GRB2
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. It is thus not surprising that targeted gene disruption of Grb2 in mice 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:
- ADAM15,[5]
- Abl gene,[6][7]
- Arachidonate 5-lipoxygenase,[8][9]
- B-cell linker,[10][11][12][13]
- BCAR1,[14][15]
- BCR gene,[16][17][18][19][20][21]
- Beta-2 adrenergic receptor,[22]
- C-Met,[23][24]
- CBLB,[25][26][27]
- CD117,[28][29][30]
- CD22,[31][32]
- CD28,[33][34]
- CDKN1B,[35]
- CRK,[36][37][38]
- Cbl gene,[25][39][40][41][42][43][44][45][46][47][48][49][50]
- Colony stimulating factor 1 receptor,[51]
- DCTN1,[52]
- DNM1,[53][54]
- Dock180,[55][56]
- Dystroglycan,[57]
- EPH receptor A2,[58]
- ETV6,[16]
- Epidermal growth factor receptor,[2][59][60][61][62][63][64][65][66][67]
- Erythropoietin receptor,[28][68]
- FRS2,[40][69][70][71]
- Fas ligand,[72][73]
- GAB1,[59][74][75]
- GAB2,[16][76][77]
- Glycoprotein 130,[78]
- Granulocyte colony-stimulating factor receptor,[79]
- HER2/neu,[61][80][81]
- HNRNPC,[82]
- Huntingtin,[83]
- INPP5D,[84]
- IRS1,[85][86][87]
- ITK,[88][89]
- Janus kinase 1,[85][90]
- Janus kinase 2,[85][91]
- KHDRBS1,[42][59][92]
- Linker of activated T cells,[93][94][95]
- Lymphocyte cytosolic protein 2,[39][74][96][97][98]
- MAP2,[99][100]
- MAP3K1[101]
- MAP4K1,[102][103][104][105]
- MED28,[106]
- MST1R,[107][108]
- MUC1,[109]
- Mitogen-activated protein kinase 9,[110][111]
- NCKIPSD,[112][113]
- NEU3,[114]
- PDGFRB,[67][115][116]
- PIK3R1,[117][118]
- PLCG1,[119][120][121]
- PRKAR1A,[64]
- PTK2,[14][122][123][124][125]
- PTPN11,[79][116][126][127][128][129][130][131][132]
- PTPN12,[133]
- PTPN1,[134][135]
- PTPN6,[41][127][136]
- PTPRA,[137][138][139]
- RAPGEF1,[140][141]
- RET proto-oncogene,[142][143]
- SH2B1,[144][145]
- SH3KBP1,[146][147]
- SHC1,[17][41][43][60][86][126][148][149][150][151][152][153][154][155][156][157][158][159][160][161][162]
- SOS1,[17][38][40][41][42][43][54][59][60][66][96][109][120][154][161][163][164][165][166][167][168]
- Src,[41][169]
- Syk,[41][127]
- TNK2,[148][170]
- TrkA,[171][172]
- VAV1,[78][163][173][174]
- VAV2,[60][80]
- VAV3,[60][175] and
- Wiskott-Aldrich syndrome protein.[176][177]
See also
References
- ↑ Matuoka K, Shibata M, Yamakawa A, Takenawa T (Oct 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". Proceedings of the National Academy of Sciences of the United States of America 89 (19): 9015–9. doi:10.1073/pnas.89.19.9015. PMC 50055. PMID 1384039.
- 1 2 Lowenstein EJ, Daly RJ, Batzer AG, Li W, Margolis B, Lammers R, Ullrich A, Skolnik EY, Bar-Sagi D, Schlessinger J (Aug 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.
- ↑ "Entrez Gene: GRB2 growth factor receptor-bound protein 2".
- ↑ Berry DM, Nash P, Liu SK, Pawson T, McGlade CJ (Aug 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". Current Biology 12 (15): 1336–41. doi:10.1016/S0960-9822(02)01038-2. PMID 12176364.
