GRB2

From Wikipedia, the free encyclopedia
Growth factor receptor-bound protein 2

PDB rendering based on 1gri.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsGRB2; ASH; EGFRBP-GRB2; Grb3-3; MST084; MSTP084; NCKAP2
External IDsOMIM: 108355 MGI: 95805 HomoloGene: 1576 ChEMBL: 3663 GeneCards: GRB2 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez288514784
EnsemblENSG00000177885ENSMUSG00000059923
UniProtP62993Q60631
RefSeq (mRNA)NM_002086NM_008163
RefSeq (protein)NP_002077NP_032189
Location (UCSC)Chr 17:
73.31 – 73.4 Mb		Chr 11:
115.64 – 115.71 Mb
PubMed search
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Growth factor receptor-bound protein 2 also known as Grb2 is an adaptor protein involved in signal transduction/cell communication. In humans, the GRB2 protein is encoded by the GRB2 gene.[1][2]

The protein encoded by this gene binds receptors such as the epidermal growth factor receptor and contains one SH2 domain and two SH3 domains. Its two SH3 domains direct complex formation with proline-rich regions of other proteins, and its SH2 domain binds tyrosine phosphorylated sequences. This gene is similar to the sem-5 gene of Caenorhabditis elegans, which is involved in the signal transduction pathway. Two alternatively spliced transcript variants encoding different isoforms have been found for this gene.[3]

Function and expression

Grb2 is widely expressed and is essential for multiple cellular functions. Inhibition of Grb2 function impairs developmental processes in various organisms and blocks transformation and proliferation of various cell types, and so it is not surprising that a targeted gene disruption of Grb2 in mouse is lethal at an early embryonic stage. Grb2 is best known for its ability to link the epidermal growth factor receptor tyrosine kinase to the activation of Ras and its downstream kinases, ERK1,2. Grb2 is composed of an SH2 domain flanked on each side by an SH3 domain. Grb2 has two closely related proteins with similar domain organizations, Gads and Grap. Gads and Grap are expressed specifically in hematopoietic cells and function in the coordination of tyrosine kinase mediated signal transduction.

Domains

The SH2 domain of Grb2 binds to phosphorylated tyrosine-containing peptides on receptors or scaffold proteins with a preference for pY-X-N-X, where X is generally a hydrophobic residue such as valine (see ).

The N-terminal SH3 domain binds to proline-rich peptides and can bind to the Ras-guanine exchange factor SOS.

The C-terminal SH3 domain binds to peptides conforming to a P-X-I/L/V/-D/N-R-X-X-K-P motif that allows it to specifically bind to proteins such as Gab-1.[4]

Interactions

Grb2 has been shown to interact with Arachidonate 5-lipoxygenase,[5][6] Lymphocyte cytosolic protein 2,[7][8][9][10][11] GAB2,[12][13][14] B-cell linker,[15][16][17][18] Abl gene,[19][20] CD28,[21][22] FRS2,[23][24][25][26] Mitogen-activated protein kinase 9,[27][28] CD22,[29][30] NEU3,[31] ETV6,[12] MAP2,[32][33] Dock180,[34][35] PIK3R1,[36][37] SH2B1,[38][39] CRK,[40][41][42] GAB1,[7][43][44] MST1R,[45][46] DNM1,[47][48] Huntingtin,[49] Src,[50][51] Beta-2 adrenergic receptor,[52] VAV2,[53][54] ADAM15,[55] RAPGEF1,[56][57] VAV1,[58][59][60][61] HER2/neu,[54][62][63] Epidermal growth factor receptor,[2][43][53][62][64][65][66][67][68][69] PDGFRB,[69][70][71] PTK2,[72][73][74][75][76] Erythropoietin receptor,[77][78] Linker of activated T cells,[79][80][81] Dystroglycan,[82] SH3KBP1,[83][84] Granulocyte colony-stimulating factor receptor,[85] DCTN1,[86] CDKN1B,[87] Colony stimulating factor 1 receptor,[88] EPH receptor A2,[89] KHDRBS1,[43][90][91] RET proto-oncogene,[92][93] PLCG1,[94][95][96] TrkA,[97][98] PRKAR1A,[66] Janus kinase 2,[99][100] MUC1,[101] CD117,[78][102][103] Fas ligand,[104][105] Janus kinase 1,[100][106] VAV3,[53][107] BCAR1,[73][108] PTPN1,[109][110] INPP5D,[111] ITK,[112][113] SHC1,[51][53][114][115][116][117][118][119][120][121][122][123][124][125][126][127][128][129][130][131][132] PTPN12,[133] C-Met,[134][135] PTPN11,[71][85][127][136][137][138][139][140][141] Glycoprotein 130,[61] PTPN6,[51][136][142] Syk,[51][136] MAP4K1,[143][144][145][146] Wiskott-Aldrich syndrome protein,[147][148] NCKIPSD,[149][150] PTPRA,[151][152][153] BCR gene,[12][115][154][155][156][157] CBLB,[158][159][160] Cbl gene,[9][24][51][90][124][158][161][162][163][164][165][166][167] SOS1,[8][24][42][43][48][51][53][60][68][90][95][101][115][122][124][131][168][169][170][171][172] IRS1,[100][114][173] TNK2,[116][174] MED28,[175] MAP3K1[176] and HNRNPC.[177]

See also

References

  1. ↑ Matuoka K, Shibata M, Yamakawa A, Takenawa T (October 1992). "Cloning of ASH, a ubiquitous protein composed of one Src homology region (SH) 2 and two SH3 domains, from human and rat cDNA libraries". Proc. Natl. Acad. Sci. U.S.A. 89 (19): 9015–9. doi:10.1073/pnas.89.19.9015. PMC 50055. PMID 1384039. 
  2. ↑ 2.0 2.1 Lowenstein EJ, Daly RJ, Batzer AG, Li W, Margolis B, Lammers R, Ullrich A, Skolnik EY, Bar-Sagi D, Schlessinger J (August 1992). "The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling". Cell 70 (3): 431–42. doi:10.1016/0092-8674(92)90167-B. PMID 1322798. 
  3. ↑ "Entrez Gene: GRB2 growth factor receptor-bound protein 2". 
  4. ↑ Berry DM, Nash P, Liu SK, Pawson T, McGlade CJ (2002). "A high-affinity Arg-X-X-Lys SH3 binding motif confers specificity for the interaction between Gads and SLP-76 in T cell signaling". Curr. Biol. 12 (15): 1336–41. doi:10.1016/S0960-9822(02)01038-2. PMID 12176364. 
  5. ↑ VanderNoot, V A; Fitzpatrick F A (Sep 1995). "Competitive binding assay of src homology domain 3 interactions between 5-lipoxygenase and growth factor receptor binding protein 2". Anal. Biochem. (UNITED STATES) 230 (1): 108–14. doi:10.1006/abio.1995.1444. ISSN 0003-2697. PMID 8585605. 
  6. ↑ Lepley, R A; Fitzpatrick F A (Sep 1994). "5-Lipoxygenase contains a functional Src homology 3-binding motif that interacts with the Src homology 3 domain of Grb2 and cytoskeletal proteins". J. Biol. Chem. (UNITED STATES) 269 (39): 24163–8. ISSN 0021-9258. PMID 7929073. 
  7. ↑ 7.0 7.1 Lewitzky, M; Kardinal C, Gehring N H, Schmidt E K, Konkol B, Eulitz M, Birchmeier W, Schaeper U, Feller S M (Mar 2001). "The C-terminal SH3 domain of the adapter protein Grb2 binds with high affinity to sequences in Gab1 and SLP-76 which lack the SH3-typical P-x-x-P core motif". Oncogene (England) 20 (9): 1052–62. doi:10.1038/sj.onc.1204202. ISSN 0950-9232. PMID 11314042. 
  8. ↑ 8.0 8.1 Robinson, A; Gibbins J, Rodríguez-Liñares B, Finan P M, Wilson L, Kellie S, Findell P, Watson S P (Jul 1996). "Characterization of Grb2-binding proteins in human platelets activated by Fc gamma RIIA cross-linking". Blood (UNITED STATES) 88 (2): 522–30. ISSN 0006-4971. PMID 8695800. 
  9. ↑ 9.0 9.1 Erdreich-Epstein, A; Liu M, Kant A M, Izadi K D, Nolta J A, Durden D L (Apr 1999). "Cbl functions downstream of Src kinases in Fc gamma RI signaling in primary human macrophages". J. Leukoc. Biol. (UNITED STATES) 65 (4): 523–34. ISSN 0741-5400. PMID 10204582. 
  10. ↑ Hendricks-Taylor, L R; Motto D G, Zhang J, Siraganian R P, Koretzky G A (Jan 1997). "SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells". J. Biol. Chem. (UNITED STATES) 272 (2): 1363–7. doi:10.1074/jbc.272.2.1363. ISSN 0021-9258. PMID 8995445. 
  11. ↑ Asada, H; Ishii N, Sasaki Y, Endo K, Kasai H, Tanaka N, Takeshita T, Tsuchiya S, Konno T, Sugamura K (May 1999). "Grf40, A novel Grb2 family member, is involved in T cell signaling through interaction with SLP-76 and LAT". J. Exp. Med. (UNITED STATES) 189 (9): 1383–90. doi:10.1084/jem.189.9.1383. ISSN 0022-1007. PMC 2193052. PMID 10224278. 
  12. ↑ 12.0 12.1 12.2 Million, Ryan P; Harakawa Nari, Roumiantsev Sergei, Varticovski Lyuba, Van Etten Richard A (Jun 2004). "A direct binding site for Grb2 contributes to transformation and leukemogenesis by the Tel-Abl (ETV6-Abl) tyrosine kinase". Mol. Cell. Biol. (United States) 24 (11): 4685–95. doi:10.1128/MCB.24.11.4685-4695.2004. ISSN 0270-7306. PMC 416425. PMID 15143164. 
  13. ↑ Lynch, Danielle K; Daly Roger J (Jan 2002). "PKB-mediated negative feedback tightly regulates mitogenic signalling via Gab2". EMBO J. (England) 21 (1–2): 72–82. doi:10.1093/emboj/21.1.72. ISSN 0261-4189. PMC 125816. PMID 11782427. 
  14. ↑ Zhao, C; Yu D H, Shen R, Feng G S (Jul 1999). "Gab2, a new pleckstrin homology domain-containing adapter protein, acts to uncouple signaling from ERK kinase to Elk-1". J. Biol. Chem. (UNITED STATES) 274 (28): 19649–54. doi:10.1074/jbc.274.28.19649. ISSN 0021-9258. PMID 10391903. 
  15. ↑ Fu, C; Turck C W, Kurosaki T, Chan A C (Jul 1998). "BLNK: a central linker protein in B cell activation". Immunity (UNITED STATES) 9 (1): 93–103. doi:10.1016/S1074-7613(00)80591-9. ISSN 1074-7613. PMID 9697839. 
  16. ↑ Engels, N; Wollscheid B, Wienands J (Jul 2001). "Association of SLP-65/BLNK with the B cell antigen receptor through a non-ITAM tyrosine of Ig-alpha". Eur. J. Immunol. (Germany) 31 (7): 2126–34. doi:10.1002/1521-4141(200107)31:7<2126::AID-IMMU2126>3.0.CO;2-O. ISSN 0014-2980. PMID 11449366. 
  17. ↑ Fusaki, N; Tomita S, Wu Y, Okamoto N, Goitsuka R, Kitamura D, Hozumi N (May 2000). "BLNK is associated with the CD72/SHP-1/Grb2 complex in the WEHI231 cell line after membrane IgM cross-linking". Eur. J. Immunol. (GERMANY) 30 (5): 1326–30. doi:10.1002/(SICI)1521-4141(200005)30:5<1326::AID-IMMU1326>3.0.CO;2-Q. ISSN 0014-2980. PMID 10820378. 
  18. ↑ Wienands, J; Schweikert J, Wollscheid B, Jumaa H, Nielsen P J, Reth M (Aug 1998). "SLP-65: a new signaling component in B lymphocytes which requires expression of the antigen receptor for phosphorylation". J. Exp. Med. (UNITED STATES) 188 (4): 791–5. doi:10.1084/jem.188.4.791. ISSN 0022-1007. PMC 2213353. PMID 9705962. 
  19. ↑ Warmuth, M; Bergmann M, Priess A, Häuslmann K, Emmerich B, Hallek M (Dec 1997). "The Src family kinase Hck interacts with Bcr-Abl by a kinase-independent mechanism and phosphorylates the Grb2-binding site of Bcr". J. Biol. Chem. (UNITED STATES) 272 (52): 33260–70. doi:10.1074/jbc.272.52.33260. ISSN 0021-9258. PMID 9407116. 
  20. ↑ Ren, R; Ye Z S, Baltimore D (Apr 1994). "Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites". Genes Dev. (UNITED STATES) 8 (7): 783–95. doi:10.1101/gad.8.7.783. ISSN 0890-9369. PMID 7926767. 
  21. ↑ Okkenhaug, K; Rottapel R (Aug 1998). "Grb2 forms an inducible protein complex with CD28 through a Src homology 3 domain-proline interaction". J. Biol. Chem. (UNITED STATES) 273 (33): 21194–202. doi:10.1074/jbc.273.33.21194. ISSN 0021-9258. PMID 9694876. 
  22. ↑ Nunès, J A; Truneh A, Olive D, Cantrell D A (Jan 1996). "Signal transduction by CD28 costimulatory receptor on T cells. B7-1 and B7-2 regulation of tyrosine kinase adaptor molecules". J. Biol. Chem. (UNITED STATES) 271 (3): 1591–8. doi:10.1074/jbc.271.3.1591. ISSN 0021-9258. PMID 8576157. 
  23. ↑ Ong, S H; Goh K C, Lim Y P, Low B C, Klint P, Claesson-Welsh L, Cao X, Tan Y H, Guy G R (Aug 1996). "Suc1-associated neurotrophic factor target (SNT) protein is a major FGF-stimulated tyrosine phosphorylated 90-kDa protein which binds to the SH2 domain of GRB2". Biochem. Biophys. Res. Commun. (UNITED STATES) 225 (3): 1021–6. doi:10.1006/bbrc.1996.1288. ISSN 0006-291X. PMID 8780727. 
  24. ↑ 24.0 24.1 24.2 Wong, Andy; Lamothe Betty, Lee Arnold, Schlessinger Joseph, Lax Irit, Li Arnold (May 2002). "FRS2 alpha attenuates FGF receptor signaling by Grb2-mediated recruitment of the ubiquitin ligase Cbl". Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (10): 6684–9. doi:10.1073/pnas.052138899. ISSN 0027-8424. PMC 124463. PMID 11997436. 
  25. ↑ Meakin, S O; MacDonald J I, Gryz E A, Kubu C J, Verdi J M (Apr 1999). "The signaling adapter FRS-2 competes with Shc for binding to the nerve growth factor receptor TrkA. A model for discriminating proliferation and differentiation". J. Biol. Chem. (UNITED STATES) 274 (14): 9861–70. doi:10.1074/jbc.274.14.9861. ISSN 0021-9258. PMID 10092678. 
  26. ↑ Kouhara, H; Hadari Y R, Spivak-Kroizman T, Schilling J, Bar-Sagi D, Lax I, Schlessinger J (May 1997). "A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway". Cell (UNITED STATES) 89 (5): 693–702. doi:10.1016/S0092-8674(00)80252-4. ISSN 0092-8674. PMID 9182757. 
  27. ↑ Saleem, A; Datta R, Yuan Z M, Kharbanda S, Kufe D (Dec 1995). "Involvement of stress-activated protein kinase in the cellular response to 1-beta-D-arabinofuranosylcytosine and other DNA-damaging agents". Cell Growth Differ. (UNITED STATES) 6 (12): 1651–8. ISSN 1044-9523. PMID 9019171. 
  28. ↑ Kharbanda, S; Saleem A, Shafman T, Emoto Y, Taneja N, Rubin E, Weichselbaum R, Woodgett J, Avruch J, Kyriakis J (Aug 1995). "Ionizing radiation stimulates a Grb2-mediated association of the stress-activated protein kinase with phosphatidylinositol 3-kinase". J. Biol. Chem. (UNITED STATES) 270 (32): 18871–4. doi:10.1074/jbc.270.32.18871. ISSN 0021-9258. PMID 7642542. 
  29. ↑ Poe, J C; Fujimoto M, Jansen P J, Miller A S, Tedder T F (Jun 2000). "CD22 forms a quaternary complex with SHIP, Grb2, and Shc. A pathway for regulation of B lymphocyte antigen receptor-induced calcium flux". J. Biol. Chem. (UNITED STATES) 275 (23): 17420–7. doi:10.1074/jbc.M001892200. ISSN 0021-9258. PMID 10748054. 
  30. ↑ Otipoby, K L; Draves K E, Clark E A (Nov 2001). "CD22 regulates B cell receptor-mediated signals via two domains that independently recruit Grb2 and SHP-1". J. Biol. Chem. (United States) 276 (47): 44315–22. doi:10.1074/jbc.M105446200. ISSN 0021-9258. PMID 11551923. 
  31. ↑ Sasaki, Akinori; Hata Keiko, Suzuki Susumu, Sawada Masashi, Wada Tadashi, Yamaguchi Kazunori, Obinata Masuo, Tateno Hiroo, Suzuki Hiroshi, Miyagi Taeko (Jul 2003). "Overexpression of plasma membrane-associated sialidase attenuates insulin signaling in transgenic mice". J. Biol. Chem. (United States) 278 (30): 27896–902. doi:10.1074/jbc.M212200200. ISSN 0021-9258. PMID 12730204. 
  32. ↑ Lim, R W; Halpain S (Jul 2000). "Regulated association of microtubule-associated protein 2 (MAP2) with Src and Grb2: evidence for MAP2 as a scaffolding protein". J. Biol. Chem. (UNITED STATES) 275 (27): 20578–87. doi:10.1074/jbc.M001887200. ISSN 0021-9258. PMID 10781592. 
  33. ↑ Zamora-Leon, S P; Lee G, Davies P, Shafit-Zagardo B (Oct 2001). "Binding of Fyn to MAP-2c through an SH3 binding domain. Regulation of the interaction by ERK2". J. Biol. Chem. (United States) 276 (43): 39950–8. doi:10.1074/jbc.M107807200. ISSN 0021-9258. PMID 11546790. 
  34. ↑ Hsia, Datsun A; Mitra Satyajit K, Hauck Christof R, Streblow Daniel N, Nelson Jay A, Ilic Dusko, Huang Shuang, Li Erguang, Nemerow Glen R, Leng Jay, Spencer Kathryn S R, Cheresh David A, Schlaepfer David D (Mar 2003). "Differential regulation of cell motility and invasion by FAK". J. Cell Biol. (United States) 160 (5): 753–67. doi:10.1083/jcb.200212114. ISSN 0021-9525. PMC 2173366. PMID 12615911. 
  35. ↑ Hasegawa, H; Kiyokawa E, Tanaka S, Nagashima K, Gotoh N, Shibuya M, Kurata T, Matsuda M (Apr 1996). "DOCK180, a major CRK-binding protein, alters cell morphology upon translocation to the cell membrane". Mol. Cell. Biol. (UNITED STATES) 16 (4): 1770–6. ISSN 0270-7306. PMC 231163. PMID 8657152. 
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  37. ↑ Wang, J; Auger K R, Jarvis L, Shi Y, Roberts T M (May 1995). "Direct association of Grb2 with the p85 subunit of phosphatidylinositol 3-kinase". J. Biol. Chem. (UNITED STATES) 270 (21): 12774–80. doi:10.1074/jbc.270.21.12774. ISSN 0021-9258. PMID 7759531. 
  38. ↑ Qian, X; Riccio A, Zhang Y, Ginty D D (Nov 1998). "Identification and characterization of novel substrates of Trk receptors in developing neurons". Neuron (UNITED STATES) 21 (5): 1017–29. doi:10.1016/S0896-6273(00)80620-0. ISSN 0896-6273. PMID 9856458. 
  39. ↑ Kotani, K; Wilden P, Pillay T S (Oct 1998). "SH2-Balpha is an insulin-receptor adapter protein and substrate that interacts with the activation loop of the insulin-receptor kinase". Biochem. J. (ENGLAND) 335 (1): 103–9. ISSN 0264-6021. PMC 1219757. PMID 9742218. 
  40. ↑ Riordan, S M; Lidder S, Williams R, Skouteris G G (Sep 2000). "The beta-subunit of the hepatocyte growth factor/scatter factor (HGF/SF) receptor phosphorylates and associates with CrkII: expression of CrkII enhances HGF/SF-induced mitogenesis". Biochem. J. (ENGLAND) 350 (3): 925–32. ISSN 0264-6021. PMC 1221328. PMID 10970810. 
  41. ↑ Matsuda, M; Ota S, Tanimura R, Nakamura H, Matuoka K, Takenawa T, Nagashima K, Kurata T (Jun 1996). "Interaction between the amino-terminal SH3 domain of CRK and its natural target proteins". J. Biol. Chem. (UNITED STATES) 271 (24): 14468–72. doi:10.1074/jbc.271.24.14468. ISSN 0021-9258. PMID 8662907. 
  42. ↑ 42.0 42.1 Okada, S; Pessin J E (Oct 1996). "Interactions between Src homology (SH) 2/SH3 adapter proteins and the guanylnucleotide exchange factor SOS are differentially regulated by insulin and epidermal growth factor". J. Biol. Chem. (UNITED STATES) 271 (41): 25533–8. doi:10.1074/jbc.271.41.25533. ISSN 0021-9258. PMID 8810325. 
  43. ↑ 43.0 43.1 43.2 43.3 Oneyama, Chitose; Nakano Hirofumi, Sharma Sreenath V (Mar 2002). "UCS15A, a novel small molecule, SH3 domain-mediated protein–protein interaction blocking drug". Oncogene (England) 21 (13): 2037–50. doi:10.1038/sj.onc.1205271. ISSN 0950-9232. PMID 11960376. 
  44. ↑ Holgado-Madruga, M; Emlet D R, Moscatello D K, Godwin A K, Wong A J (Feb 1996). "A Grb2-associated docking protein in EGF- and insulin-receptor signalling". Nature (ENGLAND) 379 (6565): 560–4. doi:10.1038/379560a0. ISSN 0028-0836. PMID 8596638. 
  45. ↑ Li, B Q; Wang M H, Kung H F, Ronsin C, Breathnach R, Leonard E J, Kamata T (Nov 1995). "Macrophage-stimulating protein activates Ras by both activation and translocation of SOS nucleotide exchange factor". Biochem. Biophys. Res. Commun. (UNITED STATES) 216 (1): 110–8. doi:10.1006/bbrc.1995.2598. ISSN 0006-291X. PMID 7488076. 
