Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1993 Jan 1;289(Pt 1):17–24. doi: 10.1042/bj2890017

Biology of the Rap proteins, members of the ras superfamily of GTP-binding proteins.

G M Bokoch 1
PMCID: PMC1132124  PMID: 8424755

Full text

PDF
18

Images in this article

20Figure 2
on p.20
20Figure 3
on p.20
21Figure 4
on p.21

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Abo A., Pick E., Hall A., Totty N., Teahan C. G., Segal A. W. Activation of the NADPH oxidase involves the small GTP-binding protein p21rac1. Nature. 1991 Oct 17;353(6345):668–670. doi: 10.1038/353668a0. [DOI] [PubMed] [Google Scholar]
  2. Adari H., Lowy D. R., Willumsen B. M., Der C. J., McCormick F. Guanosine triphosphatase activating protein (GAP) interacts with the p21 ras effector binding domain. Science. 1988 Apr 22;240(4851):518–521. doi: 10.1126/science.2833817. [DOI] [PubMed] [Google Scholar]
  3. Ballester R., Furth M. E., Rosen O. M. Phorbol ester- and protein kinase C-mediated phosphorylation of the cellular Kirsten ras gene product. J Biol Chem. 1987 Feb 25;262(6):2688–2695. [PubMed] [Google Scholar]
  4. Bokoch G. M., Parkos C. A., Mumby S. M. Purification and characterization of the 22,000-dalton GTP-binding protein substrate for ADP-ribosylation by botulinum toxin, G22K. J Biol Chem. 1988 Nov 15;263(32):16744–16749. [PubMed] [Google Scholar]
  5. Bokoch G. M., Prossnitz V. Isoprenoid metabolism is required for stimulation of the respiratory burst oxidase of HL-60 cells. J Clin Invest. 1992 Feb;89(2):402–408. doi: 10.1172/JCI115599. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Bokoch G. M., Quilliam L. A., Bohl B. P., Jesaitis A. J., Quinn M. T. Inhibition of Rap1A binding to cytochrome b558 of NADPH oxidase by phosphorylation of Rap1A. Science. 1991 Dec 20;254(5039):1794–1796. doi: 10.1126/science.1763330. [DOI] [PubMed] [Google Scholar]
  7. Bokoch G. M., Quilliam L. A. Guanine nucleotide binding properties of rap1 purified from human neutrophils. Biochem J. 1990 Apr 15;267(2):407–411. doi: 10.1042/bj2670407. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Bourne H. R., Sanders D. A., McCormick F. The GTPase superfamily: conserved structure and molecular mechanism. Nature. 1991 Jan 10;349(6305):117–127. doi: 10.1038/349117a0. [DOI] [PubMed] [Google Scholar]
  9. Buss J. E., Quilliam L. A., Kato K., Casey P. J., Solski P. A., Wong G., Clark R., McCormick F., Bokoch G. M., Der C. J. The COOH-terminal domain of the Rap1A (Krev-1) protein is isoprenylated and supports transformation by an H-Ras:Rap1A chimeric protein. Mol Cell Biol. 1991 Mar;11(3):1523–1530. doi: 10.1128/mcb.11.3.1523. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Béranger F., Goud B., Tavitian A., de Gunzburg J. Association of the Ras-antagonistic Rap1/Krev-1 proteins with the Golgi complex. Proc Natl Acad Sci U S A. 1991 Mar 1;88(5):1606–1610. doi: 10.1073/pnas.88.5.1606. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Béranger F., Tavitian A., de Gunzburg J. Post-translational processing and subcellular localization of the Ras-related Rap2 protein. Oncogene. 1991 Oct;6(10):1835–1842. [PubMed] [Google Scholar]
  12. Chant J., Herskowitz I. Genetic control of bud site selection in yeast by a set of gene products that constitute a morphogenetic pathway. Cell. 1991 Jun 28;65(7):1203–1212. doi: 10.1016/0092-8674(91)90015-q. [DOI] [PubMed] [Google Scholar]
