Salt-inducible kinase-1 represses cAMP response element-binding protein activity both in the nucleus and in the cytoplasm.

@article{Katoh2004SaltinducibleKR,
  title={Salt-inducible kinase-1 represses cAMP response element-binding protein activity both in the nucleus and in the cytoplasm.},
  author={Yoshiko Katoh and Hiroshi Takemori and Li Min and Masaaki Muraoka and Junko Doi and Nanao Horike and Mitsuhiro Okamoto},
  journal={European journal of biochemistry},
  year={2004},
  volume={271 21},
  pages={
          4307-19
        }
}
Salt-inducible kinase-1 (SIK1) is phosphorylated at Ser577 by protein kinase A in adrenocorticotropic hormone-stimulated Y1 cells, and the phospho-SIK1 translocates from the nucleus to the cytoplasm. The phospho-SIK1 is dephosphorylated in the cytoplasm and re-enters the nucleus several hours later. By using green-fluorescent protein-tagged SIK1 fragments, we found that a peptide region (586-612) was responsible for the nuclear localization of SIK1. The region was named the 'RK-rich region… CONTINUE READING
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