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. 1989 Nov;9(11):4807–4811. doi: 10.1128/mcb.9.11.4807

The ras-like protein p25rab3A is partially cytosolic and is expressed only in neural tissue.

E Burstein 1, I G Macara 1
PMCID: PMC363629  PMID: 2513478

Abstract

An antipeptide antiserum has been developed against a sequence near the C terminus of the small guanine nucleotide-binding protein p25rab3A. This protein is the product of one of a large number of genes that show homology to the ras proto-oncogenes. Immunoblotting with the antiserum specifically detected a 25-kilodalton protein in brain membranes. This protein coeluted from a MonoQ high-resolution ion-exchange column with a 25-kilodalton GTP-binding protein at a salt concentration similar to that known to elute purified p25rab3A. Unlike p21ras, which is exclusively membrane bound, p25rab3A is present in both the cytosol and membrane fractions of rat brain. It was not detected in other tissues, although a band of slightly lower molecular weight was observed with skeletal muscle. Western blot (immunoblot) analysis of five regions of the rat brain indicated that p25rab3A is most abundant in the hypothalamus and hippocampus.

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Selected References

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  1. Barbacid M. ras genes. Annu Rev Biochem. 1987;56:779–827. doi: 10.1146/annurev.bi.56.070187.004023. [DOI] [PubMed] [Google Scholar]
  2. Bourne H. R. Do GTPases direct membrane traffic in secretion? Cell. 1988 Jun 3;53(5):669–671. doi: 10.1016/0092-8674(88)90081-5. [DOI] [PubMed] [Google Scholar]
  3. Calés C., Hancock J. F., Marshall C. J., Hall A. The cytoplasmic protein GAP is implicated as the target for regulation by the ras gene product. Nature. 1988 Apr 7;332(6164):548–551. doi: 10.1038/332548a0. [DOI] [PubMed] [Google Scholar]
  4. Casey P. J., Gilman A. G. G protein involvement in receptor-effector coupling. J Biol Chem. 1988 Feb 25;263(6):2577–2580. [PubMed] [Google Scholar]
  5. Chardin P., Tavitian A. The ral gene: a new ras related gene isolated by the use of a synthetic probe. EMBO J. 1986 Sep;5(9):2203–2208. doi: 10.1002/j.1460-2075.1986.tb04485.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Furth M. E., Aldrich T. H., Cordon-Cardo C. Expression of ras proto-oncogene proteins in normal human tissues. Oncogene. 1987 Mar;1(1):47–58. [PubMed] [Google Scholar]
  7. Garrett M. D., Self A. J., van Oers C., Hall A. Identification of distinct cytoplasmic targets for ras/R-ras and rho regulatory proteins. J Biol Chem. 1989 Jan 5;264(1):10–13. [PubMed] [Google Scholar]
  8. Gibbs J. B., Schaber M. D., Allard W. J., Sigal I. S., Scolnick E. M. Purification of ras GTPase activating protein from bovine brain. Proc Natl Acad Sci U S A. 1988 Jul;85(14):5026–5030. doi: 10.1073/pnas.85.14.5026. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hancock J. F., Magee A. I., Childs J. E., Marshall C. J. All ras proteins are polyisoprenylated but only some are palmitoylated. Cell. 1989 Jun 30;57(7):1167–1177. doi: 10.1016/0092-8674(89)90054-8. [DOI] [PubMed] [Google Scholar]
  10. Kikuchi A., Yamashita T., Kawata M., Yamamoto K., Ikeda K., Tanimoto T., Takai Y. Purification and characterization of a novel GTP-binding protein with a molecular weight of 24,000 from bovine brain membranes. J Biol Chem. 1988 Feb 25;263(6):2897–2904. [PubMed] [Google Scholar]
  11. Kitayama H., Sugimoto Y., Matsuzaki T., Ikawa Y., Noda M. A ras-related gene with transformation suppressor activity. Cell. 1989 Jan 13;56(1):77–84. doi: 10.1016/0092-8674(89)90985-9. [DOI] [PubMed] [Google Scholar]
