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REGULATOR OF G PROTEIN SIGNALING 7-BINDING PROTEIN; RGS7BP

REGULATOR OF G PROTEIN SIGNALING 7-BINDING PROTEIN; RGS7BP

Alternative titles; symbolsR7-BINDING PROTEIN; R7BPHGNC Approved Gene Symbol: RGS7BPCytogenetic location: 5q12.3 Genomic coordinates (GRCh38): 5:64,505,946-6...

Alternative titles; symbols

  • R7-BINDING PROTEIN; R7BP

HGNC Approved Gene Symbol: RGS7BP

Cytogenetic location: 5q12.3 Genomic coordinates (GRCh38): 5:64,505,946-64,612,329 (from NCBI)

▼ Cloning and Expression
Martemyanov et al. (2005) cloned mouse Rgs7bp, which they called R7bp, by screening for proteins that interact with the R7 subfamily of the regulator of G protein signaling (RGS) family. Database analysis identified human and rat homologs. R7bp contains 4 N-terminal alpha-helices likely to form coiled-coil domains and a C-terminal polybasic region followed by 2 cysteines. Western blot of immunoprecipitates of mouse tissues revealed that R7bp was expressed only in nervous system, including all brain regions tested, retina, and spinal cord.

Drenan et al. (2005) independently cloned mouse Rgs7bp and found that it shares 28% identity with the N-terminal region of R9ap (RGS9BP; 607814), which interacts with Rgs9 (604067) in photoreceptors. Northern blot analysis detected expression of Rgs7bp at high levels in mouse brain and much lower levels in other tissues. Confocal microscopy showed R7bp in the plasma membrane as well as the cytoplasm and nucleus. By mutation analysis of the C-terminal dicysteine motif, Drenan et al. (2005) found that both cysteine residues are palmitoylated and that they regulate the distribution of R7bp between the plasma membrane, cytoplasm, and nucleus. Blocking palmitoylation decreased plasma membrane localization and increased nuclear localization.

▼ Gene Function
By coimmunoprecipitation studies in mouse striatum, Martemyanov et al. (2005) showed that R7bp associates with all 4 members of the R7 family, Rgs6 (603984), Rgs7 (602517), Rgs9 (604067), and Rgs11(603895). R7bp has a broader range of interaction with R7 proteins than R9ap (RGS9BP; 607814), which interacts with Rgs9 and Rgs11 but not Rgs6 or Rgs7. Using pull-down assays, they found that the DEP domain of Rgs9, which is required for Rgs9 binding to R9ap, is also required for Rgs9 binding to R7bp and that R7bp binds R7-Gnb5 (604447) complexes.

Drenan et al. (2005) showed that R7bp binds the R7 subunit of the R7-Gnb5 complex and that Gnb5 may promote this interaction by stabilizing or changing the conformation of the R7 subunit. In the absence of R7bp, R7 proteins failed to associate with the plasma membrane and were cytoplasmic or nuclear. Coexpression with R7bp resulted in plasma membrane recruitment of each R7 protein. In HEK293 cells, R7-Gnb5 complexes bound palmitoylated and nonpalmitoylated R7bp. Confocal microscopy showed translocation of R7-Gnb5-R7bp complexes to the nucleus several hours after depalmitoylation and blocking of repalmitoylation. R7bp dramatically accelerated the kinetics of m2 muscarinic ACh-activated GIRK (see 601534) currents, dependent upon coexpression with Rgs7-Gnb5 complexes. At moderate or high Rgs7-Gnb5 expression, R7bp significantly increased the rates of agonist-independent GIRK deactivation and agonist-dependent activation, suggesting that R7bp facilitates the formation of GIRK channel signaling complexes containing R7 RGS proteins. Nonpalmitoylated R7bp had significantly reduced ability to augment Rgs7-Gnb5 activity, suggesting that palmitoylation of R7bp is required for facilitating modulation of receptor-coupled GIRK channels by targeting Rgs7-Gnb5 complexes to the plasma membrane.

▼ Gene Structure
Drenan et al. (2005) determined that the RGS7BP gene contains 6 exons.

▼ Mapping
Drenan et al. (2005) stated that the human RGS7BP gene maps to chromosome 5q12.3 and the mouse and rat homologs to chromosome 13D1 and 2q13, respectively.

Tags: 5q12.3