Cited by 556PI3K/AKT/mTOR signaling in cancerProtein Kinase Regulation and GTPase SignalingMetabolism, Diabetes, and Cancer

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Signalling through Class I PI3Ks in mammalian cells

Hawkins, P.T., Anderson, K.E., Davidson, K., Stephens, L.R.·2006·Biochemical Society Transactions

DOI 10.1042/bst0340647

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Abstract

It is now accepted that activation of Class I PI3Ks (phosphoinositide 3-kinases) is one of the most important signal transduction pathways used by cell-surface receptors to control intracellular events. The receptors which access this pathway include those that recognize growth factors, hormones, antigens and inflammatory stimuli, and the cellular events known to be regulated include cell growth, survival, proliferation and movement. We have learnt a great deal about the family of Class I PI3K enzymes themselves and the structural adaptations which allow a variety of cell-surface receptors to regulate their activity. Class I PI3Ks synthesize the phospholipid PtdIns(3,4,5)P3 in the membranes in which they are activated, and it is now accepted that PtdIns(3,4,5)P3 and its dephosphorylation product PtdIns(3,4)P2 are messenger molecules which regulate the localization and function of multiple effectors by binding to their specific PH (pleckstrin homology) domains. The number of direct PtdIns(3,4,5)P3/PtdIns(3,4)P2 effectors which exist, even within a single cell, creates an extremely complex signalling web downstream of PI3K activation. Some key players are beginning to emerge, however, linking PI3K activity to specific cellular responses. These include small GTPases for the Rho and Arf families which regulate the cytoskeletal and membrane rearrangements required for cell movement, and PKB (protein kinase B), which has important regulatory inputs into the regulation of cell-cycle…

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TOR signaling in growth and metabolism
Wullschleger, S., Loewith, R., & Hall, M. N. (2006) · Cell · doi:10.1016/j.cell.2006.01.016 · Cited by 5,787
The phosphoinositide 3-kinase pathway
Cantley, L. C. (2002) · Science · doi:10.1126/science.296.5573.1655 · Cited by 5,621
Cell Migration: Integrating Signals from Front to Back
Ridley, A. J., Schwartz, M. A., Burridge, K., Firtel, R., Ginsberg, M. H., Borisy, G. G., Parsons, J. T., & Horwitz, A. R. (2003) · Science · doi:10.1126/science.1092053 · Cited by 5,109
High Frequency of Mutations of the PIK3CA Gene in Human Cancers
Samuels, Y., Wang, Z., Bardelli, A., Silliman, N., Ptak, J., Szabo, S., Yan, H., Gazdar, A. F., Powell, S. M., Riggins, G. J., et al. (2004) · Science · doi:10.1126/science.1096502 · Cited by 3,448
Targeting RAS signalling pathways in cancer therapy
Downward, J. (2003) · Nature reviews. Cancer · doi:10.1038/nrc969 · Cited by 3,354
The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism
Engelman, J. A., Luo, J., & Cantley, L. C. (2006) · Nature Reviews Genetics · doi:10.1038/nrg1879 · Cited by 3,330
Ras, PI(3)K and mTOR signalling controls tumour cell growth
Shaw, R. J., & Cantley, L. C. (2006) · Nature · doi:10.1038/nature04869 · Cited by 2,019