- ↑ Poghosyan Z, Robbins SM, Houslay MD, Webster A, Murphy G, Edwards DR (Feb 2002). "Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases". The Journal of Biological Chemistry 277 (7): 4999–5007. doi:10.1074/jbc.M107430200. PMID 11741929.
- ↑ 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". The Journal of Biological Chemistry 272 (52): 33260–70. doi:10.1074/jbc.272.52.33260. PMID 9407116.
- ↑ Ren R, Ye ZS, Baltimore D (Apr 1994). "Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites". Genes & Development 8 (7): 783–95. doi:10.1101/gad.8.7.783. PMID 7926767.
- ↑ VanderNoot VA, Fitzpatrick FA (Sep 1995). "Competitive binding assay of src homology domain 3 interactions between 5-lipoxygenase and growth factor receptor binding protein 2". Analytical Biochemistry 230 (1): 108–14. doi:10.1006/abio.1995.1444. PMID 8585605.
- ↑ Lepley RA, Fitzpatrick FA (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". The Journal of Biological Chemistry 269 (39): 24163–8. PMID 7929073.
- ↑ Fu C, Turck CW, Kurosaki T, Chan AC (Jul 1998). "BLNK: a central linker protein in B cell activation". Immunity 9 (1): 93–103. doi:10.1016/S1074-7613(00)80591-9. PMID 9697839.
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- ↑ 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". European Journal of Immunology 30 (5): 1326–30. doi:10.1002/(sici)1521-4141(200005)30:5<1326::aid-immu1326>3.0.co;2-q. PMID 10820378.
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- ↑ Bai RY, Jahn T, Schrem S, Munzert G, Weidner KM, Wang JY, Duyster J (Aug 1998). "The SH2-containing adapter protein GRB10 interacts with BCR-ABL". Oncogene 17 (8): 941–8. doi:10.1038/sj.onc.1202024. PMID 9747873.
- ↑ Ma G, Lu D, Wu Y, Liu J, Arlinghaus RB (May 1997). "Bcr phosphorylated on tyrosine 177 binds Grb2". Oncogene 14 (19): 2367–72. doi:10.1038/sj.onc.1201053. PMID 9178913.
- ↑ Maru Y, Peters KL, Afar DE, Shibuya M, Witte ON, Smithgall TE (Feb 1995). "Tyrosine phosphorylation of BCR by FPS/FES protein-tyrosine kinases induces association of BCR with GRB-2/SOS". Molecular and Cellular Biology 15 (2): 835–42. PMC 231961. PMID 7529874.
- ↑ Karoor V, Wang L, Wang HY, Malbon CC (Dec 1998). "Insulin stimulates sequestration of beta-adrenergic receptors and enhanced association of beta-adrenergic receptors with Grb2 via tyrosine 350". The Journal of Biological Chemistry 273 (49): 33035–41. doi:10.1074/jbc.273.49.33035. PMID 9830057.
- ↑ Ponzetto C, Zhen Z, Audero E, Maina F, Bardelli A, Basile ML, Giordano S, Narsimhan R, Comoglio P (Jun 1996). "Specific uncoupling of GRB2 from the Met receptor. Differential effects on transformation and motility". The Journal of Biological Chemistry 271 (24): 14119–23. doi:10.1074/jbc.271.24.14119. PMID 8662889.
- ↑ Liang Q, Mohan RR, Chen L, Wilson SE (Jul 1998). "Signaling by HGF and KGF in corneal epithelial cells: Ras/MAP kinase and Jak-STAT pathways". Investigative Ophthalmology & Visual Science 39 (8): 1329–38. PMID 9660480.
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- ↑ Lavagna-Sévenier C, Marchetto S, Birnbaum D, Rosnet O (Jun 1998). "The CBL-related protein CBLB participates in FLT3 and interleukin-7 receptor signal transduction in pro-B cells". The Journal of Biological Chemistry 273 (24): 14962–7. doi:10.1074/jbc.273.24.14962. PMID 9614102.