  13. Clark R. A. The human neutrophil respiratory burst oxidase. J Infect Dis. 1990 Jun;161(6):1140–1147. doi: 10.1093/infdis/161.6.1140. [DOI] [PubMed] [Google Scholar]
  14. Cox A. D., Hisaka M. M., Buss J. E., Der C. J. Specific isoprenoid modification is required for function of normal, but not oncogenic, Ras protein. Mol Cell Biol. 1992 Jun;12(6):2606–2615. doi: 10.1128/mcb.12.6.2606. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Culine S., Olofsson B., Gosselin S., Honore N., Tavitian A. Expression of the ras-related rap genes in human tumors. Int J Cancer. 1989 Dec 15;44(6):990–994. doi: 10.1002/ijc.2910440608. [DOI] [PubMed] [Google Scholar]
  16. Curnutte J. T. Molecular basis of the autosomal recessive forms of chronic granulomatous disease. Immunodefic Rev. 1992;3(2):149–172. [PubMed] [Google Scholar]
  17. Didsbury J., Weber R. F., Bokoch G. M., Evans T., Snyderman R. rac, a novel ras-related family of proteins that are botulinum toxin substrates. J Biol Chem. 1989 Oct 5;264(28):16378–16382. [PubMed] [Google Scholar]
  18. Dumont J. E., Jauniaux J. C., Roger P. P. The cyclic AMP-mediated stimulation of cell proliferation. Trends Biochem Sci. 1989 Feb;14(2):67–71. doi: 10.1016/0968-0004(89)90046-7. [DOI] [PubMed] [Google Scholar]
  19. Eklund E. A., Marshall M., Gibbs J. B., Crean C. D., Gabig T. G. Resolution of a low molecular weight G protein in neutrophil cytosol required for NADPH oxidase activation and reconstitution by recombinant Krev-1 protein. J Biol Chem. 1991 Jul 25;266(21):13964–13970. [PubMed] [Google Scholar]
  20. Farrell F., Torti M., Lapetina E. G. Rap proteins: investigating their role in cell function. J Lab Clin Med. 1992 Oct;120(4):533–537. [PubMed] [Google Scholar]
  21. Fischer T. H., Gatling M. N., Lacal J. C., White G. C., 2nd rap1B, a cAMP-dependent protein kinase substrate, associates with the platelet cytoskeleton. J Biol Chem. 1990 Nov 15;265(32):19405–19408. [PubMed] [Google Scholar]
  22. Frech M., John J., Pizon V., Chardin P., Tavitian A., Clark R., McCormick F., Wittinghofer A. Inhibition of GTPase activating protein stimulation of Ras-p21 GTPase by the Krev-1 gene product. Science. 1990 Jul 13;249(4965):169–171. doi: 10.1126/science.2164710. [DOI] [PubMed] [Google Scholar]
  23. Grand R. J., Owen D. The biochemistry of ras p21. Biochem J. 1991 Nov 1;279(Pt 3):609–631. doi: 10.1042/bj2790609. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Hall A. Signal transduction through small GTPases--a tale of two GAPs. Cell. 1992 May 1;69(3):389–391. doi: 10.1016/0092-8674(92)90441-e. [DOI] [PubMed] [Google Scholar]
  25. Hall A. The cellular functions of small GTP-binding proteins. Science. 1990 Aug 10;249(4969):635–640. doi: 10.1126/science.2116664. [DOI] [PubMed] [Google Scholar]
  26. Hata Y., Kaibuchi K., Kawamura S., Hiroyoshi M., Shirataki H., Takai Y. Enhancement of the actions of smg p21 GDP/GTP exchange protein by the protein kinase A-catalyzed phosphorylation of smg p21. J Biol Chem. 1991 Apr 5;266(10):6571–6577. [PubMed] [Google Scholar]
  27. Hata Y., Kikuchi A., Sasaki T., Schaber M. D., Gibbs J. B., Takai Y. Inhibition of the ras p21 GTPase-activating protein-stimulated GTPase activity of c-Ha-ras p21 by smg p21 having the same putative effector domain as ras p21s. J Biol Chem. 1990 May 5;265(13):7104–7107. [PubMed] [Google Scholar]
