Cited by 184Retinoids in leukemia and cellular processesProtein Kinase Regulation and GTPase SignalingPI3K/AKT/mTOR signaling in cancer

The DOI matches its Crossref record; 65 of the 67 references it cites were found in a registry or an index.

Rapid, Nongenomic Actions of Retinoic Acid on Phosphatidylinositol-3-Kinase Signaling Pathway Mediated by the Retinoic Acid Receptor

Open access

Masiá, Susana, Alvarez, Susana, de Lera, Angel R., Barettino, Domingo·2007·Molecular Endocrinology

DOI 10.1210/me.2007-0062

Open this paper in CoChat — free account Open PDF

Abstract

Retinoic acid (RA) treatment of SH-SY5Y neuroblastoma cells results in activation of phosphatidylinositol-3-kinase (PI3K) signaling pathway, and this activation is required for RA-induced differentiation. Here we show that RA activates PI3K and ERK1/2 MAPK signaling pathways through a rapid, nongenomic mechanism that does not require new gene transcription or newly synthesized proteins. Activation of PI3K by RA appears to involve the classical nuclear receptor, retinoic acid receptor (RAR), on the basis of the pharmacological profile of the activation, loss, and gain of function experiments with mouse embryo fibroblast-RAR(alpha beta gamma)(L-/L-) null cells, and the physical association between liganded RAR and PI3K activity. The association of RAR with the two subunits of PI3K was differentially regulated by the ligand. Immunoprecipitation experiments performed in SH-SY5Y cells showed stable association between RARalpha and p85, the regulatory subunit of PI3K, independently of the presence of RA. In contrast, ligand administration increased the association of p110, the catalytic subunit of PI3K, to this complex. The intracellular localization of RAR proved to be relevant for PI3K activation. A chimerical RAR fusing c-Src myristylation domain to the N terminus of RARalpha (Myr-RARalpha) was targeted to plasma membrane. Transfection of Myr-RARalpha to mouse embryo fibroblast-RAR(alpha beta gamma)(L-/L-) null cells and COS-7 cells results in strong activation of the PI3K signaling pathway, although both in the absence as well in the presence of RA. Our results support a mechanism in which ligand binding to RAR would play a major role in the assembly and intracellular location of a signaling complex involving RAR and the subunits of PI3K.

