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Science 31 January 1997:
Vol. 275. no. 5300, pp. 661 - 665
DOI: 10.1126/science.275.5300.661
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Reports

Regulation of Neuronal Survival by the Serine-Threonine Protein Kinase Akt

Henryk Dudek, Sandeep Robert Datta, * Thomas F. Franke, * Morris J. Birnbaum, Ryoji Yao, Geoffrey M. Cooper, Rosalind A. Segal, David R. Kaplan, Michael E. Greenberg dagger

A signaling pathway was delineated by which insulin-like growth factor 1 (IGF-1) promotes the survival of cerebellar neurons. IGF-1 activation of phosphoinositide 3-kinase (PI3-K) triggered the activation of two protein kinases, the serine-threonine kinase Akt and the p70 ribosomal protein S6 kinase (p70S6K). Experiments with pharmacological inhibitors, as well as expression of wild-type and dominant-inhibitory forms of Akt, demonstrated that Akt but not p70S6K mediates PI3-K-dependent survival. These findings suggest that in the developing nervous system, Akt is a critical mediator of growth factor-induced neuronal survival.

H. Dudek, S. R. Datta, M. E. Greenberg, Division of Neuroscience, Department of Neurology, Children's Hospital, and Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA.
T. F. Franke, Montreal Neurological Institute, McGill University, PQ H3A 2B4, Canada; and Division of Signal Transduction, Beth Israel Hospital, and Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
M. J. Birnbaum, Howard Hughes Medical Institute, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.
R. Yao and G. M. Cooper, Division of Molecular Genetics, Dana-Farber Cancer Institute, and Department of Pathology, Harvard Medical School, Boston, MA 02115, USA.
R. A. Segal, Department of Neurology, Beth Israel Hospital, and Harvard Medical School, Boston, MA 02115, USA.
D. R. Kaplan, Montreal Neurological Institute, McGill University, PQ H3A 2B4, Canada.
*   These authors made comparable contributions to this report.

dagger    To whom correspondence should be addressed.