- ↑ Elly C, Witte S, Zhang Z, Rosnet O, Lipkowitz S, Altman A, Liu YC (Feb 1999). "Tyrosine phosphorylation and complex formation of Cbl-b upon T cell receptor stimulation". Oncogene 18 (5): 1147–56. doi:10.1038/sj.onc.1202411. PMID 10022120.
- 1 2 Feng GS, Ouyang YB, Hu DP, Shi ZQ, Gentz R, Ni J (May 1996). "Grap is a novel SH3-SH2-SH3 adaptor protein that couples tyrosine kinases to the Ras pathway". The Journal of Biological Chemistry 271 (21): 12129–32. doi:10.1074/jbc.271.21.12129. PMID 8647802.
- ↑ De Sepulveda P, Okkenhaug K, Rose JL, Hawley RG, Dubreuil P, Rottapel R (Feb 1999). "Socs1 binds to multiple signalling proteins and suppresses steel factor-dependent proliferation". The EMBO Journal 18 (4): 904–15. doi:10.1093/emboj/18.4.904. PMC 1171183. PMID 10022833.
- ↑ Thömmes K, Lennartsson J, Carlberg M, Rönnstrand L (Jul 1999). "Identification of Tyr-703 and Tyr-936 as the primary association sites for Grb2 and Grb7 in the c-Kit/stem cell factor receptor". The Biochemical Journal 341 (1): 211–6. doi:10.1042/0264-6021:3410211. PMC 1220349. PMID 10377264.
- ↑ Poe JC, Fujimoto M, Jansen PJ, Miller AS, Tedder TF (Jun 2000). "CD22 forms a quaternary complex with SHIP, Grb2, and Shc. A pathway for regulation of B lymphocyte antigen receptor-induced calcium flux". The Journal of Biological Chemistry 275 (23): 17420–7. doi:10.1074/jbc.M001892200. PMID 10748054.
- ↑ Otipoby KL, Draves KE, Clark EA (Nov 2001). "CD22 regulates B cell receptor-mediated signals via two domains that independently recruit Grb2 and SHP-1". The Journal of Biological Chemistry 276 (47): 44315–22. doi:10.1074/jbc.M105446200. PMID 11551923.
- ↑ Okkenhaug K, Rottapel R (Aug 1998). "Grb2 forms an inducible protein complex with CD28 through a Src homology 3 domain-proline interaction". The Journal of Biological Chemistry 273 (33): 21194–202. doi:10.1074/jbc.273.33.21194. PMID 9694876.
- ↑ Nunès JA, Truneh A, Olive D, Cantrell DA (Jan 1996). "Signal transduction by CD28 costimulatory receptor on T cells. B7-1 and B7-2 regulation of tyrosine kinase adaptor molecules". The Journal of Biological Chemistry 271 (3): 1591–8. doi:10.1074/jbc.271.3.1591. PMID 8576157.
- ↑ Sugiyama Y, Tomoda K, Tanaka T, Arata Y, Yoneda-Kato N, Kato J (Apr 2001). "Direct binding of the signal-transducing adaptor Grb2 facilitates down-regulation of the cyclin-dependent kinase inhibitor p27Kip1". The Journal of Biological Chemistry 276 (15): 12084–90. doi:10.1074/jbc.M010811200. PMID 11278754.
- ↑ Riordan SM, Lidder S, Williams R, Skouteris GG (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". The Biochemical Journal 350 (3): 925–32. doi:10.1042/0264-6021:3500925. PMC 1221328. PMID 10970810.
- ↑ 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". The Journal of Biological Chemistry 271 (24): 14468–72. doi:10.1074/jbc.271.24.14468. PMID 8662907.
- 1 2 Okada S, Pessin JE (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". The Journal of Biological Chemistry 271 (41): 25533–8. doi:10.1074/jbc.271.41.25533. PMID 8810325.