Phosphatidylinositol-3-OH kinase direct target of Ras
Rodriguez-Viciana, P., Warne, P. H., Dhand, R., Vanhaesebroeck, B., Gout, I., Fry, M. J., Waterfield, M. D., & Downward, J. (1994) · Nature · doi:10.1038/370527a0 · Cited by 1,954
Synthesis and Function of 3-Phosphorylated Inositol Lipids
Vanhaesebroeck, B., Leevers, S. J., Ahmadi, K., Timms, J., Katso, R., Driscoll, P. C., Woscholski, R., Parker, P. J., & Waterfield, M. D. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.535 · Cited by 1,535
Beyond PTEN mutations: the PI3K pathway as an integrator of multiple inputs during tumorigenesis
Cully, M., You, H., Levine, A. J., & Mak, T. W. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1819 · Cited by 1,267
Structural Determinants of Phosphoinositide 3-Kinase Inhibition by Wortmannin, LY294002, Quercetin, Myricetin, and Staurosporine
Walker, E. H., Pacold, M. E., Perišić, O., Stephens, L., Hawkins, P. T., Wymann, M. P., & Williams, R. L. (2000) · Molecular Cell · doi:10.1016/s1097-2765(05)00089-4 · Cited by 1,211
Self-citation
Central Role for G Protein-Coupled Phosphoinositide 3-Kinase γ in Inflammation
Hirsch, E., Katanaev, V. L., Garlanda, C., Azzolino, O., Pirola, L., Silengo, L., Sozzani, S., Mantovani, A., Altruda, F., & Wymann, M. P. (2000) · Science · doi:10.1126/science.287.5455.1049 · Cited by 1,209
A Pharmacological Map of the PI3-K Family Defines a Role for p110α in Insulin Signaling
Knight, Z. A., Gonzalez, B., Feldman, M. E., Zunder, E. R., Goldenberg, D. D., Williams, O., Loewith, R., Stokoe, D., Balla, A., Toth, B., et al. (2006) · Cell · doi:10.1016/j.cell.2006.03.035 · Cited by 1,174
Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: the role of phosphatidylinositol 3,4,5-trisphosphate in neutrophil responses
Arcaro, A., & Wymann, M. P. (1993) · Biochemical Journal · doi:10.1042/bj2960297 · Cited by 1,138
Function of PI3Kγ in Thymocyte Development, T Cell Activation, and Neutrophil Migration
Sasaki, T., Irie-Sasaki, J., Jones, R. G., Oliveira-dos-Santos, A., Stanford, W. L., Bolon, B. N., Wakeham, A. C., Itié, A., Bouchard, D., Kozieradzki, I., et al. (2000) · Science · doi:10.1126/science.287.5455.1040 · Cited by 1,027
Phosphoinositide 3-kinase: the key switch mechanism in insulin signalling
SHEPHERD, P. R., WITHERS, D. J., & SIDDLE, K. (1998) · Biochemical Journal · doi:10.1042/bj3330471 · Cited by 953
Phosphatidylinositol 3-kinase mutations identified in human cancer are oncogenic
Kang, S., Bader, A. G., & Vogt, P. K. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408864102 · Cited by 827
PI3K in lymphocyte development, differentiation and activation
Okkenhaug, K., & Vanhaesebroeck, B. (2003) · Nature reviews. Immunology · doi:10.1038/nri1056 · Cited by 824
PDK1, the master regulator of AGC kinase signal transduction
Mora, A., Komander, D., van Aalten, D. M. F., & Alessi, D. R. (2004) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2003.12.022 · Cited by 818
Roles of PLC-β2 and -β3 and PI3Kγ in Chemoattractant-Mediated Signal Transduction
Li, Z., Jiang, H., Xie, W., Zhang, Z., Smrcka, A. V., & Wu, D. (2000) · Science · doi:10.1126/science.287.5455.1046 · Cited by 807
PI 3-kinase, Akt and cell survival
Downward, J. (2004) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2004.01.002 · Cited by 791