Integrity signals

Registry

Crossref · 10.1210/me.2007-0062

Cites

65 of 65 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

1 retracted

Activation of Phosphatidylinositol 3-Kinase/Akt Pathway by Androgen through Interaction of p85α, Androgen Receptor, and Src
Sun, M., Yang, L., Feldman, R. I., Sun, X.-M., Bhalla, K. N., Jove, R., Nicosia, S. V., & Cheng, J. Q. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306295200 · Cited by 175
Retracted
Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
Brown, D. A., & Rose, J. K. (1992) · Cell · doi:10.1016/0092-8674(92)90189-j · Cited by 2,921
Production of high-titer helper-free retroviruses by transient transfection.
Pear, W. S., Nolan, G. P., Scott, M. L., & Baltimore, D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.18.8392 · Cited by 2,267
Advanced mammalian gene transfer: high titre retroviral vectors with multiple drug selection markers and a complementary helper-free packaging cell line
Morgenstern, J. P., & Land, H. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.12.3587 · Cited by 2,099
Treatment of High-Risk Neuroblastoma with Intensive Chemotherapy, Radiotherapy, Autologous Bone Marrow Transplantation, and 13-cis-Retinoic Acid
Matthay, K. K., Villablanca, J. G., Seeger, R. C., Stram, D. O., Harris, R. E., Ramsay, N. K. C., Swift, P. S., Shimada, H., Black, C. T., Brodeur, G. M., et al. (1999) · New England Journal of Medicine · doi:10.1056/nejm199910143411601 · Cited by 1,891
Interaction of oestrogen receptor with the regulatory subunit of phosphatidylinositol-3-OH kinase
Simoncini, T., Hafezi‐Moghadam, A., Brazil, D. P., Ley, K. F., Chin, W. W., & Liao, J. K. (2000) · Nature · doi:10.1038/35035131 · Cited by 1,436
Principles for modulation of the nuclear receptor superfamily
Gronemeyer, H., Gustafsson, J.-Å., & Laudet, V. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1551 · Cited by 1,285
Cellular Function of Phosphoinositide 3-Kinases: Implications for Development, Immunity, Homeostasis, and Cancer
Katso, R., Okkenhaug, K., Ahmadi, K., White, S., Timms, J. F., & Waterfield, M. D. (2001) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.17.1.615 · Cited by 1,234
Nongenotropic, Sex-Nonspecific Signaling through the Estrogen or Androgen Receptors
Kousteni, S., Bellido, T., Plotkin, L. I., O’Brien, C. A., Bodenner, D., Li, H., Han, K., Gregorio, G. B. D., Katzenellenbogen, J. A., Katzenellenbogen, B. S., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00268-9 · Cited by 1,163
Cell Membrane and Nuclear Estrogen Receptors (ERs) Originate from a Single Transcript: Studies of ER and ER Expressed in Chinese Hamster Ovary Cells
Razandi, M., Pedram, A., Greene, G. L., & Levin, E. R. (1999) · Molecular Endocrinology · doi:10.1210/mend.13.2.0239 · Cited by 1,075
Nongenomic actions of steroid hormones
Lösel, R., & Wehling, M. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1009 · Cited by 980
Tyrosine kinase/p21ras/MAP‐kinase pathway activation by estradiol‐receptor complex in MCF‐7 cells.
Migliaccio, A., Domenico, M. D., Castoria, G., de Falco, A., Bontempo, P., Nola, E., & Auricchio, F. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00471.x · Cited by 950
Nongenotropic, Sex-Nonspecific Signaling through the Estrogen or Androgen Receptors Dissociation from Transcriptional Activity
Kousteni, S. (2001) · Cell · doi:10.1016/s0092-8674(02)08100-x · Cited by 757
Integration of the extranuclear and nuclear actions of estrogen
Levin, E. R. (2005) · Molecular Endocrinology · doi:10.1210/me.2004-0390 · Cited by 708
SPECIFIC, NONGENOMIC ACTIONS OF STEROID HORMONES
Wehling, M. (1997) · Annual Review of Physiology · doi:10.1146/annurev.physiol.59.1.365 · Cited by 663
Decreased expression of N-myc precedes retinoic acid-induced morphological differentiation of human neuroblastoma
Thiele, C. J., Reynolds, C. P., & Israel, M. A. (1985) · Nature · doi:10.1038/313404a0 · Cited by 649
Acute cardiovascular protective effects of corticosteroids are mediated by non-transcriptional activation of endothelial nitric oxide synthase
