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Beta-adrenergic receptor kinase: primary structure delineates a multigene family.

Publication ,  Journal Article
Benovic, JL; DeBlasi, A; Stone, WC; Caron, MG; Lefkowitz, RJ
Published in: Science
October 13, 1989

The beta-adrenergic receptor kinase (beta-ARK), which specifically phosphorylates only the agonist-occupied form of the beta-adrenergic and closely related receptors, appears to be important in mediating rapid agonist-specific (homologous) desensitization. The structure of this enzyme was elucidated by isolating clones from a bovine brain complementary DNA library through the use of oligonucleotide probes derived from partial amino acid sequence. The beta-ARK cDNA codes for a protein of 689 amino acids (79.7 kilodaltons) with a protein kinase catalytic domain that bears greatest sequence similarity to protein kinase C and the cyclic adenosine monophosphate (cyclic AMP)--dependent protein kinase. When this clone was inserted into a mammalian expression vector and transfected into COS-7 cells, a protein that specifically phosphorylated the agonist-occupied form of the beta 2-adrenergic receptor and phosphorylated, much more weakly, the light-bleached form of rhodopsin was expressed. RNA blot analysis revealed a messenger RNA of four kilobases with highest amounts in brain and spleen. Genomic DNA blot analysis also suggests that beta-ARK may be the first sequenced member of a multigene family of receptor kinases.

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Published In

Science

DOI

ISSN

0036-8075

Publication Date

October 13, 1989

Volume

246

Issue

4927

Start / End Page

235 / 240

Location

United States

Related Subject Headings

  • beta-Adrenergic Receptor Kinases
  • Substrate Specificity
  • Sequence Homology, Nucleic Acid
  • Receptors, Adrenergic, beta
  • Protein Kinases
  • Phosphorylation
  • Organ Specificity
  • Multigene Family
  • Molecular Sequence Data
  • General Science & Technology
 

Citation

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Benovic, J. L., DeBlasi, A., Stone, W. C., Caron, M. G., & Lefkowitz, R. J. (1989). Beta-adrenergic receptor kinase: primary structure delineates a multigene family. Science, 246(4927), 235–240. https://doi.org/10.1126/science.2552582
Benovic, J. L., A. DeBlasi, W. C. Stone, M. G. Caron, and R. J. Lefkowitz. “Beta-adrenergic receptor kinase: primary structure delineates a multigene family.Science 246, no. 4927 (October 13, 1989): 235–40. https://doi.org/10.1126/science.2552582.
Benovic JL, DeBlasi A, Stone WC, Caron MG, Lefkowitz RJ. Beta-adrenergic receptor kinase: primary structure delineates a multigene family. Science. 1989 Oct 13;246(4927):235–40.
Benovic, J. L., et al. “Beta-adrenergic receptor kinase: primary structure delineates a multigene family.Science, vol. 246, no. 4927, Oct. 1989, pp. 235–40. Pubmed, doi:10.1126/science.2552582.
Benovic JL, DeBlasi A, Stone WC, Caron MG, Lefkowitz RJ. Beta-adrenergic receptor kinase: primary structure delineates a multigene family. Science. 1989 Oct 13;246(4927):235–240.
Journal cover image

Published In

Science

DOI

ISSN

0036-8075

Publication Date

October 13, 1989

Volume

246

Issue

4927

Start / End Page

235 / 240

Location

United States

Related Subject Headings

  • beta-Adrenergic Receptor Kinases
  • Substrate Specificity
  • Sequence Homology, Nucleic Acid
  • Receptors, Adrenergic, beta
  • Protein Kinases
  • Phosphorylation
  • Organ Specificity
  • Multigene Family
  • Molecular Sequence Data
  • General Science & Technology