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S. Brand, F. Beigel, T. Olszak, K. Zitzmann, S. T. Eichhorst, J.-M. Otte, J. Diebold, H. Diepolder, B. Adler, C. J. Auernhammer, et al. (2005)
Am J Physiol Gastrointest Liver Physiol 289, G960-G968
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Apoptosis-associated Tyrosine Kinase (AATYK) Has Differential Ca2+-dependent Phosphorylation States in Response to Survival and Apoptotic Conditions in Cerebellar Granule Cells.
M. Tomomura and T. Furuichi (2005)
J. Biol. Chem. 280, 35157-35163
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Zn2+ Inhibits Mitochondrial Movement in Neurons by Phosphatidylinositol 3-Kinase Activation.
L. M. Malaiyandi, A. S. Honick, G. L. Rintoul, Q. J. Wang, and I. J. Reynolds (2005)
J. Neurosci. 25, 9507-9514
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Identification of MMP-15 as an Anti-apoptotic Factor in Cancer Cells.
R. Abraham, J. Schafer, M. Rothe, J. Bange, P. Knyazev, and A. Ullrich (2005)
J. Biol. Chem. 280, 34123-34132
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Corneal Cell Survival in Adenovirus Type 19 Infection Requires Phosphoinositide 3-Kinase/Akt Activation.
M. S. Rajala, R. V. S. Rajala, R. A. Astley, A. L. Butt, and J. Chodosh (2005)
J. Virol. 79, 12332-12341
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Activation of protein kinase C{beta}I constitutes a new neurotrophic pathway for deafferented spiral ganglion neurons.
F. Lallemend, S. Hadjab, G. Hans, G. Moonen, P. P. Lefebvre, and B. Malgrange (2005)
J. Cell Sci. 118, 4511-4525
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Increased Expression of Mcl-1 Is Required for Protection against Serum Starvation in Phosphatase and Tensin Homologue on Chromosome 10 Null Mouse Embryonic Fibroblasts, but Repression of Bim Is Favored in Human Glioblastomas.
M. Austin and S. J. Cook (2005)
J. Biol. Chem. 280, 33280-33288
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Activation of Mammalian Target of Rapamycin in Transformed B Lymphocytes Is Nutrient Dependent but Independent of Akt, Mitogen-Activated Protein Kinase/Extracellular Signal-Regulated Kinase Kinase, Insulin Growth Factor-I, and Serum.
P. Wlodarski, M. Kasprzycka, X. Liu, M. Marzec, E. S. Robertson, A. Slupianek, and M. A. Wasik (2005)
Cancer Res. 65, 7800-7808
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State-dependent Ras signaling and AMPA receptor trafficking.
Y. Qin, Y. Zhu, J. P. Baumgart, R. L. Stornetta, K. Seidenman, V. Mack, L. van Aelst, and J. J. Zhu (2005)
Genes & Dev. 19, 2000-2015
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Cellular and molecular mechanisms of sex differences in renal ischemia-reperfusion injury.
A. Kher, K. K. Meldrum, M. Wang, B. M. Tsai, J. M. Pitcher, and D. R. Meldrum (2005)
Cardiovasc Res 67, 594-603
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Docosahexaenoic acid: A positive modulator of Akt signaling in neuronal survival.
M. Akbar, F. Calderon, Z. Wen, and H.-Y. Kim (2005)
PNAS 102, 10858-10863
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PED Mediates AKT-Dependent Chemoresistance in Human Breast Cancer Cells.
G. Stassi, M. Garofalo, M. Zerilli, L. Ricci-Vitiani, C. Zanca, M. Todaro, F. Aragona, G. Limite, G. Petrella, and G. Condorelli (2005)
Cancer Res. 65, 6668-6675
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Phosphorylation of Human p53 at Serine 46 Determines Promoter Selection and whether Apoptosis Is Attenuated or Amplified.
L. D. Mayo, Y. R. Seo, M. W. Jackson, M. L. Smith, J. R. Guzman, C. K. Korgaonkar, and D. B. Donner (2005)
J. Biol. Chem. 280, 25953-25959
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PTEN deletion in Bergmann glia leads to premature differentiation and affects laminar organization.
Q. Yue, M. Groszer, J. S. Gil, A. J. Berk, A. Messing, H. Wu, and X. Liu (2005)
Development 132, 3281-3291
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Essential role of protein kinase B{gamma} (PKB{gamma}/Akt3) in postnatal brain development but not in glucose homeostasis.
O. Tschopp, Z.-Z. Yang, D. Brodbeck, B. A. Dummler, M. Hemmings-Mieszczak, T. Watanabe, T. Michaelis, J. Frahm, and B. A. Hemmings (2005)
Development 132, 2943-2954
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The Roles of Leptin and Adiponectin: A Novel Paradigm in Adipocytokine Regulation of Liver Fibrosis and Stellate Cell Biology.
X. Ding, N. K. Saxena, S. Lin, A. Xu, S. Srinivasan, and F. A. Anania (2005)
Am. J. Pathol. 166, 1655-1669
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TEF, an antiapoptotic bZIP transcription factor related to the oncogenic E2A-HLF chimera, inhibits cell growth by down-regulating expression of the common {beta} chain of cytokine receptors.
T. Inukai, T. Inaba, J. Dang, R. Kuribara, K. Ozawa, A. Miyajima, W. Wu, A. T. Look, Y. Arinobu, H. Iwasaki, et al. (2005)
Blood 105, 4437-4444
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{alpha}-Melanocortin and Endothelin-1 Activate Antiapoptotic Pathways and Reduce DNA Damage in Human Melanocytes.
A. L. Kadekaro, R. Kavanagh, H. Kanto, S. Terzieva, J. Hauser, N. Kobayashi, S. Schwemberger, J. Cornelius, G. Babcock, H. G. Shertzer, et al. (2005)
Cancer Res. 65, 4292-4299
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