- 1 2 Erdreich-Epstein A, Liu M, Kant AM, Izadi KD, Nolta JA, Durden DL (Apr 1999). "Cbl functions downstream of Src kinases in Fc gamma RI signaling in primary human macrophages". Journal of Leukocyte Biology 65 (4): 523–34. PMID 10204582.
- 1 2 3 Wong A, Lamothe B, Lee A, Schlessinger J, Lax I, Li A (May 2002). "FRS2 alpha attenuates FGF receptor signaling by Grb2-mediated recruitment of the ubiquitin ligase Cbl". Proceedings of the National Academy of Sciences of the United States of America 99 (10): 6684–9. doi:10.1073/pnas.052138899. PMC 124463. PMID 11997436.
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- 1 2 3 Liu SK, McGlade CJ (Dec 1998). "Gads is a novel SH2 and SH3 domain-containing adaptor protein that binds to tyrosine-phosphorylated Shc". Oncogene 17 (24): 3073–82. doi:10.1038/sj.onc.1202337. PMID 9872323.
- 1 2 3 Park RK, Erdreich-Epstein A, Liu M, Izadi KD, Durden DL (Dec 1999). "High affinity IgG receptor activation of Src family kinases is required for modulation of the Shc-Grb2-Sos complex and the downstream activation of the nicotinamide adenine dinucleotide phosphate (reduced) oxidase". Journal of Immunology 163 (11): 6023–34. PMID 10570290.
- ↑ Jain SK, Langdon WY, Varticovski L (May 1997). "Tyrosine phosphorylation of p120cbl in BCR/abl transformed hematopoietic cells mediates enhanced association with phosphatidylinositol 3-kinase". Oncogene 14 (18): 2217–28. doi:10.1038/sj.onc.1201049. PMID 9174058.
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- ↑ Husson H, Mograbi B, Schmid-Antomarchi H, Fischer S, Rossi B (May 1997). "CSF-1 stimulation induces the formation of a multiprotein complex including CSF-1 receptor, c-Cbl, PI 3-kinase, Crk-II and Grb2". Oncogene 14 (19): 2331–8. doi:10.1038/sj.onc.1201074. PMID 9178909.
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- ↑ Ng C, Jackson RA, Buschdorf JP, Sun Q, Guy GR, Sivaraman J (Mar 2008). "Structural basis for a novel intrapeptidyl H-bond and reverse binding of c-Cbl-TKB domain substrates". The EMBO Journal 27 (5): 804–16. doi:10.1038/emboj.2008.18. PMC 2265755. PMID 18273061.
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- 1 2 Braverman LE, Quilliam LA (Feb 1999). "Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck". The Journal of Biological Chemistry 274 (9): 5542–9. doi:10.1074/jbc.274.9.5542. PMID 10026169.
- ↑ Tauchi T, Feng GS, Shen R, Hoatlin M, Bagby GC, Kabat D, Lu L, Broxmeyer HE (Mar 1995). "Involvement of SH2-containing phosphotyrosine phosphatase Syp in erythropoietin receptor signal transduction pathways". The Journal of Biological Chemistry 270 (10): 5631–5. doi:10.1074/jbc.270.10.5631. PMID 7534299.
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- ↑ Lazar DF, Knez JJ, Medof ME, Cuatrecasas P, Saltiel AR (Oct 1994). "Stimulation of glycogen synthesis by insulin in human erythroleukemia cells requires the synthesis of glycosyl-phosphatidylinositol". Proceedings of the National Academy of Sciences of the United States of America 91 (21): 9665–9. doi:10.1073/pnas.91.21.9665. PMC 44877. PMID 7524086.
- ↑ VanderKuur J, Allevato G, Billestrup N, Norstedt G, Carter-Su C (Mar 1995). "Growth hormone-promoted tyrosyl phosphorylation of SHC proteins and SHC association with Grb2". The Journal of Biological Chemistry 270 (13): 7587–93. doi:10.1074/jbc.270.13.7587. PMID 7535773.
