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dc.contributor.authorKomatsu, Satoshi
dc.contributor.authorMiyazaki, Koji
dc.contributor.authorTuft, Richard A.
dc.contributor.authorIkebe, Mitsuo
dc.date2022-08-11T08:09:31.000
dc.date.accessioned2022-08-23T16:34:11Z
dc.date.available2022-08-23T16:34:11Z
dc.date.issued2002-08-15
dc.date.submitted2007-12-21
dc.identifier.citationAm J Physiol Cell Physiol. 2002 Sep;283(3):C752-61. <a href="http://dx.doi.org/10.1152/ajpcell.00501.2001">Link to article on publisher's site</a>
dc.identifier.issn0363-6143 (Print)
dc.identifier.doi10.1152/ajpcell.00501.2001
dc.identifier.pmid12176732
dc.identifier.urihttp://hdl.handle.net/20.500.14038/38277
dc.description.abstractTelokin is an acidic protein with a sequence identical to the COOH-terminal domain of myosin light chain kinase (MLCK) produced by an alternate promoter of the MLCK gene. Although 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 diffusely in cytosol. 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. 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 (cGMP-dependent protein kinase inhibitor) and PD-98059 (mitogen-activated protein kinase inhibitor) diminished the telokin-GFP translocation. These results suggest that telokin changes its intracellular localization because of phosphorylation at Ser13 and/or Ser19 via the cGMP-signaling pathway.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12176732&dopt=Abstract ">Link to article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1152/ajpcell.00501.2001
dc.subjectAnimals
dc.subjectBinding Sites
dc.subjectCOS Cells
dc.subjectCell Membrane
dc.subjectCells, Cultured
dc.subjectCyclic GMP
dc.subjectCyclic GMP-Dependent Protein Kinases
dc.subjectEnzyme Inhibitors
dc.subjectGreen Fluorescent Proteins
dc.subjectLuminescent Proteins
dc.subjectMuscle Proteins
dc.subjectMuscle, Smooth
dc.subjectMutagenesis, Site-Directed
dc.subjectMyosin-Light-Chain Kinase
dc.subjectMyosins
dc.subjectNitric Oxide Donors
dc.subjectPeptides
dc.subjectPhosphorylation
dc.subjectProtein Binding
dc.subjectProtein Transport
dc.subjectRecombinant Fusion Proteins
dc.subjectSignal Transduction
dc.subjectSwine
dc.subjectTrachea
dc.subjectTransfection
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleTranslocation of telokin by cGMP signaling in smooth muscle cells
dc.typeJournal Article
dc.source.journaltitleAmerican journal of physiology. Cell physiology
dc.source.volume283
dc.source.issue3
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/115
dc.identifier.contextkey407410
html.description.abstract<p>Telokin is an acidic protein with a sequence identical to the COOH-terminal domain of myosin light chain kinase (MLCK) produced by an alternate promoter of the MLCK gene. Although 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 diffusely in cytosol. 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. 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 (cGMP-dependent protein kinase inhibitor) and PD-98059 (mitogen-activated protein kinase inhibitor) diminished the telokin-GFP translocation. These results suggest that telokin changes its intracellular localization because of phosphorylation at Ser13 and/or Ser19 via the cGMP-signaling pathway.</p>
dc.identifier.submissionpathoapubs/115
dc.contributor.departmentDepartment of Physiology
dc.source.pagesC752-61


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