  28. Heyworth P. G., Curnutte J. T., Nauseef W. M., Volpp B. D., Pearson D. W., Rosen H., Clark R. A. Neutrophil nicotinamide adenine dinucleotide phosphate oxidase assembly. Translocation of p47-phox and p67-phox requires interaction between p47-phox and cytochrome b558. J Clin Invest. 1991 Jan;87(1):352–356. doi: 10.1172/JCI114993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Hiroyoshi M., Kaibuchi K., Kawamura S., Hata Y., Takai Y. Role of the C-terminal region of smg p21, a ras p21-like small GTP-binding protein, in membrane and smg p21 GDP/GTP exchange protein interactions. J Biol Chem. 1991 Feb 15;266(5):2962–2969. [PubMed] [Google Scholar]
  30. Hong H. J., Hsu L. C., Gould M. N. Molecular cloning of rat Krev-1 cDNA and analysis of the mRNA levels in normal and NMU-induced mammary carcinomas. Carcinogenesis. 1990 Jul;11(7):1245–1247. doi: 10.1093/carcin/11.7.1245. [DOI] [PubMed] [Google Scholar]
  31. Hoshijima M., Kikuchi A., Kawata M., Ohmori T., Hashimoto E., Yamamura H., Takai Y. Phosphorylation by cyclic AMP-dependent protein kinase of a human platelet Mr 22,000 GTP-binding protein (smg p21) having the same putative effector domain as the ras gene products. Biochem Biophys Res Commun. 1988 Dec 30;157(3):851–860. doi: 10.1016/s0006-291x(88)80953-7. [DOI] [PubMed] [Google Scholar]
  32. Hsu L. C., Gould M. N. Molecular cloning of Copenhagen rat Krev-1 and rap1B cDNAs and study of their association with mammary tumor resistance in the Copenhagen rat. Carcinogenesis. 1991 Mar;12(3):533–536. doi: 10.1093/carcin/12.3.533. [DOI] [PubMed] [Google Scholar]
  33. Huzoor-Akbar, Winegar D. A., Lapetina E. G. Carboxyl methylation of platelet rap1 proteins is stimulated by guanosine 5'-(3-O-thio)triphosphate. J Biol Chem. 1991 Mar 5;266(7):4387–4391. [PubMed] [Google Scholar]
  34. Itoh T., Kaibuchi K., Sasaki T., Takai Y. The smg GDS-induced activation of smg p21 is initiated by cyclic AMP-dependent protein kinase-catalyzed phosphorylation of smg p21. Biochem Biophys Res Commun. 1991 Jun 28;177(3):1319–1324. doi: 10.1016/0006-291x(91)90685-z. [DOI] [PubMed] [Google Scholar]
  35. Jimenez B., Pizon V., Lerosey I., Béranger F., Tavitian A., de Gunzburg J. Effects of the ras-related rap2 protein on cellular proliferation. Int J Cancer. 1991 Sep 30;49(3):471–479. doi: 10.1002/ijc.2910490327. [DOI] [PubMed] [Google Scholar]
  36. Kahn R. A., Der C. J., Bokoch G. M. The ras superfamily of GTP-binding proteins: guidelines on nomenclature. FASEB J. 1992 May;6(8):2512–2513. doi: 10.1096/fasebj.6.8.1592203. [DOI] [PubMed] [Google Scholar]
  37. Kaibuchi K., Mizuno T., Fujioka H., Yamamoto T., Kishi K., Fukumoto Y., Hori Y., Takai Y. Molecular cloning of the cDNA for stimulatory GDP/GTP exchange protein for smg p21s (ras p21-like small GTP-binding proteins) and characterization of stimulatory GDP/GTP exchange protein. Mol Cell Biol. 1991 May;11(5):2873–2880. doi: 10.1128/mcb.11.5.2873. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Kawamura S., Kaibuchi K., Hiroyoshi M., Fujioka H., Mizuno T., Takai Y. Inhibition of the action of a stimulatory GDP/GTP exchange protein for smg p21 by acidic membrane phospholipids. Jpn J Cancer Res. 1991 Jul;82(7):758–761. doi: 10.1111/j.1349-7006.1991.tb02699.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Kawamura S., Kaibuchi K., Hiroyoshi M., Hata Y., Takai Y. Stoichiometric interaction of smg p21 with its GDP/GTP exchange protein and its novel action to regulate the translocation of smg p21 between membrane and cytoplasm. Biochem Biophys Res Commun. 1991 Feb 14;174(3):1095–1102. doi: 10.1016/0006-291x(91)91533-i. [DOI] [PubMed] [Google Scholar]
