High impact information on Gnb5

• In addition to the plasma membrane, a large portion of RGS9-2 was found in the neuronal specializations, the postsynaptic densities, where it forms complexes with R7BP and its constitutive partner Gbeta5 [1].
• Complexes of the G protein subunit gbeta 5 with the regulators of G protein signaling RGS7 and RGS9. Characterization in native tissues and in transfected cells [2].
• An RGS subfamily consisting of RGS 6, 7, 9, and 11 also interacts with the G protein beta subunit Gbeta5 via a characteristic Ggamma-like domain [3].
• RGS7 complex formation and colocalization with the Gbeta5 subunit in the adult rat brain and influence on Gbeta5gamma2-mediated PLCbeta signaling [4].
• This study describes the colocalized distribution and dimeric complex formation between RGS7, a GTPase-activating protein for several heterotrimeric Galpha protein families, and the Gbeta5 subunit in the adult rat brain [4].

Biological context of Gnb5

• Protein-protein interactions involving the Gbeta5-RGS7 complex can be studied in cells using fluorescence resonance energy transfer utilizing Gbeta5, RGS, and Galpha subunits fused to the cyan and yellow versions of green fluorescent protein [5].

Anatomical context of Gnb5

• Our findings show that RGS7-Gbeta5 complex is expressed in immunocompetent cells such as resident microglia and peripheral macrophages following spinal cord injury [3].
• Confocal dual immunofluorescence labeling studies indicated a broad regional specificity in the cellular coexpression between RGS7 and Gbeta5 within the cerebral cortical layers I and V-VI, hippocampal formation, caudate-putamen, medial habenula, most thalamic nuclei, and cerebellar molecular and granular layers [4].
• To rule out interference from the adjacent neurons and confirm the presence of RGS7-Gbeta5 complex in inflammatory cells, we performed immunocytochemistry, RT-PCR, Western blot, and immunoprecipitation using microglial (BV2) and peripheral macrophage (RAW) cell lines [3].
• In addition, cDNAs corresponding to the Gbeta5 and Ggamma11 isoforms exhibited restricted expression to inner and outer hair cells, respectively [6].

Associations of Gnb5 with chemical compounds

• This article describes the purification of heterodimers from Sf9 insect cells following the expression of recombinant R7 protein and histidine-tagged Gbeta5 using affinity and ion-exchange chromatography [7].

References