Blockade of PI3Kγ suppresses joint inflammation and damage in mouse models of rheumatoid arthritis
Camps, M., Rückle, T., Ji, H., Ardissone, V., Rintelen, F., Shaw, J. P., Ferrandi, C., Chabert, C., Gilliéron, C., Françon, B., et al. (2005) · Nature Medicine · doi:10.1038/nm1284 · Cited by 753
Signal-dependent membrane targeting by pleckstrin homology (PH) domains
Lemmon, M. A., & Ferguson, K. M. (2000) · Biochemical Journal · doi:10.1042/bj3500001 · Cited by 739
Chemotaxis: signalling the way forward
Haastert, P. J. M. V., & Devreotes, P. N. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1435 · Cited by 706
Structure and function of phosphoinositide 3-kinases
Wymann, M. P., & Pirola, L. (1998) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s0005-2760(98)00139-8 · Cited by 667
mTOR·RICTOR Is the Ser473 Kinase for Akt/Protein Kinase B in 3T3-L1 Adipocytes
Hresko, R. C., & Mueckler, M. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508361200 · Cited by 642
Redox regulation of PI 3‐kinase signalling via inactivation of PTEN
Leslie, N. R., Bennett, D., Lindsay, Y. E., Stewart, H., Gray, A., & Downes, C. P. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg513 · Cited by 631
Crystal Structure and Functional Analysis of Ras Binding to Its Effector Phosphoinositide 3-Kinase γ
Pacold, M. E., Suire, S., Perišić, O., Lara‐González, S., Davis, C. T., Walker, E. H., Hawkins, P. T., Stephens, L., Eccleston, J. F., & Williams, R. L. (2000) · Cell · doi:10.1016/s0092-8674(00)00196-3 · Cited by 611
Self-citation
PI 3-kinase p110β: a new target for antithrombotic therapy
Jackson, S. P., Schoenwaelder, S. M., Goncalves, I., Nesbitt, W. S., Yap, C. L., Wright, C. E., Kenche, V. B., Anderson, K. E., Dopheide, S. M., Yuan, Y., et al. (2005) · Nature Medicine · doi:10.1038/nm1232 · Cited by 582
Self-citation
Phosphoinositide Recognition Domains
Lemmon, M. A. (2003) · Traffic · doi:10.1034/j.1600-0854.2004.00071.x · Cited by 571
Activation of phosphoinositide 3‐kinase by interaction with Ras and by point mutation.
Rodriguez‐Viciana, P., Warne, P. H., Vanhaesebroeck, B., Waterfield, M. D., & Downward, J. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00602.x · Cited by 566
The Gβγ Sensitivity of a PI3K Is Dependent upon a Tightly Associated Adaptor, p101
Stephens, L., Eguinoa, A., Erdjument‐Bromage, H., Lui, M. L., Cooke, F. T., Coadwell, J., Smrcka, A., Thelen, M., Cadwallader, K. A., Tempst, P., et al. (1997) · Cell · doi:10.1016/s0092-8674(00)80187-7 · Cited by 557
Self-citation
Pathway of phosphatidylinositol(3,4,5)-trisphosphate synthesis in activated neutrophils
Stephens, L., Hughes, K. T., & Irvine, R. F. (1991) · Nature · doi:10.1038/351033a0 · Cited by 494
Self-citation
The PHD Finger of the Chromatin-Associated Protein ING2 Functions as a Nuclear Phosphoinositide Receptor
Gozani, O., Karuman, P., Jones, D. R., Ivanov, D., Cha, J., Lugovskoy, A. A., Baird, C. L., Zhu, H., Field, S. J., Lessnick, S. L., et al. (2003) · Cell · doi:10.1016/s0092-8674(03)00480-x · Cited by 487
PI3Kγ Modulates the Cardiac Response to Chronic Pressure Overload by Distinct Kinase-Dependent and -Independent Effects
