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

Citations

Publications citing this paper.
Showing 1-10 of 35 extracted citations

Metabolic regulation by salt inducible kinases

Frontiers in Biology • 2011
View 6 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…