  40. Kawata M., Farnsworth C. C., Yoshida Y., Gelb M. H., Glomset J. A., Takai Y. Posttranslationally processed structure of the human platelet protein smg p21B: evidence for geranylgeranylation and carboxyl methylation of the C-terminal cysteine. Proc Natl Acad Sci U S A. 1990 Nov;87(22):8960–8964. doi: 10.1073/pnas.87.22.8960. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Kawata M., Kawahara Y., Araki S., Sunako M., Tsuda T., Fukuzaki H., Mizoguchi A., Takai Y. Identification of a major GTP-binding protein in bovine aortic smooth muscle membranes as smg p21, a GTP-binding protein having the same effector domain as ras p21s. Biochem Biophys Res Commun. 1989 Sep 29;163(3):1418–1427. doi: 10.1016/0006-291x(89)91137-6. [DOI] [PubMed] [Google Scholar]
  42. Kawata M., Kikuchi A., Hoshijima M., Yamamoto K., Hashimoto E., Yamamura H., Takai Y. Phosphorylation of smg p21, a ras p21-like GTP-binding protein, by cyclic AMP-dependent protein kinase in a cell-free system and in response to prostaglandin E1 in intact human platelets. J Biol Chem. 1989 Sep 15;264(26):15688–15695. [PubMed] [Google Scholar]
  43. Kawata M., Matsui Y., Kondo J., Hishida T., Teranishi Y., Takai Y. A novel small molecular weight GTP-binding protein with the same putative effector domain as the ras proteins in bovine brain membranes. Purification, determination of primary structure, and characterization. J Biol Chem. 1988 Dec 15;263(35):18965–18971. [PubMed] [Google Scholar]
  44. Kemp B. E., Pearson R. B. Protein kinase recognition sequence motifs. Trends Biochem Sci. 1990 Sep;15(9):342–346. doi: 10.1016/0968-0004(90)90073-k. [DOI] [PubMed] [Google Scholar]
  45. Kim S., Mizoguchi A., Kikuchi A., Takai Y. Tissue and subcellular distributions of the smg-21/rap1/Krev-1 proteins which are partly distinct from those of c-ras p21s. Mol Cell Biol. 1990 Jun;10(6):2645–2652. doi: 10.1128/mcb.10.6.2645. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Kitayama H., Matsuzaki T., Ikawa Y., Noda M. A domain responsible for the transformation suppressor activity in Krev-1 protein. Jpn J Cancer Res. 1990 May;81(5):445–448. doi: 10.1111/j.1349-7006.1990.tb02589.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Kitayama H., Matsuzaki T., Ikawa Y., Noda M. Genetic analysis of the Kirsten-ras-revertant 1 gene: potentiation of its tumor suppressor activity by specific point mutations. Proc Natl Acad Sci U S A. 1990 Jun;87(11):4284–4288. doi: 10.1073/pnas.87.11.4284. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. 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]
  49. Knaus U. G., Heyworth P. G., Evans T., Curnutte J. T., Bokoch G. M. Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac 2. Science. 1991 Dec 6;254(5037):1512–1515. doi: 10.1126/science.1660188. [DOI] [PubMed] [Google Scholar]