Hafezi‐Moghadam, A., Simoncini, T., Yang, Z., Limbourg, F. P., Plumier, J.-C., Rebsamen, M. C., Hsieh, C.-M., Chui, D.-S., Thomas, K. L., Prorock, A. J., et al. (2002) · Nature Medicine · doi:10.1038/nm0502-473 · Cited by 596
Retinoic acid-induced differentiation of cultured human neuroblastoma cells: a comparison with phorbolester-induced differentiation
Påhlman, S., Ruusala, A.-I., Abrahamsson, L., Mattsson, M. E. K., & Esscher, T. (1984) · Cell Differentiation · doi:10.1016/0045-6039(84)90038-1 · Cited by 571
Regulation of the p85/p110 Phosphatidylinositol 3′-Kinase: Stabilization and Inhibition of the p110α Catalytic Subunit by the p85 Regulatory Subunit
Yu, J., Zhang, Y., McIlroy, J., Rordorf-Nikolic, T., Orr, G. A., & Backer, J. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.3.1379 · Cited by 527
Nature of Functional Estrogen Receptors at the Plasma Membrane
Pedram, A., Razandi, M., & Levin, E. R. (2006) · Molecular Endocrinology · doi:10.1210/me.2005-0525 · Cited by 523
PI3‐kinase in concert with Src promotes the S‐phase entry of oestradiol‐stimulated MCF‐7 cells
Castoria, G., Migliaccio, A., Bilancio, A., Domenico, M. D., de Falco, A., Lombardi, M., Fiorentino, R., Varricchio, L., Barone, M. V., & Auricchio, F. (2001) · The EMBO Journal · doi:10.1093/emboj/20.21.6050 · Cited by 477
Proximal Events in Signaling by Plasma Membrane Estrogen Receptors
Razandi, M., Pedram, A., Park, S. T., & Levin, E. R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m205692200 · Cited by 474
Palmitoylation-dependent Estrogen Receptor α Membrane Localization: Regulation by 17β-Estradiol
Acconcia, F., Ascenzi, P., Bocedi, A., Spisni, E., Tomasi, V., Trentalance, A., Visca, P., & Marino, M. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-07-0547 · Cited by 440
Membrane Localization of Phosphatidylinositol 3-Kinase Is Sufficient To Activate Multiple Signal-Transducing Kinase Pathways
Klippel, A., Reinhard, C., Kavanaugh, W. M., Apell, G., Escobedo, M.-A., & Williams, L. T. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.8.4117 · Cited by 440
A short sequence in the p60src N terminus is required for p60src myristylation and membrane association and for cell transformation.
Cross, F. R., Garber, E. A., Pellman, D. S., & Hanafusa, H. (1984) · Molecular and Cellular Biology · doi:10.1128/mcb.4.9.1834 · Cited by 439
Retinoid signalling in the development of the central nervous system
Maden, M. (2002) · Nature Reviews Neuroscience · doi:10.1038/nrn963 · Cited by 428
Retinoic Acid-Induced Growth Inhibition and Morphologic Differentiation of Human Neuroblastoma Cells In Vitro 2
Sidell, N. (1982) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/68.4.589 · Cited by 378
Non-genomic actions of sex steroid hormones
Simoncini, T., & Genazzani, A. R. (2003) · European Journal of Endocrinology · doi:10.1530/eje.0.1480281 · Cited by 369
Plasma Membrane Estrogen Receptors Exist and Functions as Dimers
Razandi, M., Pedram, A., Merchenthaler, I. J., Greene, G. L., & Levin, E. R. (2004) · Molecular Endocrinology · doi:10.1210/me.2004-0115 · Cited by 330
Identification of a Structural Determinant Necessary for the Localization and Function of Estrogen Receptor α at the Plasma Membrane
Razandi, M., Alton, G., Pedram, A., Ghonshani, S., Webb, P., & Levin, E. R. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.5.1633-1646.2003 · Cited by 319
Activation of the Phosphatidylinositol 3-Kinase/Akt Signaling Pathway by Retinoic Acid Is Required for Neural Differentiation of SH-SY5Y Human Neuroblastoma Cells
López‐Carballo, G., Moreno, L., Masiá, S., Pérez, P., & Barettino, D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201869200 · Cited by 301
Self-citation
Molecular Balance between the Regulatory and Catalytic Subunits of Phosphoinositide 3-Kinase Regulates Cell Signaling and Survival
Ueki, K., Fruman, D. A., Brachmann, S. M., Tseng, Y., Cantley, L. C., & Kahn, C. R. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.3.965-977.2002 · Cited by 285
A novel steroid thyroid hormone receptor-related gene inappropriately expressed in human hepatocellular carcinoma
de Thé, H., Marchio, A., Tiollais, P., & Dejean, A. (1987) · Nature · doi:10.1038/330667a0 · Cited by 284
Function of Vitamin A in Vertebrate Embryonic Development