Patrucco, E., Notte, A., Barberis, L., Selvetella, G., Maffei, A., Brancaccio, M., Marengo, S., Russo, G., Azzolino, O., Rybalkin, S. D., et al. (2004) · Cell · doi:10.1016/j.cell.2004.07.017 · Cited by 465
Critical role for the p110α phosphoinositide-3-OH kinase in growth and metabolic regulation
Foukas, L. C., Claret, M., Pearce, W., Okkenhaug, K., Meek, S., Peskett, E., Sancho, S., Smith, A. J. H., Withers, D. J., & Vanhaesebroeck, B. (2006) · Nature · doi:10.1038/nature04694 · Cited by 463
Signalling by PI3K isoforms: insights from gene-targeted mice
Vanhaesebroeck, B., Ali, K., Bilancio, A., Geering, B., & Foukas, L. C. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.02.008 · Cited by 450
Agonist-stimulated synthesis of phosphatidylinositol(3,4,5)-trisphosphate
Stephens, L., Jackson, T., & Hawkins, P. T. (1993) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(93)90072-w · Cited by 447
Self-citation
Regulation of membrane traffic by phosphoinositide 3-kinases
Lindmo, K., & Stenmark, H. (2006) · Journal of Cell Science · doi:10.1242/jcs.02855 · Cited by 436
An enzymatic cascade of Rab5 effectors regulates phosphoinositide turnover in the endocytic pathway
Shin, H., Hayashi, M., Christoforidis, S., Lacas‐Gervais, S., Hoepfner, S., Wenk, M. R., Modregger, J., Uttenweiler‐Joseph, S., Wilm, M. S., Nystuen, A., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200505128 · Cited by 409
Essential role for the p110δ phosphoinositide 3-kinase in the allergic response
Ali, K., Bilancio, A., Thomas, M. J., Pearce, W. P., Gilfillan, A. M., Tkaczyk, C., Kuehn, N., Gray, A., Giddings, J., Peskett, E., et al. (2004) · Nature · doi:10.1038/nature02991 · Cited by 386
Svp1p defines a family of phosphatidylinositol 3,5‐bisphosphate effectors
Dove, S. K., Piper, R. C., McEwen, R. K., Yu, J. W., King, M. C., Hughes, D. C., Thuring, J. W., Holmes, A. B., Cooke, F. T., Michell, R. H., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600203 · Cited by 366
P hosphoinositide 3-K inase : Diverse Roles in Immune Cell Activation
Deane, J. A., & Fruman, D. A. (2004) · Annual Review of Immunology · doi:10.1146/annurev.immunol.22.012703.104721 · Cited by 347
Signaling Specificity by Ras Family GTPases Is Determined by the Full Spectrum of Effectors They Regulate
Rodriguez-Viciana, P., Sabatier, C., & McCormick, F. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.11.4943-4954.2004 · Cited by 327
The oncogenic properties of mutant p110α and p110β phosphatidylinositol 3-kinases in human mammary epithelial cells
Zhao, J. J., Liu, Z., Wang, L., Shin, E., Loda, M. F., & Roberts, T. M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508988102 · Cited by 324
Phosphoinositide 3‐kinase‐dependent activation of Rac
Welch, H. C. E., Coadwell, W. J., Stephens, L., & Hawkins, P. T. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00454-x · Cited by 320
Self-citation
VAV proteins as signal integrators for multi-subunit immune-recognition receptors
Turner, M., & Billadeau, D. D. (2002) · Nature reviews. Immunology · doi:10.1038/nri840 · Cited by 320
Bifurcation of Lipid and Protein Kinase Signals of PI3Kγ to the Protein Kinases PKB and MAPK
Bondeva, T., Pirola, L., Bulgarelli-Leva, G., Rubio, I., Wetzker, R., & Wymann, M. P. (1998) · Science · doi:10.1126/science.282.5387.293 · Cited by 314
