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Phosphorylation of telokin by cyclic nucleotide kinases and the identification of in vivo phosphorylation sites in smooth muscle.

Publication ,  Journal Article
MacDonald, JA; Walker, LA; Nakamoto, RK; Gorenne, I; Somlyo, AV; Somlyo, AP; Haystead, TA
Published in: FEBS Lett
August 18, 2000

The Ca(2+)-independent acceleration of dephosphorylation of the regulatory light chain of smooth muscle myosin and relaxation of smooth muscle by telokin are enhanced by cyclic nucleotide-activated protein kinase(s) [Wu et al. (1998) J. Biol. Chem. 273, 11362-113691. The purpose of this study was to determine the in vivo site(s) and in vitro rates of telokin phosphorylation and to evaluate the possible effects of sequential phosphorylation by different kinases. The in vivo site(s) of phosphorylation of telokin were determined in rabbit smooth muscles of longitudinal ileum and portal vein. Following stimulation of ileum with forskolin (20 microM) the serine at position 13 was the only amino acid to exhibit increased phosphorylation. Rabbit portal vein telokin was phosphorylated on both Ser-13 and -19 as a result of forskolin and GTPgammaS stimulation in vivo. Point mutation of Ser-13 (to Ala or Asp) abolished in vitro phosphorylation by cyclic nucleotide-dependent protein kinases.

Duke Scholars

Published In

FEBS Lett

DOI

ISSN

0014-5793

Publication Date

August 18, 2000

Volume

479

Issue

3

Start / End Page

83 / 88

Location

England

Related Subject Headings

  • Time Factors
  • Serine Endopeptidases
  • Recombinant Proteins
  • Rabbits
  • Protein Kinases
  • Portal Vein
  • Point Mutation
  • Phosphorylation
  • Peptides
  • Peptide Fragments
 

Citation

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MacDonald, J. A., Walker, L. A., Nakamoto, R. K., Gorenne, I., Somlyo, A. V., Somlyo, A. P., & Haystead, T. A. (2000). Phosphorylation of telokin by cyclic nucleotide kinases and the identification of in vivo phosphorylation sites in smooth muscle. FEBS Lett, 479(3), 83–88. https://doi.org/10.1016/s0014-5793(00)01884-6
MacDonald, J. A., L. A. Walker, R. K. Nakamoto, I. Gorenne, A. V. Somlyo, A. P. Somlyo, and T. A. Haystead. “Phosphorylation of telokin by cyclic nucleotide kinases and the identification of in vivo phosphorylation sites in smooth muscle.FEBS Lett 479, no. 3 (August 18, 2000): 83–88. https://doi.org/10.1016/s0014-5793(00)01884-6.
MacDonald JA, Walker LA, Nakamoto RK, Gorenne I, Somlyo AV, Somlyo AP, et al. Phosphorylation of telokin by cyclic nucleotide kinases and the identification of in vivo phosphorylation sites in smooth muscle. FEBS Lett. 2000 Aug 18;479(3):83–8.
MacDonald, J. A., et al. “Phosphorylation of telokin by cyclic nucleotide kinases and the identification of in vivo phosphorylation sites in smooth muscle.FEBS Lett, vol. 479, no. 3, Aug. 2000, pp. 83–88. Pubmed, doi:10.1016/s0014-5793(00)01884-6.
MacDonald JA, Walker LA, Nakamoto RK, Gorenne I, Somlyo AV, Somlyo AP, Haystead TA. Phosphorylation of telokin by cyclic nucleotide kinases and the identification of in vivo phosphorylation sites in smooth muscle. FEBS Lett. 2000 Aug 18;479(3):83–88.
Journal cover image

Published In

FEBS Lett

DOI

ISSN

0014-5793

Publication Date

August 18, 2000

Volume

479

Issue

3

Start / End Page

83 / 88

Location

England

Related Subject Headings

  • Time Factors
  • Serine Endopeptidases
  • Recombinant Proteins
  • Rabbits
  • Protein Kinases
  • Portal Vein
  • Point Mutation
  • Phosphorylation
  • Peptides
  • Peptide Fragments