Zile, M. H. (2001) · The Journal of Nutrition · doi:10.1093/jn/131.3.705 · Cited by 263
Thyroid Hormone Induces Rapid Activation of Akt/Protein Kinase B-Mammalian Target of Rapamycin-p70S6KCascade through Phosphatidylinositol 3-Kinase in Human Fibroblasts
Cao, X., Kambe, F., Moeller, L. C., Refetoff, S., & Seo, H. (2004) · Molecular Endocrinology · doi:10.1210/me.2004-0093 · Cited by 241
Rapid effects of retinoic acid on CREB and ERK phosphorylation in neuronal cells
Cañón, E., Cosgaya, J. M., Scsucova, S., & Aranda, A. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-05-0439 · Cited by 184
Transcriptional Activities of Retinoic Acid Receptors
Lefèbvre, P., Martin, P. J., Flajollet, S., Dedieu, S., Billaut, X., & Lefebvre, B. (2005) · Vitamins and hormones · doi:10.1016/s0083-6729(05)70007-8 · Cited by 129
1,25(OH)2‐vitamin D3 induces translocation of the vitamin D receptor (VDR) to the plasma membrane in skeletal muscle cells
Capiati, D. A., Benassati, S., & Boland, R. (2002) · Journal of Cellular Biochemistry · doi:10.1002/jcb.10191 · Cited by 126
Nongenomic Mechanisms of Endothelial Nitric Oxide Synthase Activation by the Selective Estrogen Receptor Modulator Raloxifene
Simoncini, T., Genazzani, A. R., & Liao, J. K. (2002) · Circulation · doi:10.1161/hc1102.105267 · Cited by 125
Rapid signaling at the plasma membrane by a nuclear receptor for thyroid hormone
Storey, N. M., Gentile, S., Ullah, H., Russo, A., Muessel, M. J., Erxleben, C. F. J., & Armstrong, D. L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600089103 · Cited by 123
Rexinoid-Triggered Differentiation and Tumor-Selective Apoptosis of Acute Myeloid Leukemia by Protein Kinase A–Mediated Desubordination of Retinoid X Receptor
Altucci, L., Rossin, A., Hirsch, O., Nebbioso, A., Vitoux, D., Wilhelm, E., Guidez, F., Simone, M. D., Schiavone, E. M., Grimwade, D. J., et al. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-3569 · Cited by 120
Activation of Protein Kinase Cδ by All-trans-retinoic Acid
Kambhampati, S., Li, Y., Verma, A. K., Sassano, A., Majchrzak, B., Deb, D. K., Parmar, S., Giafis, N., Kalvakolanu, D. V., Rahman, A., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301523200 · Cited by 110
Characterization of DNA binding and retinoic acid binding properties of retinoic acid receptor.
Yang, N., Schüle, R., Mangelsdorf, D. J., & Evans, R. M. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.9.3559 · Cited by 109
Nongenotropic, Anti-Apoptotic Signaling of 1α,25(OH)2-Vitamin D3 and Analogs through the Ligand Binding Domain of the Vitamin D Receptor in Osteoblasts and Osteocytes
Vertino, A. M., Bula, C. M., Chen, J., Almeida, M., Han, L., Bellido, T., Kousteni, S., Norman, A. W., & Manolagas, S. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m410720200 · Cited by 105
A Region of the 85-Kilodalton (kDa) Subunit of Phosphatidylinositol 3-Kinase Binds the 110-kDa Catalytic Subunit In Vivo
Klippel, A., Escobedo, J. A., Hu, Q., & Williams, L. T. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.9.5560 · Cited by 104
Rapid activation of endothelial NO synthase by estrogen: evidence for a steroid receptor fast-action complex (SRFC) in caveolae
Chambliss, K. L., & Shaul, P. W. (2002) · Steroids · doi:10.1016/s0039-128x(01)00177-5 · Cited by 94
Activation of Rac1 by phosphatidylinositol 3‐kinase in vivo: role in activation of mitogen‐activated protein kinase (MAPK) pathways and retinoic acid‐induced neuronal differentiation of SH‐SY5Y cells
Pan, J., Kao, Y., Joshi, S., Jeetendran, S., DiPette, D., & Singh, U. S. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03106.x · Cited by 94
Upregulation of Nitric Oxide Production in Vascular Endothelial Cells by All- trans Retinoic Acid Through the Phosphoinositide 3-Kinase/Akt Pathway
Uruno, A., Sugawara, A., Kanatsuka, H., Kagechika, H., Saito, A. M., Sato, K., Kudo, M., Takeuchi, K., & Ito, S. (2005) · Circulation · doi:10.1161/circulationaha.104.500959 · Cited by 85
Synthesis and Characterization of a Highly Potent and Effective Antagonist of Retinoic Acid Receptors
