The Akt1-eNOS axis illustrates the specificity of kinase-substrate relationships in vivo.

@article{Schleicher2009TheAA,
  title={The Akt1-eNOS axis illustrates the specificity of kinase-substrate relationships in vivo.},
  author={Michael Schleicher and Jun Yu and Takahisa Murata and Berhad Derakhshan and Dimitriy Atochin and Li Qian and Satoshi Kashiwagi and Annarita Di Lorenzo and Kenneth D. Harrison and Paul Lee Huang and William C Sessa},
  journal={Science signaling},
  year={2009},
  volume={2 82},
  pages={ra41}
}
Akt1 is critical for many in vivo functions; however, the cell-specific substrates responsible remain to be defined. Here, we examine the importance of endothelial nitric oxide synthase (eNOS) as an Akt1 substrate by generating Akt1-deficient mice (Akt1(-/-) mice) carrying knock-in mutations (serine to aspartate or serine to alanine substitutions) of the critical Akt1 phosphorylation site on eNOS (serine 1176) that render the enzyme "constitutively active" or "less active." The eNOS mutations… CONTINUE READING

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  • We thank M. Birnbaum for the Akt-1–deficient mice, F. Giordano for helpful discussions, +9 authors NS33335 to P. Huang. Submitted 26 March 2009 Accepted 10 J Citation
  • Schleicher, J. Yu, T. Murata, B. Derakhshan, D…
  • 2009

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