OpenLB
Open Library of Bioscience
Advanced Search
Molecular and cellular biology
Jun, 1996;16 (6): 2561-9.

A Ras-GTPase-activating protein SH3-domain-binding protein.

F Parker, F Maurier, I Delumeau, M Duchesne, D Faucher, L Debussche, A Dugue, F Schweighoffer, B Tocque
Author Information
  1. F Parker: Gene Medicine Department, Rhône-Poulenc Rorer, Centre de Recherche de Vitry-Alfortville, Vitry Sur Seine, France.
PMID: 8649363 DOI: 10.1128/MCB.16.6.2561

Abstract

We report the purification of a Ras-GTPase-activating protein (GAP)-binding protein, G3BP, a ubiquitously expressed cytosolic 68-kDa protein that coimmunoprecipitates with GAP. G3BP physically associates with the SH3 domain of GAP, which previously had been shown to be essential for Ras signaling. The G3BP cDNA revealed that G3BP is a novel 466-amino-acid protein that shares several features with heterogeneous nuclear RNA-binding proteins, including ribonucleoprotein (RNP) motifs RNP1 and RNP2, an RG-rich domain, and acidic sequences. Recombinant G3BP binds effectively to the GAP SH3 domain G3BP coimmunoprecipitates with GAP only when cells are in a proliferating state, suggesting a recruitment of a GAP-G3BP complex when Ras is in its activated conformation.

Associated Data

GENBANK | U32519

References

  1. Genes Dev. 1992 Sep;6(9):1631-42 [PMID: 1516827]
  2. EMBO J. 1994 Nov 15;13(22):5483-95 [PMID: 7957114]
  3. Proc Natl Acad Sci U S A. 1987 Oct;84(19):6720-4 [PMID: 3477803]
  4. Nature. 1988 Mar 17;332(6161):269-72 [PMID: 2831461]
  5. Nature. 1988 Mar 17;332(6161):272-5 [PMID: 2450282]
  6. EMBO J. 1988 Jan;7(1):161-8 [PMID: 2834200]
  7. Gene. 1988 Jul 15;67(1):31-40 [PMID: 3047011]
  8. Science. 1988 Dec 23;242(4886):1697-700 [PMID: 3201259]
  9. J Cell Biol. 1989 Jan;108(1):79-93 [PMID: 2910879]
  10. EMBO J. 1989 Apr;8(4):1105-10 [PMID: 2545441]
  11. Nature. 1990 Jan 18;343(6255):288-90 [PMID: 2405279]
  12. Nature. 1990 Jan 25;343(6256):377-81 [PMID: 1689011]
  13. Science. 1990 May 11;248(4956):727-30 [PMID: 1692159]
  14. Cell. 1990 Jun 1;61(5):769-76 [PMID: 2188736]
  15. Mol Cell Biol. 1990 Oct;10(10):5314-23 [PMID: 2118993]
  16. Mol Cell Biol. 1990 Oct;10(10):5324-32 [PMID: 2118994]
  17. Mol Cell Biol. 1990 Oct;10(10):5388-96 [PMID: 2398896]
  18. Nature. 1994 Nov 24;372(6504):375-9 [PMID: 7802869]
  19. Biochim Biophys Acta. 1994 Dec 30;1198(2-3):131-47 [PMID: 7819271]
  20. EMBO J. 1995 Feb 1;14(3):484-91 [PMID: 7859737]
  21. Mol Cell Biol. 1995 Mar;15(3):1324-32 [PMID: 7862126]
  22. Cell. 1995 Feb 24;80(4):533-41 [PMID: 7867061]
  23. Nature. 1995 Mar 30;374(6521):457-9 [PMID: 7700355]
  24. Mol Cell Biol. 1995 Oct;15(10):5627-34 [PMID: 7565714]
  25. Cell. 1996 Jan 12;84(1):23-4 [PMID: 8548822]
  26. Proc Natl Acad Sci U S A. 1990 Nov;87(21):8622-6 [PMID: 2236073]
  27. Nature. 1991 Jan 31;349(6308):426-8 [PMID: 1992343]
  28. Mol Cell Biol. 1991 Apr;11(4):1804-12 [PMID: 2005883]
  29. Nature. 1992 Sep 10;359(6391):153-4 [PMID: 1522900]
  30. Biotechnology (N Y). 1992 Oct;10(10):1151-6 [PMID: 1368795]
  31. Science. 1992 Dec 4;258(5088):1665-8 [PMID: 1280858]
  32. Science. 1993 Jan 22;259(5094):525-8 [PMID: 7678707]
  33. Science. 1993 Feb 19;259(5098):1157-61 [PMID: 8438166]
  34. Nature. 1993 May 6;363(6424):45-51 [PMID: 8479536]
  35. Nature. 1993 May 6;363(6424):83-5 [PMID: 8479540]
  36. Nature. 1993 May 6;363(6424):85-8 [PMID: 8479541]
  37. Cell. 1993 May 21;73(4):813-22 [PMID: 7684655]
  38. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):4887-91 [PMID: 8506332]
  39. EMBO J. 1993 Aug;12(8):3073-81 [PMID: 8344248]
  40. Annu Rev Biochem. 1993;62:289-321 [PMID: 8352591]
  41. Mol Cell Biol. 1993 Sep;13(9):5225-32 [PMID: 7689147]
  42. Oncogene. 1993 Oct;8(10):2773-80 [PMID: 8378086]
  43. Cell. 1993 Oct 8;75(1):25-36 [PMID: 8402898]
  44. Mol Cell Biol. 1993 Dec;13(12):7708-17 [PMID: 8246987]
  45. Mol Cell Biol. 1993 Dec;13(12):7892-900 [PMID: 8247004]
  46. Cell. 1994 Mar 11;76(5):933-45 [PMID: 7510218]
  47. Science. 1994 Mar 18;263(5153):1609-12 [PMID: 8128248]
  48. EMBO J. 1994 Mar 15;13(6):1270-9 [PMID: 8137811]
  49. Cancer Metastasis Rev. 1994 Mar;13(1):67-89 [PMID: 8143346]
  50. Cell. 1994 Apr 8;77(1):33-9 [PMID: 8156595]
  51. Nature. 1994 Apr 28;368(6474):867-71 [PMID: 7512694]
  52. Nature. 1994 Apr 28;368(6474):871-4 [PMID: 7512695]
  53. Mol Cell Biol. 1994 Jul;14(7):4509-21 [PMID: 7516469]
  54. Science. 1994 Jul 29;265(5172):615-21 [PMID: 8036511]
  55. J Biol Chem. 1994 Aug 12;269(32):20225-8 [PMID: 8051112]
  56. Cell. 1991 Apr 5;65(1):91-104 [PMID: 1707345]
  57. Trends Biochem Sci. 1991 Jun;16(6):214-20 [PMID: 1716386]
  58. Mol Cell Biol. 1991 Oct;11(10):5113-24 [PMID: 1922035]
  59. Mol Cell Biol. 1992 Jan;12(1):164-71 [PMID: 1729596]
  60. Nature. 1992 Mar 5;356(6364):77-9 [PMID: 1538785]
  61. Science. 1992 Jan 10;255(5041):192-4 [PMID: 1553544]
  62. Cell. 1992 May 1;69(3):539-49 [PMID: 1581965]
  63. Science. 1992 May 8;256(5058):825-7 [PMID: 1317056]
  64. FEBS Lett. 1992 Jul 27;307(1):55-61 [PMID: 1639195]
  65. Cell. 1992 Aug 7;70(3):431-42 [PMID: 1322798]

MeSH Term

3T3 Cells
Amino Acid Sequence
Animals
Base Sequence
Cell Line
Cloning, Molecular
Cricetinae
Cytosol
DNA, Complementary
GTPase-Activating Proteins
Mice
Molecular Sequence Data
Molecular Weight
Open Reading Frames
Precipitin Tests
Protein Binding
Proteins
Sequence Homology, Amino Acid
ras GTPase-Activating Proteins
src Homology Domains

Chemicals

DNA, Complementary
GTPase-Activating Proteins
Proteins
ras GTPase-Activating Proteins
Journal Article Research Support, Non-U.S. Gov't
Article has an altmetric score of 9

Word Cloud

Created with Highcharts 10.0.0proteinG3BPGAPdomainRas-GTPase-activatingcoimmunoprecipitatesSH3Rasreportpurification-bindingubiquitouslyexpressedcytosolic68-kDaphysicallyassociatespreviouslyshownessentialsignalingcDNArevealednovel466-amino-acidsharesseveralfeaturesheterogeneousnuclearRNA-bindingproteinsincludingribonucleoproteinRNPmotifsRNP1RNP2RG-richacidicsequencesRecombinantbindseffectivelycellsproliferatingstatesuggestingrecruitmentGAP-G3BPcomplexactivatedconformationSH3-domain-binding

Similar Articles

Cited By