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Functional differences in the beta gamma complexes of transducin and the inhibitory guanine nucleotide regulatory protein.

Publication ,  Journal Article
Cerione, RA; Gierschik, P; Staniszewski, C; Benovic, JL; Codina, J; Somers, R; Birnbaumer, L; Spiegel, AM; Lefkowitz, RJ; Caron, MG
Published in: Biochemistry
March 10, 1987

We have examined the mechanism of inhibition of adenylate cyclase using the purified alpha and beta gamma subunits of bovine brain inhibitory guanine nucleotide regulatory protein (Ni) (i.e., alpha i and beta gamma N) and bovine retinal transducin (alpha T and beta gamma T) in reconstituted phospholipid vesicle systems. The addition of beta gamma N or beta gamma T to lipid vesicles containing the pure stimulatory guanine nucleotide regulatory protein (Ns) from human erythrocytes as well as a resolved preparation of the catalytic moiety (C) of bovine caudate adenylate cyclase results in significant inhibition of guanine nucleotide stimulated cyclase activity (80-90%). The inhibition by these beta gamma subunit complexes appears to fully account for the inhibitory effects observed with holo-Ni or holotransducin. A variety of structure-function comparisons of the beta gamma N and beta gamma T complexes were performed in order to further probe the molecular mechanisms involved in the inhibitory pathway. Whereas the beta subunits of beta gamma N and beta gamma T appear to be very similar, if not identical, on the basis of comparisons of their gel electrophoretic mobility and immunological cross-reactivity, clear differences exist in the apparent structures of gamma N and gamma T. Interestingly, functional differences are observed in the effectiveness of these two beta gamma complexes to inhibit adenylate cyclase activity. Specifically, while both beta gamma N and beta gamma T are capable of effecting significant levels of inhibition of the guanine nucleotide stimulated activities, the beta gamma N complex is consistently more potent than beta gamma T in inhibiting these activities.(ABSTRACT TRUNCATED AT 250 WORDS)

Duke Scholars

Published In

Biochemistry

DOI

ISSN

0006-2960

Publication Date

March 10, 1987

Volume

26

Issue

5

Start / End Page

1485 / 1491

Location

United States

Related Subject Headings

  • Transducin
  • Structure-Activity Relationship
  • Retina
  • Receptors, Adrenergic, beta
  • Membrane Proteins
  • Macromolecular Substances
  • Isoproterenol
  • Guanosine Triphosphate
  • GTP-Binding Proteins
  • Cricetinae
 

Citation

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Cerione, R. A., Gierschik, P., Staniszewski, C., Benovic, J. L., Codina, J., Somers, R., … Caron, M. G. (1987). Functional differences in the beta gamma complexes of transducin and the inhibitory guanine nucleotide regulatory protein. Biochemistry, 26(5), 1485–1491. https://doi.org/10.1021/bi00379a041
Cerione, R. A., P. Gierschik, C. Staniszewski, J. L. Benovic, J. Codina, R. Somers, L. Birnbaumer, A. M. Spiegel, R. J. Lefkowitz, and M. G. Caron. “Functional differences in the beta gamma complexes of transducin and the inhibitory guanine nucleotide regulatory protein.Biochemistry 26, no. 5 (March 10, 1987): 1485–91. https://doi.org/10.1021/bi00379a041.
Cerione RA, Gierschik P, Staniszewski C, Benovic JL, Codina J, Somers R, et al. Functional differences in the beta gamma complexes of transducin and the inhibitory guanine nucleotide regulatory protein. Biochemistry. 1987 Mar 10;26(5):1485–91.
Cerione, R. A., et al. “Functional differences in the beta gamma complexes of transducin and the inhibitory guanine nucleotide regulatory protein.Biochemistry, vol. 26, no. 5, Mar. 1987, pp. 1485–91. Pubmed, doi:10.1021/bi00379a041.
Cerione RA, Gierschik P, Staniszewski C, Benovic JL, Codina J, Somers R, Birnbaumer L, Spiegel AM, Lefkowitz RJ, Caron MG. Functional differences in the beta gamma complexes of transducin and the inhibitory guanine nucleotide regulatory protein. Biochemistry. 1987 Mar 10;26(5):1485–1491.

Published In

Biochemistry

DOI

ISSN

0006-2960

Publication Date

March 10, 1987

Volume

26

Issue

5

Start / End Page

1485 / 1491

Location

United States

Related Subject Headings

  • Transducin
  • Structure-Activity Relationship
  • Retina
  • Receptors, Adrenergic, beta
  • Membrane Proteins
  • Macromolecular Substances
  • Isoproterenol
  • Guanosine Triphosphate
  • GTP-Binding Proteins
  • Cricetinae