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Articles in PresS, published online ahead of print May 8, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00501.2001
Submitted on October 18, 2001
Accepted on April 30, 2002
1 Physiology, University of Massachusetts Medical School, Worcester, Massachusetts, USA
2 Biomedical Imaging Group, University of Massachusetts Medical School, Worcester, Massachusetts, USA
* To whom correspondence should be addressed. E-mail: mitsuo.ikebe{at}umassmed.edu.
Telokin is an acidic protein having sequence identical to the C-terminal domain of myosin light chain kinase (MLCK), produced by an alternate promoter of the MLCK gene. While it is abundantly expressed in smooth muscle, its physiological function is not understood. In the present study, we attempted to clarify the function of telokin by analyzing its spatial and temporal localization in living single smooth muscle cells. Primary cultured smooth muscle cells were transfected with green fluorescent protein (GFP)-tagged telokin. The telokin-GFP localized mostly diffuse in cytosol. The stimulation with both sodium nitroprusside (SNP) and 8-bromo-cyclic GMP induced translocation of GFP-tagged telokin to near plasma membrane in living single smooth muscle cells. Time required for the translocation was slow and it took more than 10 min at room temperature. Mutation of the phosphorylation sites of telokin (S13A, S19A, and S13A/S19A) significantly attenuated SNP induced translocation. Both KT 5823 (PKG inhibitor) and PD98059 (MAPK inhibitor) diminished the telokin-GFP translocation. These results suggest that telokin changes its intra-cellular localization due to the phosphorylation at Ser13 and/or Ser19 via by cGMP-signaling pathway.
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