  12. Lerner R. A., Green N., Alexander H., Liu F. T., Sutcliffe J. G., Shinnick T. M. Chemically synthesized peptides predicted from the nucleotide sequence of the hepatitis B virus genome elicit antibodies reactive with the native envelope protein of Dane particles. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3403–3407. doi: 10.1073/pnas.78.6.3403. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Matsui Y., Kikuchi A., Kondo J., Hishida T., Teranishi Y., Takai Y. Nucleotide and deduced amino acid sequences of a GTP-binding protein family with molecular weights of 25,000 from bovine brain. J Biol Chem. 1988 Aug 15;263(23):11071–11074. [PubMed] [Google Scholar]
  14. Molenaar C. M., Prange R., Gallwitz D. A carboxyl-terminal cysteine residue is required for palmitic acid binding and biological activity of the ras-related yeast YPT1 protein. EMBO J. 1988 Apr;7(4):971–976. doi: 10.1002/j.1460-2075.1988.tb02903.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Ohmori T., Kikuchi A., Yamamoto K., Kim S., Takai Y. Small molecular weight GTP-binding proteins in human platelet membranes. Purification and characterization of a novel GTP-binding protein with a molecular weight of 22,000. J Biol Chem. 1989 Jan 25;264(3):1877–1881. [PubMed] [Google Scholar]
  16. Olofsson B., Chardin P., Touchot N., Zahraoui A., Tavitian A. Expression of the ras-related ralA, rho12 and rab genes in adult mouse tissues. Oncogene. 1988 Aug;3(2):231–234. [PubMed] [Google Scholar]
  17. Salminen A., Novick P. J. A ras-like protein is required for a post-Golgi event in yeast secretion. Cell. 1987 May 22;49(4):527–538. doi: 10.1016/0092-8674(87)90455-7. [DOI] [PubMed] [Google Scholar]
  18. Sano K., Kikuchi A., Matsui Y., Teranishi Y., Takai Y. Tissue-specific expression of a novel GTP-binding protein (smg p25A) mRNA and its increase by nerve growth factor and cyclic AMP in rat pheochromocytoma PC-12 cells. Biochem Biophys Res Commun. 1989 Jan 31;158(2):377–385. doi: 10.1016/s0006-291x(89)80058-0. [DOI] [PubMed] [Google Scholar]
  19. Seuwen K., Lagarde A., Pouysségur J. Deregulation of hamster fibroblast proliferation by mutated ras oncogenes is not mediated by constitutive activation of phosphoinositide-specific phospholipase C. EMBO J. 1988 Jan;7(1):161–168. doi: 10.1002/j.1460-2075.1988.tb02796.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Touchot N., Chardin P., Tavitian A. Four additional members of the ras gene superfamily isolated by an oligonucleotide strategy: molecular cloning of YPT-related cDNAs from a rat brain library. Proc Natl Acad Sci U S A. 1987 Dec;84(23):8210–8214. doi: 10.1073/pnas.84.23.8210. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Trahey M., McCormick F. A cytoplasmic protein stimulates normal N-ras p21 GTPase, but does not affect oncogenic mutants. Science. 1987 Oct 23;238(4826):542–545. doi: 10.1126/science.2821624. [DOI] [PubMed] [Google Scholar]
  22. Wakelam M. J., Davies S. A., Houslay M. D., McKay I., Marshall C. J., Hall A. Normal p21N-ras couples bombesin and other growth factor receptors to inositol phosphate production. Nature. 1986 Sep 11;323(6084):173–176. doi: 10.1038/323173a0. [DOI] [PubMed] [Google Scholar]
  23. Wingrove T. G., Watt R., Keng P., Macara I. G. Stabilization of myc proto-oncogene proteins during Friend murine erythroleukemia cell differentiation. J Biol Chem. 1988 Jun 25;263(18):8918–8924. [PubMed] [Google Scholar]
  24. Wolfman A., Macara I. G. Elevated levels of diacylglycerol and decreased phorbol ester sensitivity in ras-transformed fibroblasts. Nature. 1987 Jan 22;325(6102):359–361. doi: 10.1038/325359a0. [DOI] [PubMed] [Google Scholar]
  25. Wolfman A., Moscucci A., Macara I. G. Evidence for multiple, ras-like, guanine nucleotide-binding proteins in Swiss 3T3 plasma membranes. Stimulation of GTPase activity by cytosolic factors. J Biol Chem. 1989 Jun 25;264(18):10820–10827. [PubMed] [Google Scholar]
  26. Yamamoto K., Kim S., Kikuchi A., Takai Y. Multiple small molecular weight GTP-binding proteins in bovine brain cytosol. Purification and characterization of a 24KDa protein. Biochem Biophys Res Commun. 1988 Sep 30;155(3):1284–1292. doi: 10.1016/s0006-291x(88)81280-4. [DOI] [PubMed] [Google Scholar]

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