Identification of ARAP3, a Novel PI3K Effector Regulating Both Arf and Rho GTPases, by Selective Capture on Phosphoinositide Affinity Matrices
Krugmann, S., Anderson, K. E., Ridley, S. H., Risso, N., McGregor, A., Coadwell, J., Davidson, K., Eguinoa, A., Ellson, C. D., Lipp, P., et al. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00434-3 · Cited by 302
Self-citation
Leukocytes navigate by compass: roles of PI3Kγ and its lipid products
Rickert, P. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01841-9 · Cited by 295
Sequential activation of class IB and class IA PI3K is important for the primed respiratory burst of human but not murine neutrophils
Condliffe, A. M. (2005) · Blood · doi:10.1182/blood-2005-03-0944 · Cited by 295
Structure, function, and biology of SHIP proteins
Rohrschneider, L. R., Fuller, J. F., Wolf, I., Liu, Y., & Lucas, D. M. (2000) · Genes & Development · doi:10.1101/gad.14.5.505 · Cited by 294
Phosphoinositide 3-Kinase γ Is an Essential Amplifier of Mast Cell Function
Laffargue, M., Calvez, R., Finan, P. M., Trifilieff, A., Barbier, M., Altruda, F., Hirsch, E., & Wymann, M. P. (2002) · Immunity · doi:10.1016/s1074-7613(02)00282-0 · Cited by 286
Heterodimeric Phosphoinositide 3-Kinase Consisting of p85 and p110β Is Synergistically Activated by the βγ Subunits of G Proteins and Phosphotyrosyl Peptide
Kurosu, H., Maehama, T., Okada, T., Yamamoto, T., Hoshino, S.-I., Fukui, Y., Ui, M., Hazeki, O., & Katada, T. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.39.24252 · Cited by 260
Absence of the lipid phosphatase SHIP2 confers resistance to dietary obesity
Sleeman, M. W., Wortley, K. E., Lai, K. V., Gowen, L. C., Kintner, J., Kline, W. O., García, K., Stitt, T. N., Yancopoulos, G. D., Wiegand, S. J., et al. (2005) · Nature Medicine · doi:10.1038/nm1178 · Cited by 260
Cloning of a human phosphoinositide 3-kinase with a C2 domain that displays reduced sensitivity to the inhibitor wortmannin
Jan Domin, Y., Pagès, F., Volinia, S., Rittenhouse-Simmons, S., Zvelebil, M., Stein, R. C., & Waterfield, M. D. (1997) · Biochemical Journal · doi:10.1042/bj3260139 · Cited by 251
Roles of Gβγ in membrane recruitment and activation of p110γ/p101 phosphoinositide 3-kinase γ
Brock, C., Schaefer, M., Reusch, H. P., Czupalla, C., Michalke, M., Spicher, K., Schultz, G., & Nürnberg, B. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200210115 · Cited by 238
A novel and evolutionarily conserved PtdIns(3,4,5)P3-binding domain is necessary for DOCK180 signalling
Côté, J., Motoyama, A. B., Bush, J., & Vuori, K. (2005) · Nature Cell Biology · doi:10.1038/ncb1280 · Cited by 231
Probing phosphoinositide functions in signaling and membrane trafficking
Downes, C. P., Gray, A., & Lucocq, J. M. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2005.03.008 · Cited by 226
Phosphoinositide 3-kinase in disease: timing, location, and scaffolding
Wymann, M. P., & Marone, R. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.02.011 · Cited by 212
Targeted biallelic inactivation of Pten in the mouse prostate leads to prostate cancer accompanied by increased epithelial cell proliferation but not by reduced apoptosis.
