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RGSZ1, a Gz-selective regulator of G protein signaling whose action is sensitive to the phosphorylation state of Gzalpha.

Publication ,  Journal Article
Glick, JL; Meigs, TE; Miron, A; Casey, PJ
Published in: J Biol Chem
October 2, 1998

Regulators of G protein signaling (RGS) are a family of proteins that attenuate the activity of the trimeric G proteins. RGS proteins act as GTPase-activating proteins (GAPs) for the alpha subunits of several trimeric G proteins, much like the GAPs that regulate the activity of monomeric G proteins such as Ras. RGS proteins have been cloned from many eukaryotes, and those whose biochemical activity has been characterized regulate the members of the Gi family of G proteins; some forms can also act on Gq proteins. In an ongoing effort to elucidate the role of Gzalpha in cell signaling, the yeast two-hybrid system was employed to identify proteins that could interact with a mutationally activated form of Gzalpha. A novel RGS, termed RGSZ1, was identified that is most closely related to two existing RGS proteins termed RetRGS1 and GAIP. Northern blot analysis revealed that expression of RGSZ1 was limited to brain, and expression was particularly high in the caudate nucleus. Biochemical characterization of recombinant RGSZ1 protein revealed that RGSZ1 was indeed a GAP and, most significantly, showed a marked preference for Gzalpha over other members of the Gialpha family. Phosphorylation of Gzalpha by protein kinase C, an event known to occur in cells and that was previously shown to influence alpha-betagamma interactions of Gz, rendered the G protein much less susceptible to RGSZ1 action.

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Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

October 2, 1998

Volume

273

Issue

40

Start / End Page

26008 / 26013

Location

United States

Related Subject Headings

  • ras GTPase-Activating Proteins
  • Signal Transduction
  • Sequence Homology, Amino Acid
  • Sequence Analysis, DNA
  • Recombinant Proteins
  • RNA, Messenger
  • RGS Proteins
  • Proteins
  • Protein Processing, Post-Translational
  • Protein Kinase C
 

Citation

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Glick, J. L., Meigs, T. E., Miron, A., & Casey, P. J. (1998). RGSZ1, a Gz-selective regulator of G protein signaling whose action is sensitive to the phosphorylation state of Gzalpha. J Biol Chem, 273(40), 26008–26013. https://doi.org/10.1074/jbc.273.40.26008
Glick, J. L., T. E. Meigs, A. Miron, and P. J. Casey. “RGSZ1, a Gz-selective regulator of G protein signaling whose action is sensitive to the phosphorylation state of Gzalpha.J Biol Chem 273, no. 40 (October 2, 1998): 26008–13. https://doi.org/10.1074/jbc.273.40.26008.
Glick JL, Meigs TE, Miron A, Casey PJ. RGSZ1, a Gz-selective regulator of G protein signaling whose action is sensitive to the phosphorylation state of Gzalpha. J Biol Chem. 1998 Oct 2;273(40):26008–13.
Glick, J. L., et al. “RGSZ1, a Gz-selective regulator of G protein signaling whose action is sensitive to the phosphorylation state of Gzalpha.J Biol Chem, vol. 273, no. 40, Oct. 1998, pp. 26008–13. Pubmed, doi:10.1074/jbc.273.40.26008.
Glick JL, Meigs TE, Miron A, Casey PJ. RGSZ1, a Gz-selective regulator of G protein signaling whose action is sensitive to the phosphorylation state of Gzalpha. J Biol Chem. 1998 Oct 2;273(40):26008–26013.

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

October 2, 1998

Volume

273

Issue

40

Start / End Page

26008 / 26013

Location

United States

Related Subject Headings

  • ras GTPase-Activating Proteins
  • Signal Transduction
  • Sequence Homology, Amino Acid
  • Sequence Analysis, DNA
  • Recombinant Proteins
  • RNA, Messenger
  • RGS Proteins
  • Proteins
  • Protein Processing, Post-Translational
  • Protein Kinase C