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Gene Review

GPSM1  -  G-protein signaling modulator 1

Homo sapiens

Synonyms: AGS3, Activator of G-protein signaling 3, DKFZP727I051, G-protein-signaling modulator 1
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Disease relevance of GPSM1

  • An AGS3 deletion strain was found to produce faster and more robust disease than the parental strain in an experimental mouse model of aspergillosis [1].
  • By using biochemical and microscopic methods, which allow one to measure the rate of autophagy, the role of two regulators of Gi3 protein activity, activator of G-protein-signaling-3 (AGS3) and Galpha-interacting protein (GAIP), was studied in the control of autophagy in human colon cancer HT-29 cells [2].

High impact information on GPSM1

  • Furthermore, they find that AGS3 is responsible for altered behavior, such as enhanced drug seeking, and altered neurotransmission in cocaine-treated rats, representing a novel therapeutic target [3].
  • In this issue of Neuron, Bowers et al. demonstrate that an activator of G protein signaling (AGS3) is persistently upregulated in the prefrontal cortex after cessation of chronic cocaine treatment [3].
  • Accordingly, expressing its non-Galphai3-interacting NH2-terminal domain or its Galphai3-interacting COOH-terminal domain reversed the stimulatory role of AGS3 on autophagy [4].
  • The G-protein regulator AGS3 controls an early event during macroautophagy in human intestinal HT-29 cells [4].
  • Together with the full-length form, minute amounts of the mRNA encoding a NH2-terminal truncated form of AGS3, previously characterized in cardiac tissues, were also detected [4].

Biological context of GPSM1

  • Both the endogenous form of AGS3 and a tagged expressed form have a localization compatible with a role in the Galphai3-dependent control of autophagy [4].
  • Thus, AGS3 exists as a short and long form, both of which apparently stabilize the GDP-bound conformation of Galpha(i), but which differ in their tissue distribution and trafficking within the cell [5].
  • Transfection of COS-7 cells with AGS3-SHORT cDNAs resulted in the expression of a major immunoreactive AGS3 polypeptide (M(r) approximately 23,000) with a translational start site at Met(495) of AGS3-LONG [5].
  • The G-protein regulatory (GPR) motif in AGS3 was recently identified as a region for protein binding to heterotrimeric G-protein alpha subunits [6].
  • The GPR peptide sequence (28 amino acids) encompassed the consensus sequence defined by the four GPR motifs conserved in the family of AGS3 proteins [6].

Anatomical context of GPSM1

  • In the present work we show that the mRNA encoding for AGS3 is expressed in human intestinal cell lines (Caco-2 and HT-29) whatever their state of differentiation [4].
  • In primary neuronal cultures as well as in dividing cultures of PC12 cells, immunocytochemistry indicated distinct subcellular locations of AGS3 and LGN [7].
  • Asymmetric localization of LGN but not AGS3, two homologs of Drosophila pins, in dividing human neural progenitor cells [8].
  • The apparent hyper-virulence in the AGS3-deleted mutant was correlated with an increased melanin content of the conidial cell wall, a better resistance to reactive oxygen species and a quicker germination rate [1].
  • The intracellular localization of AGS3 (Golgi apparatus and endoplasmic reticulum, two membranes known to be at the origin of autophagosomes) is consistent with its role in autophagy [2].

Associations of GPSM1 with chemical compounds

  • AGS3, a 650-amino acid protein encoded by an approximately 4-kilobase (kb) mRNA enriched in rat brain, is a Galpha(i)/Galpha(t)-binding protein that competes with Gbetagamma for interaction with Galpha(GDP) and acts as a guanine nucleotide dissociation inhibitor for heterotrimeric G-proteins [5].
  • The GPR consensus peptide effectively prevented the binding of AGS3 to Gialpha1,2 in protein interaction assays, inhibited guanosine 5'-O-(3-thiotriphosphate) binding to Gialpha, and stabilized the GDP-bound conformation of Gialpha [6].
  • Chitosan-silicate hybrids were synthesized using gamma-glycidoxypropyltrimethoxysilane (GPSM) as the agent for cross-linking the chitosan chains [9].

Other interactions of GPSM1


Analytical, diagnostic and therapeutic context of GPSM1

  • Immunofluorescence studies and confocal imaging indicated that AGS3 was predominantly cytoplasmic and enriched in microdomains of the cell [10].


  1. AGS3, an alpha(1-3)glucan synthase gene family member of Aspergillus fumigatus, modulates mycelium growth in the lung of experimentally infected mice. Maubon, D., Park, S., Tanguy, M., Huerre, M., Schmitt, C., Prévost, M.C., Perlin, D.S., Latgé, J.P., Beauvais, A. Fungal Genet. Biol. (2006) [Pubmed]
  2. Analyses of Galpha-interacting protein and activator of G-protein-signaling-3 functions in macroautophagy. Pattingre, S., Petiot, A., Codogno, P. Meth. Enzymol. (2004) [Pubmed]
  3. Accessories to addiction: G protein regulators play a key role in cocaine seeking and neuroplasticity. Kelley, A.E., Schiltz, C.A. Neuron (2004) [Pubmed]
  4. The G-protein regulator AGS3 controls an early event during macroautophagy in human intestinal HT-29 cells. Pattingre, S., De Vries, L., Bauvy, C., Chantret, I., Cluzeaud, F., Ogier-Denis, E., Vandewalle, A., Codogno, P. J. Biol. Chem. (2003) [Pubmed]
  5. Identification of a truncated form of the G-protein regulator AGS3 in heart that lacks the tetratricopeptide repeat domains. Pizzinat, N., Takesono, A., Lanier, S.M. J. Biol. Chem. (2001) [Pubmed]
  6. Stabilization of the GDP-bound conformation of Gialpha by a peptide derived from the G-protein regulatory motif of AGS3. Peterson, Y.K., Bernard, M.L., Ma, H., Hazard, S., Graber, S.G., Lanier, S.M. J. Biol. Chem. (2000) [Pubmed]
  7. Expression analysis and subcellular distribution of the two G-protein regulators AGS3 and LGN indicate distinct functionality. Localization of LGN to the midbody during cytokinesis. Blumer, J.B., Chandler, L.J., Lanier, S.M. J. Biol. Chem. (2002) [Pubmed]
  8. Asymmetric localization of LGN but not AGS3, two homologs of Drosophila pins, in dividing human neural progenitor cells. Fuja, T.J., Schwartz, P.H., Darcy, D., Bryant, P.J. J. Neurosci. Res. (2004) [Pubmed]
  9. In vitro cytocompatibility of MG63 cells on chitosan-organosiloxane hybrid membranes. Shirosaki, Y., Tsuru, K., Hayakawa, S., Osaka, A., Lopes, M.A., Santos, J.D., Fernandes, M.H. Biomaterials (2005) [Pubmed]
  10. Selective interaction of AGS3 with G-proteins and the influence of AGS3 on the activation state of G-proteins. Bernard, M.L., Peterson, Y.K., Chung, P., Jourdan, J., Lanier, S.M. J. Biol. Chem. (2001) [Pubmed]
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