Ma, X.-Q., der Made, A. C. J. Z.-V., Autar, B., van der Korput, H. A., Vermeij, M., van Duijn, P. V., Cleutjens, K., de Krijger, R. D., Krimpenfort, P., Berns, A., et al. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-4519 · Cited by 204
Regulation of Akt/PKB Ser473 Phosphorylation
Bayascas, J. R., & Alessi, D. R. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.03.020 · Cited by 184
Structural insights into the regulation of PDK1 by phosphoinositides and inositol phosphates
Komander, D., Fairservice, A., Deák, M., Kular, G. S., Prescott, A. R., Downes, C. P., Safrany, S. T., Alessi, D. R., & van Aalten, D. M. F. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600379 · Cited by 170
p84, a New Gβγ-Activated Regulatory Subunit of the Type IB Phosphoinositide 3-Kinase p110γ
Suire, S., Coadwell, J., Ferguson, G. J., Davidson, K., Hawkins, P. T., & Stephens, L. (2005) · Current Biology · doi:10.1016/j.cub.2005.02.020 · Cited by 164
Self-citation
Membrane binding domains
Hurley, J. H. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2006.02.020 · Cited by 158
Phosphoinositide 3-kinase regulatory subunit p85α suppresses insulin action via positive regulation of PTEN
Taniguchi, C. M., Tran, T. T., Kondo, T., Luo, J., Ueki, K., Cantley, L. C., & Kahn, C. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604628103 · Cited by 153
Cutting Edge: T Cell Development Requires the Combined Activities of the p110γ and p110δ Catalytic Isoforms of Phosphatidylinositol 3-Kinase
Webb, L. M. C., Vigorito, E., Wymann, M. P., Hirsch, E., & Turner, M. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.5.2783 · Cited by 148
Phosphoinositide 3‐kinase controls early and late events in mammalian cell division
García, Z., Kumar, A., Marqués, M., Cortés, I., & Carrera, A. C. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7600967 · Cited by 138
The in vivo role of PtdIns(3,4,5)P3 binding to PDK1 PH domain defined by knockin mutation
McManus, E. J., Collins, B., Ashby, P. R., Prescott, A. R., Murray-Tait, V., Armit, L. J., Arthur, J. S. C., & Alessi, D. R. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600218 · Cited by 134
Characterization of p87PIKAP, a Novel Regulatory Subunit of Phosphoinositide 3-Kinase γ That Is Highly Expressed in Heart and Interacts with PDE3B
Voigt, P., Dorner, M. B., & Schaefer, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512502200 · Cited by 127
Activation of Phosphoinositide 3-Kinase γ by Ras
Suire, S., Hawkins, P. T., & Stephens, L. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00933-8 · Cited by 118
Self-citation
A targeted mass spectrometric analysis of phosphatidylinositol phosphate species
Milne, S. B., Ivanova, P. T., DeCamp, D. L., Hsueh, R. C., & Brown, H. A. (2005) · Journal of Lipid Research · doi:10.1194/jlr.d500010-jlr200 · Cited by 117
Receptor specificity of growth factor-stimulated synthesis of 3-phosphorylated inositol lipids in Swiss 3T3 cells.
JACKSON, T. R., Stephens, L., & Hawkins, P. T. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42049-2 · Cited by 114
Self-citation
Essential role of PI3Kδ and PI3Kγ in thymocyte survival
Swat, W., Montgrain, V., Doggett, T. A., Douangpanya, J., Puri, K. D., Vermi, W., & Diacovo, T. G. (2005) · Blood · doi:10.1182/blood-2005-08-3300 · Cited by 111
Phosphoinositide 3-kinases as drug targets in cancer
Stephens, L., WILLIAMS, R., & Hawkins, P. T. (2005) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2005.03.002 · Cited by 105
Self-citation
Then Negative Regulation of Phosphoinositide 3-Kinase Signaling by p85 and Its Implication in Cancer
Luo, J., & Cantley, L. C. (2005) · Cell Cycle · doi:10.4161/cc.4.10.2062 · Cited by 99
Telomerase RNA Mutated in Autosomal Dyskeratosis Congenita Reconstitutes a Weakly Active Telomerase Enzyme Defective in Telomere Elongation
Cerone, M. A., Ward, R. J., Londoño‐Vallejo, A., & Autexier, C. (2005) · Cell Cycle · doi:10.4161/cc.4.4.1586 · Cited by 87
Signal transduction; a practical approach
(1993) · Comparative Biochemistry and Physiology Part A Physiology · doi:10.1016/0300-9629(93)90059-d · Cited by 85
Phosphoinositide 3-Kinase C2β Regulates Cytoskeletal Organization and Cell Migration via Rac-dependent Mechanisms
Katso, R., Pardo, O. E., Palamidessi, A., Franz, C. M., Marinov, M., Laurentiis, A. D., Downward, J., Scita, G., Ridley, A. J., Waterfield, M. D., et al. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-11-1083 · Cited by 82
Changes in the concentration and fatty acid composition of phosphoinositides induced by hormones in hepatocytes
Augert, G., Blackmore, P. F., & Exton, J. H. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81651-4 · Cited by 76
The role of SHIP1 in macrophage programming and activation
Rauh, M. J., Sly, L. M., Kalesnikoff, J., Hughes, M. R., Cao, L., Lam, V., & Krystal, G. (2004) · Biochemical Society Transactions · doi:10.1042/bst0320785 · Cited by 75
Mutated PI 3-Kinases: Cancer Targets on a Silver Platter
Kang, S., Bader, A. G., Zhao, L., & Vogt, P. K. (2005) · Cell Cycle · doi:10.4161/cc.4.4.1593 · Cited by 62
Expression profiling of lineage differentiation in pluripotential human embryonal carcinoma cells.