  50. Kyprianou N., Taylor-Papadimitriou J. Isolation of azatyrosine-induced revertants from ras-transformed human mammary epithelial cells. Oncogene. 1992 Jan;7(1):57–63. [PubMed] [Google Scholar]
  51. Lapetina E. G., Lacal J. C., Reep B. R., Molina y Vedia L. A ras-related protein is phosphorylated and translocated by agonists that increase cAMP levels in human platelets. Proc Natl Acad Sci U S A. 1989 May;86(9):3131–3134. doi: 10.1073/pnas.86.9.3131. [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Lazarowski E. R., Winegar D. A., Nolan R. D., Oberdisse E., Lapetina E. G. Effect of protein kinase A on inositide metabolism and rap 1 G-protein in human erythroleukemia cells. J Biol Chem. 1990 Aug 5;265(22):13118–13123. [PubMed] [Google Scholar]
  53. Lerosey I., Pizon V., Tavitian A., de Gunzburg J. The cAMP-dependent protein kinase phosphorylates the rap1 protein in vitro as well as in intact fibroblasts, but not the closely related rap2 protein. Biochem Biophys Res Commun. 1991 Mar 15;175(2):430–436. doi: 10.1016/0006-291x(91)91582-w. [DOI] [PubMed] [Google Scholar]
  54. Maltese W. A. Posttranslational modification of proteins by isoprenoids in mammalian cells. FASEB J. 1990 Dec;4(15):3319–3328. doi: 10.1096/fasebj.4.15.2123808. [DOI] [PubMed] [Google Scholar]
  55. Maridonneau-Parini I., de Gunzburg J. Association of rap1 and rap2 proteins with the specific granules of human neutrophils. Translocation to the plasma membrane during cell activation. J Biol Chem. 1992 Mar 25;267(9):6396–6402. [PubMed] [Google Scholar]
  56. Marshall M. S., Davis L. J., Keys R. D., Mosser S. D., Hill W. S., Scolnick E. M., Gibbs J. B. Identification of amino acid residues required for Ras p21 target activation. Mol Cell Biol. 1991 Aug;11(8):3997–4004. doi: 10.1128/mcb.11.8.3997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  57. Marti K. B., Lapetina E. G. Epinephrine suppresses rap1B.GAP-activated GTPase activity in human platelets. Proc Natl Acad Sci U S A. 1992 Apr 1;89(7):2784–2788. doi: 10.1073/pnas.89.7.2784. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Marx J. New genes may shed light on cell growth control. Science. 1992 Jul 24;257(5069):484–485. doi: 10.1126/science.1636083. [DOI] [PubMed] [Google Scholar]
  59. Miura Y., Kaibuchi K., Itoh T., Corbin J. D., Francis S. H., Takai Y. Phosphorylation of smg p21B/rap1B p21 by cyclic GMP-dependent protein kinase. FEBS Lett. 1992 Feb 3;297(1-2):171–174. doi: 10.1016/0014-5793(92)80353-i. [DOI] [PubMed] [Google Scholar]
  60. Mizuno T., Kaibuchi K., Ando S., Musha T., Hiraoka K., Takaishi K., Asada M., Nunoi H., Matsuda I., Takai Y. Regulation of the superoxide-generating NADPH oxidase by a small GTP-binding protein and its stimulatory and inhibitory GDP/GTP exchange proteins. J Biol Chem. 1992 May 25;267(15):10215–10218. [PubMed] [Google Scholar]
  61. Mizuno T., Kaibuchi K., Yamamoto T., Kawamura M., Sakoda T., Fujioka H., Matsuura Y., Takai Y. A stimulatory GDP/GTP exchange protein for smg p21 is active on the post-translationally processed form of c-Ki-ras p21 and rhoA p21. Proc Natl Acad Sci U S A. 1991 Aug 1;88(15):6442–6446. doi: 10.1073/pnas.88.15.6442. [DOI] [PMC free article] [PubMed] [Google Scholar]
