Isolation of mutations in the catalytic domain of the snf1 kinase that render its activity independent of the snf4 subunit.

@article{Leech2003IsolationOM,
  title={Isolation of mutations in the catalytic domain of the snf1 kinase that render its activity independent of the snf4 subunit.},
  author={Anna M. Leech and Nandita Nath and Rhonda R. McCartney and Martin Schmidt},
  journal={Eukaryotic cell},
  year={2003},
  volume={2 2},
  pages={
          265-73
        }
}
Activation of the Snf1 kinase requires at least two events, phosphorylation of the activation loop on threonine 210 and an Snf4-dependent process that is not completely defined. Snf4 directly interacts with a region of the regulatory domain of Snf1 that may otherwise act as an autoinhibitory domain. In order to gain insight into the regulation of Snf1 kinase by Snf4, deletions in the regulatory domain of the catalytic subunit were engineered and tested for their effect on Snf1 function in the… CONTINUE READING

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