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Evidence for the Role of Membrane Receptor Lateral Movement in GTP-Binding Protein-Mediated Signal Transduction

  • David A. Jans
Part of the Molecular Biology Intelligence Unit book series (MBIU)

Abstract

As we saw in the previous chapter, direct measurements indicate that plasma membrane polypeptide hormone receptors are mobile within the plane of the lipid bilayer. Tyrosine kinase and GTP-binding protein activating receptors appear to be essentially different in terms of their lateral mobility properties, and it seems plausible to relate these differences to their distinct signal transduction mechanisms.1–8 As discussed in chapter 4, lateral movement of hormone-occupied tyrosine kinase receptors is required to effect receptor dimerization which triggers the association of a variety of cytosolic signaling molecules in order to effect signal transduction.9–13 Movement of the hormone-occupied receptor is not required subsequent to dimerization, and consistent with this, activated receptors appear to be aggregated and essentially immobile at physiological temperature (see section E, chapter 4).

Keywords

Adenylate Cyclase Adenylate Cyclase Activation Renal Epithelial Cell Mobile Fraction Lateral Mobility 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© R.G. Landes Company 1997

Authors and Affiliations

  • David A. Jans
    • 1
  1. 1.John Curtin School of Medical ResearchAustralian National UniversityCanberraAustralia

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