  62. Moores S. L., Schaber M. D., Mosser S. D., Rands E., O'Hara M. B., Garsky V. M., Marshall M. S., Pompliano D. L., Gibbs J. B. Sequence dependence of protein isoprenylation. J Biol Chem. 1991 Aug 5;266(22):14603–14610. [PubMed] [Google Scholar]
  63. Mueller H., Motulsky H. J., Sklar L. A. The potency and kinetics of the beta-adrenergic receptors on human neutrophils. Mol Pharmacol. 1988 Sep;34(3):347–353. [PubMed] [Google Scholar]
  64. Nauseef W. M., Volpp B. D., McCormick S., Leidal K. G., Clark R. A. Assembly of the neutrophil respiratory burst oxidase. Protein kinase C promotes cytoskeletal and membrane association of cytosolic oxidase components. J Biol Chem. 1991 Mar 25;266(9):5911–5917. [PubMed] [Google Scholar]
  65. Nice E. C., Fabri L., Hammacher A., Holden J., Simpson R. J., Burgess A. W. The purification of a Rap1 GTPase-activating protein from bovine brain cytosol. J Biol Chem. 1992 Jan 25;267(3):1546–1553. [PubMed] [Google Scholar]
  66. Nur-E-Kamal M. S., Sizeland A., D'Abaco G., Maruta H. Asparagine 26, glutamic acid 31, valine 45, and tyrosine 64 of Ras proteins are required for their oncogenicity. J Biol Chem. 1992 Jan 25;267(3):1415–1418. [PubMed] [Google Scholar]
  67. 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]
  68. Ohmstede C. A., Farrell F. X., Reep B. R., Clemetson K. J., Lapetina E. G. RAP2B: a RAS-related GTP-binding protein from platelets. Proc Natl Acad Sci U S A. 1990 Sep;87(17):6527–6531. doi: 10.1073/pnas.87.17.6527. [DOI] [PMC free article] [PubMed] [Google Scholar]
  69. Peveri P., Heyworth P. G., Curnutte J. T. Absolute requirement for GTP in activation of human neutrophil NADPH oxidase in a cell-free system: role of ATP in regenerating GTP. Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2494–2498. doi: 10.1073/pnas.89.6.2494. [DOI] [PMC free article] [PubMed] [Google Scholar]
  70. Pizon V., Chardin P., Lerosey I., Olofsson B., Tavitian A. Human cDNAs rap1 and rap2 homologous to the Drosophila gene Dras3 encode proteins closely related to ras in the 'effector' region. Oncogene. 1988 Aug;3(2):201–204. [PubMed] [Google Scholar]
  71. Pizon V., Lerosey I., Chardin P., Tavitian A. Nucleotide sequence of a human cDNA encoding a ras-related protein (rap1B). Nucleic Acids Res. 1988 Aug 11;16(15):7719–7719. doi: 10.1093/nar/16.15.7719. [DOI] [PMC free article] [PubMed] [Google Scholar]
  72. Polakis P. G., Rubinfeld B., Evans T., McCormick F. Purification of a plasma membrane-associated GTPase-activating protein specific for rap1/Krev-1 from HL60 cells. Proc Natl Acad Sci U S A. 1991 Jan 1;88(1):239–243. doi: 10.1073/pnas.88.1.239. [DOI] [PMC free article] [PubMed] [Google Scholar]
  73. Polakis P., Rubinfeld B., McCormick F. Phosphorylation of rap1GAP in vivo and by cAMP-dependent kinase and the cell cycle p34cdc2 kinase in vitro. J Biol Chem. 1992 May 25;267(15):10780–10785. [PubMed] [Google Scholar]
  74. Quilliam L. A., Der C. J., Clark R., O'Rourke E. C., Zhang K., McCormick F., Bokoch G. M. Biochemical characterization of baculovirus-expressed rap1A/Krev-1 and its regulation by GTPase-activating proteins. Mol Cell Biol. 1990 Jun;10(6):2901–2908. doi: 10.1128/mcb.10.6.2901. [DOI] [PMC free article] [PubMed] [Google Scholar]
  75. Quilliam L. A., Mueller H., Bohl B. P., Prossnitz V., Sklar L. A., Der C. J., Bokoch G. M. Rap1A is a substrate for cyclic AMP-dependent protein kinase in human neutrophils. J Immunol. 1991 Sep 1;147(5):1628–1635. [PubMed] [Google Scholar]