Houldsworth, J., Heath, S. C., Bosl, G. J., Studer, L., & Chaganti, R. S. K. (2002) · PubMed · Cited by 59
The role of phosphoinositides and phosphorylation in regulation of NADPH oxidase
Perišić, O., Wilson, M. I., Karathanassis, D., Bravo, J., Pacold, M. E., Ellson, C. D., Hawkins, P. T., Stephens, L., & Williams, R. L. (2004) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2003.11.003 · Cited by 43
Self-citation
The N‐terminus of phosphoinositide 3‐kinase‐C2β regulates lipid kinase activity and binding to clathrin
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Application of phosphoinositide-binding domains for the detection and quantification of specific phosphoinositides
Furutani, M., Tsujita, K., Itoh, T., Ijuin, T., & Takenawa, T. (2006) · Analytical Biochemistry · doi:10.1016/j.ab.2006.05.014 · Cited by 39
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Vermeren, S., Cooper, M. A., Williams, D. H., Hawkins, P. T., & Stephens, L. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3620725 · Cited by 32
Self-citation
Advances in Procedures for the Detection and Localization of Inositol Phospholipid Signals in Cells, Tissues, and Enzyme Assays
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Research works printed but not linked: 4

Krugmann, 2002, Biochem. J., 362, 725, 10.1042/bj3620725 · DOI
Suire, 2006, Nat. Cell Biol.
Houldsworth, 2002, Cell Growth Differ., 13, 257
McManus, 2004, EMBO J., 23, 2071, 10.1038/sj.emboj.7600218 · DOI

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Authors: Hawkins, P. T., Anderson, K. E., Davidson, K., & Stephens, L. R.
Affiliations: Babraham Institute (GB)
ORCID: Hawkins, P.T.
Anderson, K.E.
Stephens, L.R.
Venue: Biochemical Society Transactions
Publisher: Portland Press Ltd.
Published: 2006-10-01
Volume: 34
Issue: 5
Pages: 647-662
ISSN: 0300-5127 (ISSN-L)
1470-8752
DOI: 10.1042/bst0340647
OpenAlex: W1988224683
Cited by: 540
References: 89
Citations by year: 2026: 5 · 2025: 11 · 2024: 10 · 2023: 11 · 2022: 17 · 2021: 20 · 2020: 14 · 2019: 14 · 2018: 21 · 2017: 21 · 2016: 24 · 2015: 19 · 2014: 34 · 2013: 33 · 2012: 48
FWCI: 3.71
Type: journal article
Language: en
Open access: closed
Locations: Biochemical Society Transactions (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Keywords: class I PI3K, phosphatidylinositol 3,4,5-trisphosphate, PtdIns(3,4)P2, pleckstrin homology domain, cell surface receptors, small GTPases, Akt, cell growth and proliferation, cell survival, oncogenes, PTEN, PI3K isoforms, PI3K inhibitors, transgenic mouse model
MeSH terms: Animals, Cell Division, Cell Movement, Cell Survival, Mammals, Models, Biological, Phosphatidylinositols, Receptors, Cell Surface, Signal Transduction, GTP Phosphohydrolases, Carboxylesterase

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Signalling through Class I PI3Ks in mammalian cells

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