Johnson, A. T., Klein, E. S., Gillett, S. J., Wang, L., Song, T. K., Pino, M. E., & Chandraratna, R. A. S. (1995) · Journal of Medicinal Chemistry · doi:10.1021/jm00024a003 · Cited by 85
Unliganded T3R, but not its oncogenic variant, v‐erbA, suppresses RAR‐dependent transactivation by titrating out RXR.
Barettino, D., Bugge, T. H., Bartůněk, P., Vivanco, M. D., Sonntag-Buck, V., Beug, H., Zenke, M., & Stunnenberg, H. G. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05779.x · Cited by 81
Self-citation
Rapid induction of cAMP/PKA pathway during retinoic acid-induced acute promyelocytic leukemia cell differentiation
Zhao, Q. C., Tao, J., Zhu, Q., Jia, P.-M., Dou, A.-X., Li, X., Cheng, F., Waxman, S., Chen, G.-Q., Chen, S.-J., et al. (2003) · Leukemia · doi:10.1038/sj.leu.2403226 · Cited by 79
Lipid Raft Disruption Triggers Protein Kinase C and Src-dependent Protein Kinase D Activation and Kidins220 Phosphorylation in Neuronal Cells
Cabrera-Poch, N., Sánchez‐Ruiloba, L., Rodríguez‐Martínez, M., & Iglesias, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312242200 · Cited by 71
Retinoids Run Rampant
Appel, B., & Eisen, J. S. (2003) · Neuron · doi:10.1016/s0896-6273(03)00688-3 · Cited by 69
Association of 1 alpha,25-dihydroxyvitamin D3-occupied vitamin D receptors with cellular membrane acceptance sites
Kim, Y. S., MacDonald, P. N., Dedhar, S., & Hruska, K. A. (1996) · Endocrinology · doi:10.1210/en.137.9.3649 · Cited by 64
Cellular retinol-binding protein-I inhibits PI3K/Akt signaling through a retinoic acid receptor-dependent mechanism that regulates p85–p110 heterodimerization
Farias, E., Marzan, C., & Mira-y-Lopez, R. (2004) · Oncogene · doi:10.1038/sj.onc.1208347 · Cited by 52
The phosphoinositide 3-kinase/Akt pathway is essential for the retinoic acid-induced differentiation of F9 cells
Bastien, J., Plassat, J. L., Payrastre, B., & Rochette‐Egly, C. (2005) · Oncogene · doi:10.1038/sj.onc.1209241 · Cited by 46
Classical and novel steroid actions: a unified but complex view
Valverde, M. A., & Parker, M. G. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02075-3 · Cited by 43
Phosphoinositide 3-Kinase Activity Is Required for Retinoic Acid-induced Expression and Activation of the Tissue Transglutaminase
Antonyak, M. A., Boehm, J. E., & Cerione, R. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112259200 · Cited by 38
A rapid, nongenomic pathway facilitates the synaptic transmission induced by retinoic acid at the developing synapse
Liou, J., Ho, S., Shen, M., Liao, Y.-P., Chiu, W., & Kang, K. (2005) · Journal of Cell Science · doi:10.1242/jcs.02603 · Cited by 35
Discovery of Novel Retinoic Acid Receptor Agonists Having Potent Antiproliferative Activity in Cervical Cancer Cells
Zhang, L., Nadzan, A. M., Heyman, R. A., Love, D. L., Mais, D. E., Croston, G. E., Lamph, W. W., & Boehm, M. F. (1996) · Journal of Medicinal Chemistry · doi:10.1021/jm960285j · Cited by 31
A direct protein‐protein interaction is involved in the cooperation between thyroid hormone and retinoic acid receptors and the transcription factor GHF‐1
Palomino, T., Sánchez‐Pacheco, A., de la Peña, P., & Aranda, A. (1998) · The FASEB Journal · doi:10.1096/fasebj.12.12.1201 · Cited by 30
Retinoid‐mediated stimulation of steroid sulfatase activity in myeloid leukemic cell lines requires RARα and RXR and involves the phosphoinositide 3‐kinase and ERK‐MAP kinase pathways
Hughes, P., Zhao, Y., Chandraratna, R. A. S., & Brown, G. (2005) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20579 · Cited by 29
Is there a role for retinoids to treat minimal residual disease in neuroblastoma?
Matthay, K. K., & Reynolds, C. P. (2000) · British Journal of Cancer · doi:10.1054/bjoc.2000.1430 · Cited by 24
Synthesis and Characterization of a Highly Potent and Selective Isotopically Labeled Retinoic Acid Receptor Ligand, ALRT1550
Bennani, Y. L., Marron, K. S., Mais, D. E., Flatten, K. S., Nadzan, A. M., & Boehm, M. F. (1998) · The Journal of Organic Chemistry · doi:10.1021/jo971409i · Cited by 18
Retinoic acid signaling through PI 3-kinase induces differentiation of human endometrial adenocarcinoma cells
Carter, C. A. (2003) · Experimental and Molecular Pathology · doi:10.1016/s0014-4800(03)00033-9 · Cited by 10