- ↑ Kanai M, Göke M, Tsunekawa S, Podolsky DK (Mar 1997). "Signal transduction pathway of human fibroblast growth factor receptor 3. Identification of a novel 66-kDa phosphoprotein". The Journal of Biological Chemistry 272 (10): 6621–8. doi:10.1074/jbc.272.10.6621. PMID 9045692.
- 1 2 Spivak-Kroizman T, Mohammadi M, Hu P, Jaye M, Schlessinger J, Lax I (May 1994). "Point mutation in the fibroblast growth factor receptor eliminates phosphatidylinositol hydrolysis without affecting neuronal differentiation of PC12 cells". The Journal of Biological Chemistry 269 (20): 14419–23. PMID 7514169.
- ↑ Giordano V, De Falco G, Chiari R, Quinto I, Pelicci PG, Bartholomew L, Delmastro P, Gadina M, Scala G (May 1997). "Shc mediates IL-6 signaling by interacting with gp130 and Jak2 kinase". Journal of Immunology 158 (9): 4097–103. PMID 9126968.
- 1 2 Germani A, Romero F, Houlard M, Camonis J, Gisselbrecht S, Fischer S, Varin-Blank N (May 1999). "hSiah2 is a new Vav binding protein which inhibits Vav-mediated signaling pathways". Molecular and Cellular Biology 19 (5): 3798–807. PMC 84217. PMID 10207103.
- ↑ Li N, Batzer A, Daly R, Yajnik V, Skolnik E, Chardin P, Bar-Sagi D, Margolis B, Schlessinger J (May 1993). "Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling". Nature 363 (6424): 85–8. doi:10.1038/363085a0. PMID 8479541.
- ↑ Reif K, Buday L, Downward J, Cantrell DA (May 1994). "SH3 domains of the adapter molecule Grb2 complex with two proteins in T cells: the guanine nucleotide exchange protein Sos and a 75-kDa protein that is a substrate for T cell antigen receptor-activated tyrosine kinases". The Journal of Biological Chemistry 269 (19): 14081–7. PMID 8188688.
- ↑ D'Angelo G, Martini JF, Iiri T, Fantl WJ, Martial J, Weiner RI (May 1999). "16K human prolactin inhibits vascular endothelial growth factor-induced activation of Ras in capillary endothelial cells". Molecular Endocrinology 13 (5): 692–704. doi:10.1210/mend.13.5.0280. PMID 10319320.
- ↑ Tong XK, Hussain NK, de Heuvel E, Kurakin A, Abi-Jaoude E, Quinn CC, Olson MF, Marais R, Baranes D, Kay BK, McPherson PS (Mar 2000). "The endocytic protein intersectin is a major binding partner for the Ras exchange factor mSos1 in rat brain". The EMBO Journal 19 (6): 1263–71. doi:10.1093/emboj/19.6.1263. PMC 305667. PMID 10716926.
- ↑ Chin H, Saito T, Arai A, Yamamoto K, Kamiyama R, Miyasaka N, Miura O (Oct 1997). "Erythropoietin and IL-3 induce tyrosine phosphorylation of CrkL and its association with Shc, SHP-2, and Cbl in hematopoietic cells". Biochemical and Biophysical Research Communications 239 (2): 412–7. doi:10.1006/bbrc.1997.7480. PMID 9344843.
- ↑ Wan KF, Sambi BS, Tate R, Waters C, Pyne NJ (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". The Journal of Biological Chemistry 278 (20): 18658–63. doi:10.1074/jbc.M212103200. PMID 12624098.
- ↑ Kato-Stankiewicz J, Ueda S, Kataoka T, Kaziro Y, Satoh T (Jun 2001). "Epidermal growth factor stimulation of the ACK1/Dbl pathway in a Cdc42 and Grb2-dependent manner". Biochemical and Biophysical Research Communications 284 (2): 470–7. doi:10.1006/bbrc.2001.5004. PMID 11394904.
- ↑ Song C, Perides G, Liu YF (Feb 2002). "Expression of full-length polyglutamine-expanded Huntingtin disrupts growth factor receptor signaling in rat pheochromocytoma (PC12) cells". The Journal of Biological Chemistry 277 (8): 6703–7. doi:10.1074/jbc.M110338200. PMID 11733534.
- ↑ MacDonald JI, Gryz EA, Kubu CJ, Verdi JM, Meakin SO (Jun 2000). "Direct binding of the signaling adapter protein Grb2 to the activation loop tyrosines on the nerve growth factor receptor tyrosine kinase, TrkA". The Journal of Biological Chemistry 275 (24): 18225–33. doi:10.1074/jbc.M001862200. PMID 10748052.
- ↑ Song JS, Gomez J, Stancato LF, Rivera J (Oct 1996). "Association of a p95 Vav-containing signaling complex with the FcepsilonRI gamma chain in the RBL-2H3 mast cell line. Evidence for a constitutive in vivo association of Vav with Grb2, Raf-1, and ERK2 in an active complex". The Journal of Biological Chemistry 271 (43): 26962–70. doi:10.1074/jbc.271.43.26962. PMID 8900182.
- ↑ Ye ZS, Baltimore D (Dec 1994). "Binding of Vav to Grb2 through dimerization of Src homology 3 domains". Proceedings of the National Academy of Sciences of the United States of America 91 (26): 12629–33. doi:10.1073/pnas.91.26.12629. PMC 45492. PMID 7809090.
- ↑ Zeng L, Sachdev P, Yan L, Chan JL, Trenkle T, McClelland M, Welsh J, Wang LH (Dec 2000). "Vav3 mediates receptor protein tyrosine kinase signaling, regulates GTPase activity, modulates cell morphology, and induces cell transformation". Molecular and Cellular Biology 20 (24): 9212–24. doi:10.1128/mcb.20.24.9212-9224.2000. PMC 102179. PMID 11094073.
- ↑ Banin S, Truong O, Katz DR, Waterfield MD, Brickell PM, Gout I (Aug 1996). "Wiskott-Aldrich syndrome protein (WASp) is a binding partner for c-Src family protein-tyrosine kinases". Current Biology 6 (8): 981–8. doi:10.1016/s0960-9822(02)00642-5. PMID 8805332.
- ↑ She HY, Rockow S, Tang J, Nishimura R, Skolnik EY, Chen M, Margolis B, Li W (Sep 1997). "Wiskott-Aldrich syndrome protein is associated with the adapter protein Grb2 and the epidermal growth factor receptor in living cells". Molecular Biology of the Cell 8 (9): 1709–21. doi:10.1091/mbc.8.9.1709. PMC 305731. PMID 9307968.
Further reading
- Colledge M, Froehner SC (May 1998). "Interaction between the nicotinic acetylcholine receptor and Grb2. Implications for signaling at the neuromuscular junction". Annals of the New York Academy of Sciences 841: 17–27. doi:10.1111/j.1749-6632.1998.tb10907.x. PMID 9668219.
- Ramesh N, Antón IM, Martínez-Quiles N, Geha RS (Jan 1999). "Waltzing with WASP". Trends in Cell Biology 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". The International Journal of Biochemistry & Cell Biology 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". Progress in Biophysics and Molecular Biology 71 (3-4): 435–78. doi:10.1016/S0079-6107(98)00052-2. PMID 10354709.
- Vidal M, Liu WQ, Gril B, Assayag F, Poupon MF, Garbay C (2004). "[Design of new anti-tumor agents interrupting deregulated signaling pathways induced by tyrosine kinase proteins. Inhibition of protein-protein interaction involving Grb2]". Journal De La Société De Biologie 198 (2): 133–7. PMID 15368963.
External links
- GRB2 Adaptor Protein at the US National Library of Medicine Medical Subject Headings (MeSH)
- The Grb2 protein page on The SH2 Website
- GeneCards entry for Grb2
- Human Protein Resource Database entry for Grb2
- Grb2 information on iHOP (Information Hyperlinked over Proteins)
- GRB2 Info with links in the Cell Migration Gateway
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