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Gene Review:

ARHGEF12 - Rho guanine nucleotide exchange factor...

Bos taurus

Jedlicka, P. et al., Luo, H.R. et al., Higashibata, A. et al., Pagano, A. et al., Franco, M. et al., et al.

Higashibata, Imamizo-Sato, Seki, Yamazaki, Ishioka,

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High impact information on LARG

We now report the identification, cloning, and characterization of a novel protein, GRAB (guanine nucleotide exchange factor for Rab3A), which interacts with both InsP6K1 and Rab3A, a Ras-like GTPase that regulates synaptic vesicle exocytosis [1].
Vesicle formation was stimulated by supplemented clathrin, but inhibited by brefeldin A, consistent with the involvement of ARF1 and a brefeldin-sensitive guanine nucleotide exchange factor [2].
Identification of a plasma membrane-associated guanine nucleotide exchange factor for ARF6 in chromaffin cells. Possible role in the regulated exocytotic pathway [3].
This acceleration is totally abolished by brefeldin A (IC50 = 2 microM) and by trypsin treatment of the retinal extract, as expected for an ARF-specific guanine nucleotide exchange factor [4].
In response to mitogen, levels of both eukaryotic initiation factor (eIF)-2 and guanine nucleotide exchange factor, GEF, increase in parallel with ribosomes which is consistent with a general increase in the translational machinery but cannot explain the increase in activity per ribosome [5].

Biological context of LARG

Furthermore, the full-length cDNA of bovine LARG, a member of the Rho guanine nucleotide exchange factor (GEF) family, was identified, and its gene expression was observed to be downregulated under clinorotation [6].

References

GRAB: a physiologic guanine nucleotide exchange factor for Rab3A, which interacts with inositol hexakisphosphate kinase. Luo, H.R., Saiardi, A., Nagata, E., Ye, K., Yu, H., Jung, T.S., Luo, X., Jain, S., Sawa, A., Snyder, S.H. Neuron (2001) [Pubmed]
In vitro formation of recycling vesicles from endosomes requires adaptor protein-1/clathrin and is regulated by rab4 and the connector rabaptin-5. Pagano, A., Crottet, P., Prescianotto-Baschong, C., Spiess, M. Mol. Biol. Cell (2004) [Pubmed]
Identification of a plasma membrane-associated guanine nucleotide exchange factor for ARF6 in chromaffin cells. Possible role in the regulated exocytotic pathway. Caumont, A.S., Vitale, N., Gensse, M., Galas, M.C., Casanova, J.E., Bader, M.F. J. Biol. Chem. (2000) [Pubmed]
Myristoylation-facilitated binding of the G protein ARF1GDP to membrane phospholipids is required for its activation by a soluble nucleotide exchange factor. Franco, M., Chardin, P., Chabre, M., Paris, S. J. Biol. Chem. (1996) [Pubmed]
Mechanism of activation of protein synthesis initiation in mitogen-stimulated T lymphocytes. Jedlicka, P., Panniers, R. J. Biol. Chem. (1991) [Pubmed]
Influence of simulated microgravity on the activation of the small GTPase Rho involved in cytoskeletal formation--molecular cloning and sequencing of bovine leukemia-associated guanine nucleotide exchange factor. Higashibata, A., Imamizo-Sato, M., Seki, M., Yamazaki, T., Ishioka, N. BMC Biochem. (2006) [Pubmed]

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