  76. Quinn M. T., Curnutte J. T., Parkos C. A., Mullen M. L., Scott P. J., Erickson R. W., Jesaitis A. J. Reconstitution of defective respiratory burst activity with partially purified human neutrophil cytochrome B in two genetic forms of chronic granulomatous disease: possible role of Rap1A. Blood. 1992 May 1;79(9):2438–2445. [PubMed] [Google Scholar]
  77. Quinn M. T., Mullen M. L., Jesaitis A. J., Linner J. G. Subcellular distribution of the Rap1A protein in human neutrophils: colocalization and cotranslocation with cytochrome b559. Blood. 1992 Mar 15;79(6):1563–1573. [PubMed] [Google Scholar]
  78. Quinn M. T., Parkos C. A., Walker L., Orkin S. H., Dinauer M. C., Jesaitis A. J. Association of a Ras-related protein with cytochrome b of human neutrophils. Nature. 1989 Nov 9;342(6246):198–200. doi: 10.1038/342198a0. [DOI] [PubMed] [Google Scholar]
  79. Rivkin I., Rosenblatt J., Becker E. L. The role of cyclic AMP in the chemotactic responsiveness and spontaneous motility of rabbit peritoneal neutrophils. The inhibition of neutrophil movement and the elevation of cyclic AMP levels by catecholamines, prostaglandins, theophylline and cholera toxin. J Immunol. 1975 Oct;115(4):1126–1134. [PubMed] [Google Scholar]
  80. Rousseau-Merck M. F., Pizon V., Tavitian A., Berger R. Chromosome mapping of the human RAS-related RAP1A, RAP1B, and RAP2 genes to chromosomes 1p12----p13, 12q14, and 13q34, respectively. Cytogenet Cell Genet. 1990;53(1):2–4. doi: 10.1159/000132883. [DOI] [PubMed] [Google Scholar]
  81. Rubinfeld B., Munemitsu S., Clark R., Conroy L., Watt K., Crosier W. J., McCormick F., Polakis P. Molecular cloning of a GTPase activating protein specific for the Krev-1 protein p21rap1. Cell. 1991 Jun 14;65(6):1033–1042. doi: 10.1016/0092-8674(91)90555-d. [DOI] [PubMed] [Google Scholar]
  82. Ruggieri R., Bender A., Matsui Y., Powers S., Takai Y., Pringle J. R., Matsumoto K. RSR1, a ras-like gene homologous to Krev-1 (smg21A/rap1A): role in the development of cell polarity and interactions with the Ras pathway in Saccharomyces cerevisiae. Mol Cell Biol. 1992 Feb;12(2):758–766. doi: 10.1128/mcb.12.2.758. [DOI] [PMC free article] [PubMed] [Google Scholar]
  83. Sahyoun N., McDonald O. B., Farrell F., Lapetina E. G. Phosphorylation of a Ras-related GTP-binding protein, Rap-1b, by a neuronal Ca2+/calmodulin-dependent protein kinase, CaM kinase Gr. Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2643–2647. doi: 10.1073/pnas.88.7.2643. [DOI] [PMC free article] [PubMed] [Google Scholar]
  84. Schejter E. D., Shilo B. Z. Characterization of functional domains of p21 ras by use of chimeric genes. EMBO J. 1985 Feb;4(2):407–412. doi: 10.1002/j.1460-2075.1985.tb03643.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  85. Sha'afi R. I., Molski T. F. Activation of the neutrophil. Prog Allergy. 1988;42:1–64. doi: 10.1159/000318681. [DOI] [PubMed] [Google Scholar]
  86. Shinjo K., Koland J. G., Hart M. J., Narasimhan V., Johnson D. I., Evans T., Cerione R. A. Molecular cloning of the gene for the human placental GTP-binding protein Gp (G25K): identification of this GTP-binding protein as the human homolog of the yeast cell-division-cycle protein CDC42. Proc Natl Acad Sci U S A. 1990 Dec;87(24):9853–9857. doi: 10.1073/pnas.87.24.9853. [DOI] [PMC free article] [PubMed] [Google Scholar]
