Role of molecular chaperones in G protein beta5/regulator of G protein signaling dimer assembly and G protein betagamma dimer specificity.

@article{Howlett2009RoleOM,
  title={Role of molecular chaperones in G protein beta5/regulator of G protein signaling dimer assembly and G protein betagamma dimer specificity.},
  author={Alyson C Howlett and Amy J Gray and Jesse M. Hunter and Barry M. Willardson},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 24},
  pages={16386-99}
}
The G protein betagamma subunit dimer (Gbetagamma) and the Gbeta5/regulator of G protein signaling (RGS) dimer play fundamental roles in propagating and regulating G protein pathways, respectively. How these complexes form dimers when the individual subunits are unstable is a question that has remained unaddressed for many years. In the case of Gbetagamma, recent studies have shown that phosducin-like protein 1 (PhLP1) works as a co-chaperone with the cytosolic chaperonin complex (CCT) to fold… CONTINUE READING

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Experimental cell research

  • J. Grantham, K. I. Brackley, K. R. Willison
  • 2006

NUMBER 24 JOURNAL OF BIOLOGICAL CHEMISTRY 16399 at U iv of St A nrew s on M arch 5, 2015 hp://w w w .jb.org/ D

  • J. N. McLaughlin, C. D. Thulin, S. J. Hart, K. A. Resing, N. G. Ahn, B. M. Willardson
  • Chaperone-mediated G 5-RGS7 and G Assembly JUNE
  • 2002

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