Sorted by citations

Retinoic acid receptors: From molecular mechanisms to cancer therapy
di Masi, A., Leboffe, L., De Marinis, E., Pagano, F., Cicconi, L., Rochette-Egly, C., Lo-Coco, F., Ascenzi, P., & Nervi, C. (2015) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2014.12.003 · Cited by 403
Vitamin A and retinoid signaling: genomic and nongenomic effects
Al Tanoury, Z., Piskunov, A., & Rochette-Egly, C. (2013) · Journal of Lipid Research · doi:10.1194/jlr.r030833 · Cited by 408
Essential Role for Retinoic Acid in the Promotion of CD4+ T Cell Effector Responses via Retinoic Acid Receptor Alpha
Hall, J. A., Cannons, J. L., Grainger, J. R., dos Santos, L. M., Hand, T. W., Naik, S., Wohlfert, E. A., Chou, D. B., Oldenhove, G., Robinson, M., et al. (2011) · Immunity · doi:10.1016/j.immuni.2011.03.003 · Cited by 381
Retinoid pathway and cancer therapeutics
Bushue, N., & Wan, Y. Y. (2010) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2010.07.003 · Cited by 385
From carrot to clinic: an overview of the retinoic acid signaling pathway
Theodosiou, M., Laudet, V., & Schubert, M. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0268-z · Cited by 344

See all 184

Authors: Masiá, S., Alvarez, S., de Lera, A. R., & Barettino, D.
Affiliations: Biology of Hormone Action Unit (S.M., D.B.). Department of Molecular and Cellular Pathology and Therapy, Instituto de Biomedicina de Valencia [Consejo Superior de Investigaciones Cientificas (CSIC)], E-46010 Valencia, Spain;
Universidade de Vigo (S.A., A.R.d.L.), Departamento de Química Orgánica, Facultad de Ciencias, E-36200 Vigo, Spain
Consejo Superior de Investigaciones Científicas (ES)
Corresponding author: Barettino, Domingo
Venue: Molecular Endocrinology
Publisher: The Endocrine Society
Published: 2007-10-01
Volume: 21
Issue: 10
Pages: 2391-2402
ISSN: 0888-8809 (ISSN-L)
1944-9917
DOI: 10.1210/me.2007-0062
OpenAlex: W2015219861
Cited by: 184
References: 67
Citations by year: 2026: 3 · 2025: 6 · 2024: 8 · 2023: 2 · 2022: 4 · 2021: 4 · 2020: 9 · 2019: 16 · 2018: 12 · 2017: 5 · 2016: 13 · 2015: 11 · 2014: 16 · 2013: 15 · 2012: 11
FWCI: 5.01
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Molecular Endocrinology (publishedVersion)
PubMed (publishedVersion)
DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion, other-oa)
Funders: European Commission
Generalitat Valenciana
European Regional Development Fund
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinoids in leukemia and cellular processes
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Keywords: retinoic acid, non-genomic signaling, retinoic acid receptor, phosphatidylinositol 3-kinase, PI3K signaling, ERK signaling, neuronal differentiation, SH-SY5Y cells, p85 regulatory subunit, p110 catalytic subunit, RARα, subcellular localization
MeSH terms: Retinoic Acid Receptor alpha, Humans, Tretinoin, Signal Transduction, Receptors, Retinoic Acid, Phosphatidylinositol 3-Kinases, Mitogen-Activated Protein Kinase 1, Cell Line, Tumor, Mitogen-Activated Protein Kinase 3

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Rapid, Nongenomic Actions of Retinoic Acid on Phosphatidylinositol-3-Kinase Signaling Pathway Mediated by the Retinoic Acid Receptor

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks