CoChat
Sign Up
Cited by 218

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Purification and characterization from bovine brain cytosol of a novel regulatory protein inhibiting the dissociation of GDP from and the subsequent binding of GTP to rhoB p20, a ras p21-like GTP-binding protein.

Ueda, T, Kikuchi, A, Ohga, N, Yamamoto, J, Takai, Y·1990·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(19)38859-3
Open this paper in CoChat — free account

Abstract

A novel regulatory protein for the rho proteins (rhoA p21 and rhoB p20), belonging to a ras p21/ras p21-like small molecular weight (Mr) GTP-binding protein (G protein) superfamily, was purified to near homogeneity from bovine brain cytosol and characterized. This regulatory protein, designated here as GDP dissociation inhibitor (GDI) for the rho proteins (rho GDI), inhibited the dissociation of GDP from rhoB p20 and the binding of guanosine 5'-(3-O-thio)triphosphate (GTP gamma S) to the GDP-bound form of rhoB p20 but not of that to the guanine nucleotide-free form. The Mr value of rho GDI was estimated to be about 27,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and from the S value, indicating that rho GDI is composed of a single polypeptide without a subunit structure. The isoelectric point was about pH 5.7. rho GDI made a complex with the GDP-bound form of rhoB p20 with a molar ratio of 1:1 but not with the GTP gamma S-bound or guanine nucleotide-free form. rho GDI did not stimulate the GTPase activity of rhoB p20 and by itself showed neither GTP gamma S-binding nor GTPase activity. rho GDI was equally active for rhoA p21 and rhoB p20 but was inactive for other ras p21/ras p21-like G proteins including c-Ha-ras p21, smg p25A, and smg p21. rho GDI activity was detected in the cytosol fraction of various rat tissues. These results indicate that, in mammalian tissues, there is a novel type of regulatory protein specific for the rho proteins that interacts…

Overview

Integrity signals

Registry

Crossref · 10.1016/s0021-9258(19)38859-3

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

Cites

Show all 1 references

Research works printed but not linked: 53

  1. Barbacid, 1987, Annu. Rev. Biochem., 56, 779, 10.1146/annurev.bi.56.070187.004023 · DOI · Paper page
  2. Takai, 1988, 2, 995
  3. Madaule, 1985, Cell, 41, 31, 10.1016/0092-8674(85)90058-3 · DOI
  4. Yeramian, 1987, Nucleic Acids Res., 15, 1869, 10.1093/nar/15.4.1869 · DOI
  5. Chardin, 1988, Nucleic Acids Res., 16, 2717, 10.1093/nar/16.6.2717 · DOI
  6. Madaule, 1987, Proc. Natl. Acad. Sci. U. S. A., 84, 779, 10.1073/pnas.84.3.779 · DOI
  7. Yamamoto, 1988, J. Biol. Chem., 263, 9926, 10.1016/S0021-9258(19)81606-X · DOI
  8. Hoshijima, 1989, Mol. Brain Res., 7, 9, 10.1016/0169-328X(90)90067-N · DOI
  9. Kim, 1989, Mol. Brain Res., 6, 167, 10.1016/0169-328X(89)90051-X · DOI
  10. Narumiya, 1988, J. Biol. Chem., 263, 17255, 10.1016/S0021-9258(19)77828-4 · DOI
  11. Braun, 1989, FEBS Lett., 243, 70, 10.1016/0014-5793(89)81220-7 · DOI
  12. Avraham, 1989, Mol. Cell. Biol., 9, 2058
  13. Kikuchi, 1988, J. Biol. Chem., 263, 16303, 10.1016/S0021-9258(18)37593-8 · DOI
  14. Chardin, 1989, EMBO J., 8, 1087, 10.1002/j.1460-2075.1989.tb03477.x · DOI
  15. Adam-Vizi, 1988, FEBS Lett., 238, 277, 10.1016/0014-5793(88)80496-4 · DOI
  16. Rubin, 1988, Mol. Cell. Biol., 8, 418
  17. Kuroda, 1989, Biochem. Biophys. Res. Commun., 163, 674, 10.1016/0006-291X(89)92276-6 · DOI
  18. Hoshino, 1987, J. Biochem. (Tokyo), 102, 503, 10.1093/oxfordjournals.jbchem.a122082 · DOI
  19. Hall, 1986, J. Biol. Chem., 261, 10963, 10.1016/S0021-9258(18)67333-8 · DOI
  20. Shoji, 1989, Biochem. Biophys. Res. Commun., 162, 273, 10.1016/0006-291X(89)91992-X · DOI
  21. Ui, 1984, Trends Pharmacol. Sci., 5, 277, 10.1016/0165-6147(84)90444-9 · DOI
  22. Stryer, 1986, Annu. Rev. Neurosci., 9, 87, 10.1146/annurev.ne.09.030186.000511 · DOI
  23. Bourne, 1986, Nature, 321, 814, 10.1038/321814a0 · DOI
  24. Gillman, 1987, Annu. Rev. Biochem., 56, 615, 10.1146/annurev.bi.56.070187.003151 · DOI
  25. Siekierka, 1982, Proc. Natl. Acad. Sci. U. S. A., 79, 2537, 10.1073/pnas.79.8.2537 · DOI
  26. Kaziro, 1978, Biochim. Biophys. Acta, 505, 95, 10.1016/0304-4173(78)90009-5 · DOI
  27. Pain, 1986, Biochem. J., 235, 625, 10.1042/bj2350625 · DOI
  28. Ohga, 1989, Biochem. Biophys. Res. Commun., 163, 1523, 10.1016/0006-291X(89)91153-4 · DOI
  29. Zahraoui, 1988, Nucleic Acids Res., 16, 1204, 10.1093/nar/16.3.1204 · DOI
  30. Kikuchi, 1988, J. Biol. Chem., 263, 2897, 10.1016/S0021-9258(18)69153-7 · DOI
  31. Matsui, 1988, J. Biol. Chem., 263, 11071, 10.1016/S0021-9258(18)37922-5 · DOI
  32. Sasaki, 1990, J. Biol. Chem., 265, 2333, 10.1016/S0021-9258(19)39980-6 · DOI
  33. Gibbs, 1988, Proc. Natl. Acad. Sci. U. S. A., 85, 5026, 10.1073/pnas.85.14.5026 · DOI
  34. Vogel, 1988, Nature, 335, 90, 10.1038/335090a0 · DOI
  35. Trahey, 1988, Science, 242, 1697, 10.1126/science.3201259 · DOI
  36. Garrett, 1989, J. Biol. Chem., 264, 10, 10.1016/S0021-9258(17)31215-2 · DOI
  37. Yamamoto, J., Kikuchi, A., Ueda, T., Ohga, N., and Takai, Y. (1990) Mol. Brain Res., in press
  38. Kawata, 1988, J. Biol. Chem., 263, 18965, 10.1016/S0021-9258(18)37376-9 · DOI
  39. Pizon, 1988, Oncogene, 3, 201
  40. Kitayama, 1989, Cell, 56, 77, 10.1016/0092-8674(89)90985-9 · DOI
  41. Ueda, 1989, Biochem. Biophys. Res. Commun., 159, 1411, 10.1016/0006-291X(89)92267-5 · DOI
  42. Kikuchi, 1989, J. Biol. Chem., 264, 9133, 10.1016/S0021-9258(18)60503-4 · DOI
  43. Satoh, 1988, Biochim. Biophys. Acta, 949, 97, 10.1016/0167-4781(88)90059-0 · DOI
  44. Ohmori, 1989, J. Biol. Chem., 264, 1877, 10.1016/S0021-9258(18)94269-9 · DOI
  45. Laemmli, 1970, Nature, 227, 680, 10.1038/227680a0 · DOI · Paper page
  46. Martin, 1961, J. Biol. Chem., 236, 1372, 10.1016/S0021-9258(18)64180-8 · DOI
  47. O'Farrell, 1975, J. Biol. Chem., 250, 4007, 10.1016/S0021-9258(19)41496-8 · DOI
  48. Bradford, 1976, Anal. Biochem., 72, 248, 10.1016/0003-2697(76)90527-3 · DOI · Paper page
  49. Olofsson, 1988, Oncogene, 3, 231
  50. Ohashi, 1987, J. Biol. Chem., 262, 1430, 10.1016/S0021-9258(19)75651-8 · DOI
  51. Bokoch, 1988, J. Biol. Chem., 263, 16744, 10.1016/S0021-9258(18)37454-4 · DOI
  52. Matsuoka, 1989, J. Biol. Chem., 264, 706, 10.1016/S0021-9258(19)85000-7 · DOI
  53. Broek, 1987, Cell, 48, 789, 10.1016/0092-8674(87)90076-6 · DOI

Cited by

Metadata

Authors
Ueda, T., Kikuchi, A., Ohga, N., Yamamoto, J., & Takai, Y.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1990-06
Volume
265
Issue
16
Pages
9373-9380
ISSN
0021-9258
DOI
10.1016/s0021-9258(19)38859-3
Cited by
218
References
1
Language
en
Licence

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review