  87. Shirataki H., Kaibuchi K., Hiroyoshi M., Isomura M., Araki S., Sasaki T., Takai Y. Inhibition of the action of the stimulatory GDP/GTP exchange protein for smg p21 by the geranylgeranylated synthetic peptides designed from its C-terminal region. J Biol Chem. 1991 Nov 5;266(31):20672–20677. [PubMed] [Google Scholar]
  88. Siess W., Winegar D. A., Lapetina E. G. Rap1-B is phosphorylated by protein kinase A in intact human platelets. Biochem Biophys Res Commun. 1990 Jul 31;170(2):944–950. doi: 10.1016/0006-291x(90)92182-y. [DOI] [PubMed] [Google Scholar]
  89. Ueda T., Kikuchi A., Ohga N., Yamamoto J., Takai Y. GTPase activating proteins for the smg-21 GTP-binding protein having the same effector domain as the ras proteins in human platelets. Biochem Biophys Res Commun. 1989 Mar 31;159(3):1411–1419. doi: 10.1016/0006-291x(89)92267-5. [DOI] [PubMed] [Google Scholar]
  90. Uhlinger D. J., Burnham D. N., Lambeth J. D. Nucleoside triphosphate requirements for superoxide generation and phosphorylation in a cell-free system from human neutrophils. Sodium dodecyl sulfate and diacylglycerol activate independently of protein kinase C. J Biol Chem. 1991 Nov 5;266(31):20990–20997. [PubMed] [Google Scholar]
  91. Valencia A., Chardin P., Wittinghofer A., Sander C. The ras protein family: evolutionary tree and role of conserved amino acids. Biochemistry. 1991 May 14;30(19):4637–4648. doi: 10.1021/bi00233a001. [DOI] [PubMed] [Google Scholar]
  92. Vallar L., Spada A., Giannattasio G. Altered Gs and adenylate cyclase activity in human GH-secreting pituitary adenomas. Nature. 1987 Dec 10;330(6148):566–568. doi: 10.1038/330566a0. [DOI] [PubMed] [Google Scholar]
  93. Winegar D. A., Molina y Vedia L., Lapetina E. G. Isoprenylation of rap2 proteins in platelets and human erythroleukemia cells. J Biol Chem. 1991 Mar 5;266(7):4381–4386. [PubMed] [Google Scholar]
  94. Xu H. P., Wang Y., Riggs M., Rodgers L., Wigler M. Biological activity of the mammalian RAP genes in yeast. Cell Regul. 1990 Sep;1(10):763–769. doi: 10.1091/mbc.1.10.763. [DOI] [PMC free article] [PubMed] [Google Scholar]
  95. Yamamoto T., Kaibuchi K., Mizuno T., Hiroyoshi M., Shirataki H., Takai Y. Purification and characterization from bovine brain cytosol of proteins that regulate the GDP/GTP exchange reaction of smg p21s, ras p21-like GTP-binding proteins. J Biol Chem. 1990 Sep 25;265(27):16626–16634. [PubMed] [Google Scholar]
  96. Yatani A., Okabe K., Polakis P., Halenbeck R., McCormick F., Brown A. M. ras p21 and GAP inhibit coupling of muscarinic receptors to atrial K+ channels. Cell. 1990 Jun 1;61(5):769–776. doi: 10.1016/0092-8674(90)90187-j. [DOI] [PubMed] [Google Scholar]
  97. Young J., Searle J., Stitz R., Cowen A., Ward M., Chenevix-French G. Loss of heterozygosity at the human RAP1A/Krev-1 locus is a rare event in colorectal tumors. Cancer Res. 1992 Jan 15;52(2):285–289. [PubMed] [Google Scholar]
  98. Zhang K., Noda M., Vass W. C., Papageorge A. G., Lowy D. R. Identification of small clusters of divergent amino acids that mediate the opposing effects of ras and Krev-1. Science. 1990 Jul 13;249(4965):162–165. doi: 10.1126/science.2115210. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES