): 3547–60. http://dx.doi.org/10.1091/mbc.9.12.3547.

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Phosphoinositide signal transduction pathways in nuclei use enzymes that are indistinguishable from their cytosolic analogues. We demonstrate that distinct phosphatidylinositol phosphate kinases (PIPKs), the type I and type II isoforms, are concentrated in nuclei of mammalian cells. The cytosolic and nuclear PIPKs display comparable activities toward the substrates phosphatidylinositol 4-phosphate and phosphatidylinositol 3-phosphate. Indirect immunofluorescence revealed that these kinases were associated with distinct subnuclear domains, identified as “nuclear speckles,” which also contained

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King, W. G., M. D. Mattaliano, T. O. Chan, P. N. Tsichlis, and J. S. Brugge. "Phosphatidylinositol 3-kinase is required for integrin-stimulated AKT and Raf-1/mitogen-activated protein kinase pathway activation." Molecular and Cellular Biology 17, no. 8 (1997): 4406–18. http://dx.doi.org/10.1128/mcb.17.8.4406.

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Cell attachment to fibronectin stimulates the integrin-dependent interaction of p85-associated phosphatidylinositol (PI) 3-kinase with integrin-dependent focal adhesion kinase (FAK) as well as activation of the Ras/mitogen-activated protein (MAP) kinase pathway. However, it is not known if this PI 3-kinase-FAK interaction increases the synthesis of the 3-phosphorylated phosphoinositides (3-PPIs) or what role, if any, is played by activated PI 3-kinase in integrin signaling. We demonstrate here the integrin-dependent accumulation of the PI 3-kinase products, PI 3,4-bisphosphate [PI(3,4)P2] and

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Shen, Dadong, Jinlin Zhu, Guofeng Wu, Li Sheng, Haoling Gao, and Pu Wang. "Development of Synthesis of Phosphatidylinositol 3-Kinases Inhibitor Puquitinib Mesylate." Chinese Journal of Organic Chemistry 39, no. 9 (2019): 2676. http://dx.doi.org/10.6023/cjoc201902020.

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Gypakis, A., and H. K. Wasner. "Phosphatidylinositol 3-Kinase and Prostaglandylinositol Cyclic Phosphate (Cyclic PIP), a Mediator of Insulin Action, in the Signal Transduction of Insulin." Biological Chemistry 381, no. 11 (2000): 1139–41. http://dx.doi.org/10.1515/bc.2000.140.

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Abstract It has been suggested that downstream signaling from the insulin receptor to the level of the protein kinases and protein phosphatases is accomplished by prostaglandylinositol cyclic phosphate (cyclic PIP), a proposed second messenger of insulin. However, evidence points also to both phosphatidylinositol 3-kinase, which binds to the tyrosine phosphorylated insulin receptor substrate-1, and the Ras complex in insulin's downstream signaling. We have examined whether a correlation exists between these various observations. It was found that wortmannin, a specific inhibitor of phosphatidy

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COFFER, Paul J., Jing JIN, and James R. WOODGETT. "Protein kinase B (c-Akt): a multifunctional mediator of phosphatidylinositol 3-kinase activation." Biochemical Journal 335, no. 1 (1998): 1–13. http://dx.doi.org/10.1042/bj3350001.

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While a plethora of extracellular molecules exist that modulate cellular functions via binding to membrane receptors inside the cell, their actions are mediated by relatively few signalling mechanisms. One of these is activation of phosphatidylinositol 3-kinase (PI-3K), which results in the generation of a membrane-restricted second messenger, polyphosphatidylinositides containing a 3´-phosphate. How these molecules transduced the effects of agonists of PI-3K was unclear until the recent discovery that several protein kinases become activated upon exposure to 3´-phosphorylated inositol lipids.

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Chapman, Carolyn Riley, Sarah Tyler Evans, Antony M. Carr, and Tamar Enoch. "Requirement of Sequences outside the Conserved Kinase Domain of Fission Yeast Rad3p for Checkpoint Control." Molecular Biology of the Cell 10, no. 10 (1999): 3223–38. http://dx.doi.org/10.1091/mbc.10.10.3223.

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The fission yeast Rad3p checkpoint protein is a member of the phosphatidylinositol 3-kinase-related family of protein kinases, which includes human ATMp. Mutation of the ATMgene is responsible for the disease ataxia-telangiectasia. The kinase domain of Rad3p has previously been shown to be essential for function. Here, we show that although this domain is necessary, it is not sufficient, because the isolated kinase domain does not have kinase activity in vitro and cannot complement a rad3 deletion strain. Using dominant negative alleles of rad3, we have identified two sites N-terminal to the c

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Ravi, Srimadhavi, Bhanu Priya, Pankaj Dubey, Vijay Thiruvenkatam, and Sivapriya Kirubakaran. "Molecular Docking and Molecular Dynamics Simulation Studies of Quinoline-3-Carboxamide Derivatives with DDR Kinases–Selectivity Studies towards ATM Kinase." Chemistry 3, no. 2 (2021): 511–24. http://dx.doi.org/10.3390/chemistry3020036.

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Quinoline-3-carboxamides are an essential class of drug-like small molecules that are known to inhibit the phosphatidylinositol 3-kinase-related kinases (PIKK) family kinases. The quinoline nitrogen is shown to bind to the hinge region of the kinases, making them competitive inhibitors of adenosine triphosphate (ATP). We have previously designed and synthesized quinoline-3-carboxamides as potential ataxia telangiectasia mutated (ATM) kinase inhibitors to function as an adjuvant treatment with DNA damaging agents. This article discusses the molecular docking studies performed with these derivat

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Gold, M. R., V. W. Chan, C. W. Turck, and A. L. DeFranco. "Membrane Ig cross-linking regulates phosphatidylinositol 3-kinase in B lymphocytes." Journal of Immunology 148, no. 7 (1992): 2012–22. http://dx.doi.org/10.4049/jimmunol.148.7.2012.

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Abstract Cross-linking of the B cell AgR results in activation of mature B cells and tolerization of immature B cells. The initial signaling events stimulated by membrane immunoglobulin (mIg) cross-linking are tyrosine phosphorylation of a number of proteins. Among the targets of mIg-induced tyrosine phosphorylation are the tyrosine kinases encoded by the lyn, blk, fyn, and syk genes, the mIg-associated proteins MB-1 and Ig-beta, phospholipase C-gamma 1 and -gamma 2, as well as many unidentified proteins. In this report we show that mIg cross-linking also regulates phosphatidylinositol 3-kinas

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Xu, Jun, Dan Liu, Gordon Gill, and Zhou Songyang. "Regulation of cytokine-independent survival kinase (CISK) by the Phox homology domain and phosphoinositides." Journal of Cell Biology 154, no. 4 (2001): 699–706. http://dx.doi.org/10.1083/jcb.200105089.

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PKB/Akt and serum and glucocorticoid–regulated kinase (SGK) family kinases are important downstream targets of phosphatidylinositol 3 (PI-3) kinase and have been shown to mediate a variety of cellular processes, including cell growth and survival. Although regulation of Akt can be achieved through several mechanisms, including its phosphoinositide-binding Pleckstrin homology (PH) domain, how SGK kinases are targeted and regulated remains to be elucidated. Unlike Akt, cytokine-independent survival kinase (CISK)/SGK3 contains a Phox homology (PX) domain. PX domains have been implicated in severa

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Klippel, A., C. Reinhard, W. M. Kavanaugh, G. Apell, M. A. Escobedo, and L. T. Williams. "Membrane localization of phosphatidylinositol 3-kinase is sufficient to activate multiple signal-transducing kinase pathways." Molecular and Cellular Biology 16, no. 8 (1996): 4117–27. http://dx.doi.org/10.1128/mcb.16.8.4117.

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Phosphatidylinositol (PI) 3-kinase is a cytoplasmic signaling molecule recruited to the membrane by activated growth factor receptors. The p85 subunit of PI 3-kinase links the catalytic p110 subunit to activated growth factor receptors and is required for enzymatic activity of p110. In this report, we describe the effects of expressing novel forms of p110 that are targeted to the membrane by either N-terminal myristoylation or C-terminal farnesylation. The expression of membrane-localized p110 is sufficient to trigger downstream responses characteristic of growth factor action, including the s

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Buhl, Anne Mette, and John C. Cambier. "Phosphorylation of CD19 Y484 and Y515, and Linked Activation of Phosphatidylinositol 3-Kinase, Are Required for B Cell Antigen Receptor-Mediated Activation of Bruton’s Tyrosine Kinase." Journal of Immunology 162, no. 8 (1999): 4438–46. http://dx.doi.org/10.4049/jimmunol.162.8.4438.

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Abstract Bruton’s tyrosine kinase (Btk) plays a critical role in B cell Ag receptor (BCR) signaling, as indicated by the X-linked immunodeficiency and X-linked agammaglobulinemia phenotypes of mice and men that express mutant forms of the kinase. Although Btk activity can be regulated by Src-family and Syk tyrosine kinases, and perhaps by phosphatidylinositol 3,4,5-trisphosphate, BCR-coupled signaling pathways leading to Btk activation are poorly understood. In view of previous findings that CD19 is involved in BCR-mediated phosphatidylinositol 3-kinase (PI3-K) activation, we assessed its role

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