Low resolution structure of the human alpha4 protein (IgBP1) and studies on the stability of alpha4 and of its yeast ortholog Tap42.

@article{Smetana2006LowRS,
  title={Low resolution structure of the human alpha4 protein (IgBP1) and studies on the stability of alpha4 and of its yeast ortholog Tap42.},
  author={Juliana Helena Costa Smetana and Cristiano Luiz Pinto Oliveira and Willy Jablonka and Thelma Aguiar Pertinhez and Fl{\'a}via Raquel Gonçalves Carneiro and M{\'o}nica Montero-Lomel{\'i} and Iris L. Torriani and Nilson I. T. Zanchin},
  journal={Biochimica et biophysica acta},
  year={2006},
  volume={1764 4},
  pages={724-34}
}
The yeast Tap42 and mammalian alpha4 proteins belong to a highly conserved family of regulators of the type 2A phosphatases, which participate in the rapamycin-sensitive signaling pathway, connecting nutrient availability to cell growth. The mechanism of regulation involves binding of Tap42 to Sit4 and PPH21/22 in yeast and binding of alpha4 to the catalytic subunits of type 2A-related phosphatases PP2A, PP4 and PP6 in mammals. Both recombinant proteins undergo partial proteolysis, generating… CONTINUE READING

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