* 607193

REGULATOR OF G PROTEIN SIGNALING 20; RGS20


Other entities represented in this entry:

RGSZ1 ISOFORM, INCLUDED
RET-RGS ISOFORM, INCLUDED

HGNC Approved Gene Symbol: RGS20

Cytogenetic location: 8q11.23     Genomic coordinates (GRCh38): 8:53,851,795-53,959,303 (from NCBI)


TEXT

Description

Regulator of G protein signaling (RGS) proteins are regulatory and structural components of G protein-coupled receptor complexes. RGS proteins are GTPase-activating proteins for Gi (see GNAI1; 139310) and Gq (see GNAQ; 600998) class G-alpha proteins. They accelerate transit through the cycle of GTP binding and hydrolysis and thereby accelerate signaling kinetics and termination.


Cloning and Expression

Using bovine brain RGS20, or Gz-Gap, as probe, Wang et al. (1998) cloned human RGS20, which they designated RGSZ1, from HeLa cell and fetal brain cDNA libraries. The deduced 218-amino acid sequence has a calculated molecular mass of about 25 kD. It contains a cysteine string that is a potential site for multiple palmitoylation N-terminal to its RGS box. RGSZ1 lacks the 156-residue N-terminal extension found in the related bovine retinal protein Ret-Rgs1. RGSZ1 shares 58% identity with GAIP (RGS19; 605071). Northern blot analysis revealed a 1.7-kb transcript expressed exclusively in brain, with highest levels in the caudate nucleus and temporal lobe.

Using rat G-alpha-z (GNAZ; 139160) as bait in a yeast 2-hybrid screen, Glick et al. (1998) cloned a partial RGSZ1 sequence from a human brain cDNA library. They cloned the full-length cDNA by PCR of a fetal brain cDNA library. Glick et al. (1998) confirmed that the deduced 217-amino acid protein contains an N-terminal polycysteine string motif and a C-terminal RGS core domain. Northern blot analysis detected expression of RGSZ1 predominantly in caudate nucleus, with lower levels in most other regions and much lower levels in subthalamic nucleus and thalamus.

By genomic sequence analysis, Barker et al. (2001) determined that RGSZ1 and the human homolog of Ret-Rgs, a retina-specific bovine transcript, are splice variants of the full-length RGS20 gene. The authors predicted a total of 6 translation products from the RGS20 gene encoding sequences from 152 to 382 amino acids in length. Northern blot analysis using exon-specific probes showed that a broad band centered at 1.6 kb predominates in amygdala, while a transcript of about 2.1 kb predominates in human retina.


Gene Function

Wang et al. (1997) found that the bovine brain homolog of RGSZ1, Gz-Gap, is a membrane protein. Its activity was associated with at least 2 separate proteins of 22 and 28 kD that had similar specific activities. When coreconstituted into phospholipid vesicles with trimeric G-alpha-z and M2 muscarinic receptors (CHRM2; 118493), Gz-Gap did not alter the rate of nucleotide association or dissociation, but accelerated agonist-induced GTP hydrolysis.

Wang et al. (1998) found that purified recombinant human RGSZ1 accelerated the hydrolysis of G-alpha-z. They noted that RGSZ1 has no obvious membrane-spanning region but is tightly membrane-bound in brain, likely due to palmytoylation of the cysteine string. Further, the regulatory activity of RGSZ1 within membranes was found to depend on stable bilayer association. When coreconstituted into phospholipid vesicles with G-alpha-z and M2 muscarinic receptors, human RGSZ1 increased agonist-stimulated GTPase more than 15-fold. Protein kinase C (PKC; see 176960) phosphorylation of G-alpha-z inhibited RGSZ1 activity. Glick et al. (1998) confirmed the substrate preference of RGSZ1 for G-alpha-z and also noted inhibition of RGSZ1 activity following PKC phosphorylation of G-alpha-z.


Gene Structure

Barker et al. (2001) identified 7 exons within the RGS20 gene, which spans 107 kb.


Mapping

By genomic sequence analysis, Sierra et al. (2002) mapped the RGS20 gene to chromosome 8q12.1. Barker et al. (2001) and Sierra et al. (2002) mapped the mouse Rgs20 gene to chromosome 1 by interspecific backcross mapping.


REFERENCES

  1. Barker, S. A., Wang, J., Sierra, D. A., Ross, E. M. RGSZ1 and Ret RGS: two of several splice variants from the gene RGS20. Genomics 78: 223-229, 2001. [PubMed: 11735229, related citations] [Full Text]

  2. Glick, J. L., Meigs, T. E., Miron, A., Casey, P. J. RGSZ1, a G-z-selective regulator of G protein signaling whose action is sensitive to the phosphorylation state of G-z-alpha. J. Biol. Chem. 273: 26008-26013, 1998. [PubMed: 9748279, related citations] [Full Text]

  3. Sierra, D. A., Gilbert, D. J., Householder, D., Grishin, N. V., Yu, K., Ukidwe, P., Barker, S. A., He, W., Wensel, T. G., Otero, G., Brown, G., Copeland, N. G., Jenkins, N. A., Wilkie, T. M. Evolution of the regulators of G-protein signaling multigene family in mouse and human. Genomics 79: 177-185, 2002. [PubMed: 11829488, related citations] [Full Text]

  4. Wang, J., Ducret, A., Tu, Y., Kozasa, T., Aebersold, R., Ross, E. M. RGSZ1, a G-z-selective RGS protein in brain: structure, membrane association, regulation by G-alpha-z phosphorylation, and relationship to a G-z GTPase-activating protein subfamily. J. Biol. Chem. 273: 26014-26025, 1998. [PubMed: 9748280, related citations] [Full Text]

  5. Wang, J., Tu, Y., Woodson, J., Song, X., Ross, E. M. A GTPase-activating protein for the G protein G-alpha-z: identification, purification, and mechanism of action. J. Biol. Chem. 272: 5732-5740, 1997. [PubMed: 9038185, related citations] [Full Text]


Creation Date:
Patricia A. Hartz : 8/29/2002
Edit History:
mgross : 08/29/2002

* 607193

REGULATOR OF G PROTEIN SIGNALING 20; RGS20


Other entities represented in this entry:

RGSZ1 ISOFORM, INCLUDED
RET-RGS ISOFORM, INCLUDED

HGNC Approved Gene Symbol: RGS20

Cytogenetic location: 8q11.23     Genomic coordinates (GRCh38): 8:53,851,795-53,959,303 (from NCBI)


TEXT

Description

Regulator of G protein signaling (RGS) proteins are regulatory and structural components of G protein-coupled receptor complexes. RGS proteins are GTPase-activating proteins for Gi (see GNAI1; 139310) and Gq (see GNAQ; 600998) class G-alpha proteins. They accelerate transit through the cycle of GTP binding and hydrolysis and thereby accelerate signaling kinetics and termination.


Cloning and Expression

Using bovine brain RGS20, or Gz-Gap, as probe, Wang et al. (1998) cloned human RGS20, which they designated RGSZ1, from HeLa cell and fetal brain cDNA libraries. The deduced 218-amino acid sequence has a calculated molecular mass of about 25 kD. It contains a cysteine string that is a potential site for multiple palmitoylation N-terminal to its RGS box. RGSZ1 lacks the 156-residue N-terminal extension found in the related bovine retinal protein Ret-Rgs1. RGSZ1 shares 58% identity with GAIP (RGS19; 605071). Northern blot analysis revealed a 1.7-kb transcript expressed exclusively in brain, with highest levels in the caudate nucleus and temporal lobe.

Using rat G-alpha-z (GNAZ; 139160) as bait in a yeast 2-hybrid screen, Glick et al. (1998) cloned a partial RGSZ1 sequence from a human brain cDNA library. They cloned the full-length cDNA by PCR of a fetal brain cDNA library. Glick et al. (1998) confirmed that the deduced 217-amino acid protein contains an N-terminal polycysteine string motif and a C-terminal RGS core domain. Northern blot analysis detected expression of RGSZ1 predominantly in caudate nucleus, with lower levels in most other regions and much lower levels in subthalamic nucleus and thalamus.

By genomic sequence analysis, Barker et al. (2001) determined that RGSZ1 and the human homolog of Ret-Rgs, a retina-specific bovine transcript, are splice variants of the full-length RGS20 gene. The authors predicted a total of 6 translation products from the RGS20 gene encoding sequences from 152 to 382 amino acids in length. Northern blot analysis using exon-specific probes showed that a broad band centered at 1.6 kb predominates in amygdala, while a transcript of about 2.1 kb predominates in human retina.


Gene Function

Wang et al. (1997) found that the bovine brain homolog of RGSZ1, Gz-Gap, is a membrane protein. Its activity was associated with at least 2 separate proteins of 22 and 28 kD that had similar specific activities. When coreconstituted into phospholipid vesicles with trimeric G-alpha-z and M2 muscarinic receptors (CHRM2; 118493), Gz-Gap did not alter the rate of nucleotide association or dissociation, but accelerated agonist-induced GTP hydrolysis.

Wang et al. (1998) found that purified recombinant human RGSZ1 accelerated the hydrolysis of G-alpha-z. They noted that RGSZ1 has no obvious membrane-spanning region but is tightly membrane-bound in brain, likely due to palmytoylation of the cysteine string. Further, the regulatory activity of RGSZ1 within membranes was found to depend on stable bilayer association. When coreconstituted into phospholipid vesicles with G-alpha-z and M2 muscarinic receptors, human RGSZ1 increased agonist-stimulated GTPase more than 15-fold. Protein kinase C (PKC; see 176960) phosphorylation of G-alpha-z inhibited RGSZ1 activity. Glick et al. (1998) confirmed the substrate preference of RGSZ1 for G-alpha-z and also noted inhibition of RGSZ1 activity following PKC phosphorylation of G-alpha-z.


Gene Structure

Barker et al. (2001) identified 7 exons within the RGS20 gene, which spans 107 kb.


Mapping

By genomic sequence analysis, Sierra et al. (2002) mapped the RGS20 gene to chromosome 8q12.1. Barker et al. (2001) and Sierra et al. (2002) mapped the mouse Rgs20 gene to chromosome 1 by interspecific backcross mapping.


REFERENCES

  1. Barker, S. A., Wang, J., Sierra, D. A., Ross, E. M. RGSZ1 and Ret RGS: two of several splice variants from the gene RGS20. Genomics 78: 223-229, 2001. [PubMed: 11735229] [Full Text: https://doi.org/10.1006/geno.2001.6659]

  2. Glick, J. L., Meigs, T. E., Miron, A., Casey, P. J. RGSZ1, a G-z-selective regulator of G protein signaling whose action is sensitive to the phosphorylation state of G-z-alpha. J. Biol. Chem. 273: 26008-26013, 1998. [PubMed: 9748279] [Full Text: https://doi.org/10.1074/jbc.273.40.26008]

  3. Sierra, D. A., Gilbert, D. J., Householder, D., Grishin, N. V., Yu, K., Ukidwe, P., Barker, S. A., He, W., Wensel, T. G., Otero, G., Brown, G., Copeland, N. G., Jenkins, N. A., Wilkie, T. M. Evolution of the regulators of G-protein signaling multigene family in mouse and human. Genomics 79: 177-185, 2002. [PubMed: 11829488] [Full Text: https://doi.org/10.1006/geno.2002.6693]

  4. Wang, J., Ducret, A., Tu, Y., Kozasa, T., Aebersold, R., Ross, E. M. RGSZ1, a G-z-selective RGS protein in brain: structure, membrane association, regulation by G-alpha-z phosphorylation, and relationship to a G-z GTPase-activating protein subfamily. J. Biol. Chem. 273: 26014-26025, 1998. [PubMed: 9748280] [Full Text: https://doi.org/10.1074/jbc.273.40.26014]

  5. Wang, J., Tu, Y., Woodson, J., Song, X., Ross, E. M. A GTPase-activating protein for the G protein G-alpha-z: identification, purification, and mechanism of action. J. Biol. Chem. 272: 5732-5740, 1997. [PubMed: 9038185] [Full Text: https://doi.org/10.1074/jbc.272.9.5732]


Creation Date:
Patricia A. Hartz : 8/29/2002

Edit History:
mgross : 08/29/2002