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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

Rgs16  -  regulator of G-protein signaling 16

Mus musculus

Synonyms: A28-RGS14P, RGS-r, RGS16, Regulator of G-protein signaling 16, Retinal-specific RGS, ...
 
 
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High impact information on Rgs16

  • A subpopulation of endogenous RGS16 in rat liver membranes and overexpressed RGS16 in COS cells, but not the nonpalmitoylated cysteine mutant of RGS16, localized to lipid rafts [1].
  • However, disruption of lipid rafts by treatment with methyl-beta-cyclodextrin did not decrease the GTPase activating protein activity of RGS16 [1].
  • RGS1 and RGS16 were also potent inhibitors of Gq-dependent Ca2+ signaling and acted in a receptor-selective manner [2].
  • Tissue distribution analysis shows that the novel RGS16 is predominantly expressed in liver and pituitary, and that RGS5 is preferentially expressed in heart and skeletal muscle [3].
  • RGS1, RGS2 and RGS16, other members of the R4 subfamily, were expressed in distinct progenitor and mature myeloerythroid and lymphoid lineage blood cells [4].
 

Associations of Rgs16 with chemical compounds

  • The levels of regulatory proteins bearing N-terminal cysteine, such as RGS4, RGS5 and RGS16, are greatly increased in mouse ATE1-/- embryos, which lack arginylation [5].

References

  1. Palmitoylation regulates regulators of G-protein signaling (RGS) 16 function. I. Mutation of amino-terminal cysteine residues on RGS16 prevents its targeting to lipid rafts and palmitoylation of an internal cysteine residue. Hiol, A., Davey, P.C., Osterhout, J.L., Waheed, A.A., Fischer, E.R., Chen, C.K., Milligan, G., Druey, K.M., Jones, T.L. J. Biol. Chem. (2003) [Pubmed]
  2. RGS proteins determine signaling specificity of Gq-coupled receptors. Xu, X., Zeng, W., Popov, S., Berman, D.M., Davignon, I., Yu, K., Yowe, D., Offermanns, S., Muallem, S., Wilkie, T.M. J. Biol. Chem. (1999) [Pubmed]
  3. Characterization of a novel mammalian RGS protein that binds to Galpha proteins and inhibits pheromone signaling in yeast. Chen, C., Zheng, B., Han, J., Lin, S.C. J. Biol. Chem. (1997) [Pubmed]
  4. RGS18 is a myeloerythroid lineage-specific regulator of G-protein-signalling molecule highly expressed in megakaryocytes. Yowe, D., Weich, N., Prabhudas, M., Poisson, L., Errada, P., Kapeller, R., Yu, K., Faron, L., Shen, M., Cleary, J., Wilkie, T.M., Gutierrez-Ramos, C., Hodge, M.R. Biochem. J. (2001) [Pubmed]
  5. The N-end rule pathway as a nitric oxide sensor controlling the levels of multiple regulators. Hu, R.G., Sheng, J., Qi, X., Xu, Z., Takahashi, T.T., Varshavsky, A. Nature (2005) [Pubmed]
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