  46. ↑ Iwama, A; Yamaguchi N, Suda T (Nov 1996). "STK/RON receptor tyrosine kinase mediates both apoptotic and growth signals via the multifunctional docking site conserved among the HGF receptor family". EMBO J. (ENGLAND) 15 (21): 5866–75. ISSN 0261-4189. PMC 452340. PMID 8918464. 
  47. ↑ Miki, H; Miura K, Matuoka K, Nakata T, Hirokawa N, Orita S, Kaibuchi K, Takai Y, Takenawa T (Feb 1994). "Association of Ash/Grb-2 with dynamin through the Src homology 3 domain". J. Biol. Chem. (UNITED STATES) 269 (8): 5489–92. ISSN 0021-9258. PMID 8119878. 
  48. ↑ 48.0 48.1 Sastry, L; Cao T, King C R (Jan 1997). "Multiple Grb2-protein complexes in human cancer cells". Int. J. Cancer (UNITED STATES) 70 (2): 208–13. doi:10.1002/(SICI)1097-0215(19970117)70:2<208::AID-IJC12>3.0.CO;2-E. ISSN 0020-7136. PMID 9009162. 
  49. ↑ Liu, Y F; Deth R C, Devys D (Mar 1997). "SH3 domain-dependent association of huntingtin with epidermal growth factor receptor signaling complexes". J. Biol. Chem. (UNITED STATES) 272 (13): 8121–4. doi:10.1074/jbc.272.13.8121. ISSN 0021-9258. PMID 9079622. 
  50. ↑ Wan, Kah Fei; Sambi Balwinder S, Tate Rothwelle, Waters Catherine, Pyne Nigel J (May 2003). "The inhibitory gamma subunit of the type 6 retinal cGMP phosphodiesterase functions to link c-Src and G-protein-coupled receptor kinase 2 in a signaling unit that regulates p42/p44 mitogen-activated protein kinase by epidermal growth factor". J. Biol. Chem. (United States) 278 (20): 18658–63. doi:10.1074/jbc.M212103200. ISSN 0021-9258. PMID 12624098. 
  51. ↑ 51.0 51.1 51.2 51.3 51.4 51.5 Saci, Abdelhafid; Liu Wang-Qing, Vidal Michel, Garbay Christiane, Rendu Francine, Bachelot-Loza Christilla (May 2002). "Differential effect of the inhibition of Grb2-SH3 interactions in platelet activation induced by thrombin and by Fc receptor engagement". Biochem. J. (England) 363 (Pt 3): 717–25. doi:10.1042/0264-6021:3630717. ISSN 0264-6021. PMC 1222524. PMID 11964172. 
  52. ↑ Karoor, V; Wang L, Wang H Y, Malbon C C (Dec 1998). "Insulin stimulates sequestration of beta-adrenergic receptors and enhanced association of beta-adrenergic receptors with Grb2 via tyrosine 350". J. Biol. Chem. (UNITED STATES) 273 (49): 33035–41. doi:10.1074/jbc.273.49.33035. ISSN 0021-9258. PMID 9830057. 
  53. ↑ 53.0 53.1 53.2 53.3 53.4 Blagoev, Blagoy; Kratchmarova Irina, Ong Shao-En, Nielsen Mogens, Foster Leonard J, Mann Matthias (Mar 2003). "A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling". Nat. Biotechnol. (United States) 21 (3): 315–8. doi:10.1038/nbt790. ISSN 1087-0156. PMID 12577067. 
  54. ↑ 54.0 54.1 Bourguignon, L Y; Zhu H, Zhou B, Diedrich F, Singleton P A, Hung M C (Dec 2001). "Hyaluronan promotes CD44v3-Vav2 interaction with Grb2-p185(HER2) and induces Rac1 and Ras signaling during ovarian tumor cell migration and growth". J. Biol. Chem. (United States) 276 (52): 48679–92. doi:10.1074/jbc.M106759200. ISSN 0021-9258. PMID 11606575. 
  55. ↑ Poghosyan, Zaruhi; Robbins Stephen M, Houslay Miles D, Webster Ailsa, Murphy Gillian, Edwards Dylan R (Feb 2002). "Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases". J. Biol. Chem. (United States) 277 (7): 4999–5007. doi:10.1074/jbc.M107430200. ISSN 0021-9258. PMID 11741929. 
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Further reading

  • Colledge M, Froehner SC (1998). "Interaction between the nicotinic acetylcholine receptor and Grb2. Implications for signaling at the neuromuscular junction.". Ann. N. Y. Acad. Sci. 841: 17–27. doi:10.1111/j.1749-6632.1998.tb10907.x. PMID 9668219. 
  • Ramesh N, Antón IM, Martínez-Quiles N, Geha RS (1999). "Waltzing with WASP.". Trends Cell Biol. 9 (1): 15–9. doi:10.1016/S0962-8924(98)01411-1. PMID 10087612. 
  • O'Sullivan E, Kinnon C, Brickell P (1999). "Wiskott-Aldrich syndrome protein, WASP.". Int. J. Biochem. Cell Biol. 31 (3–4): 383–7. doi:10.1016/S1357-2725(98)00118-6. PMID 10224664. 
  • Schlaepfer DD, Hauck CR, Sieg DJ (1999). "Signaling through focal adhesion kinase.". Prog. Biophys. Mol. Biol. 71 (3–4): 435–78. doi:10.1016/S0079-6107(98)00052-2. PMID 10354709. 
  • Vidal M, Liu WQ, Gril B, et al. (2004). "[Design of new anti-tumor agents interrupting deregulated signaling pathways induced by tyrosine kinase proteins. Inhibition of protein-protein interaction involving Grb2]". J. Soc. Biol. 198 (2): 133–7. PMID 15368963. 

External links

JAK-STAT
  • see JAK-STAT signaling pathway
Growth factor receptor-bound protein
Other
B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)
Signaling pathways
Agents
Receptor ligands
Receptors
2nd messenger
Assistants:
Transcription factors
By distance
Other concepts
B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)
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