GRB2
PDBに登録されている構造
PDBオルソログ検索: RCSB PDBe PDBj
PDBのIDコード一覧

1AZE, 1BM2, 1BMB, 1CJ1, 1FHS, 1FYR, 1GCQ, 1GFC, 1GFD, 1GHU, 1GRI, 1IO6, 1JYQ, 1JYR, 1JYU, 1QG1, 1TZE, 1X0N, 1ZFP, 2AOA, 2AOB, 2H5K, 2HUW, 2VVK, 2VWF, 2W0Z, 3C7I, 3IMD, 3IMJ, 3IN7, 3IN8, 3KFJ, 3MXC, 3MXY, 3N7Y, 3N84, 3N8M, 3OV1, 3OVE, 3S8L, 3S8N, 3S8O, 2H46, 3WA4, 4P9V, 4P9Z, 5CDW

識別子
記号GRB2, ASH, EGFRBP-Grb3-3, MST084, MSTP084, NCKAP2, growth factor receptor bound protein 2
外部IDOMIM: 108355 MGI: 95805 HomoloGene: 1576 GeneCards: GRB2
遺伝子の位置 (ヒト)
17番染色体 (ヒト)
染色体17番染色体 (ヒト)[1]
17番染色体 (ヒト)
GRB2遺伝子の位置
GRB2遺伝子の位置
バンドデータ無し開始点75,318,076 bp[1]
終点75,405,709 bp[1]
遺伝子の位置 (マウス)
11番染色体 (マウス)
染色体11番染色体 (マウス)[2]
11番染色体 (マウス)
GRB2遺伝子の位置
GRB2遺伝子の位置
バンドデータ無し開始点115,534,871 bp[2]
終点115,599,423 bp[2]
RNA発現パターン
さらなる参照発現データ
遺伝子オントロジー
分子機能• protein domain specific binding
• SH3 domain binding
• プロテインキナーゼ結合
• identical protein binding
• neurotrophin TRKA receptor binding
• protein phosphatase binding
• 血漿タンパク結合
• ephrin receptor binding
• insulin receptor substrate binding
• epidermal growth factor receptor binding
• phosphatidylinositol-4,5-bisphosphate 3-kinase activity
• 1-phosphatidylinositol-3-kinase activity
• phosphoprotein binding
• 酵素結合
• RNA結合
• non-membrane spanning protein tyrosine kinase activity
• phosphotyrosine residue binding
細胞の構成要素• エキソソーム
• 核小体
• 細胞質
• 核質
• COP9シグナロソーム
• ゴルジ体
• 細胞質基質
• 細胞核
• cell-cell junction
• 膜
• Grb2-EGFR complex
• エンドソーム
• vesicle membrane
• 細胞膜
• extrinsic component of cytoplasmic side of plasma membrane
• 高分子複合体
• 細胞内
生物学的プロセス• T cell costimulation
• Fc-gamma receptor signaling pathway involved in phagocytosis
• branching involved in labyrinthine layer morphogenesis
• MAPK cascade
• epidermal growth factor receptor signaling pathway
• fibroblast growth factor receptor signaling pathway
• insulin receptor signaling pathway
• receptor internalization
• 細胞間シグナル伝達
• 軸索誘導
• positive regulation of reactive oxygen species metabolic process
• cellular response to ionizing radiation
• Fc-epsilon receptor signaling pathway
• viral process
• positive regulation of actin filament polymerization
• signal transduction in response to DNA damage
• negative regulation of epidermal growth factor receptor signaling pathway
• leukocyte migration
• regulation of MAPK cascade
• anatomical structure formation involved in morphogenesis
• 老化
• ERBB2 signaling pathway
• phosphatidylinositol phosphate biosynthetic process
• phosphatidylinositol-3-phosphate biosynthetic process
• protein heterooligomerization
• entry of bacterium into host cell
• membrane organization
• 遊走
• 細胞分化
• peptidyl-tyrosine autophosphorylation
• regulation of cell population proliferation
• 自然免疫
• Ras protein signal transduction
• interleukin-15-mediated signaling pathway
• positive regulation of protein kinase B signaling
• regulation of molecular function
• サイトカイン媒介シグナル伝達経路
• positive regulation of Ras protein signal transduction
• neurotrophin TRK receptor signaling pathway
出典:Amigo / QuickGO
オルソログ
種ヒトマウス
Entrez

2885

14784

Ensembl

ENSG00000177885

ENSMUSG00000059923

UniProt

P62993,J3KT38

Q60631

RefSeq
(mRNA)

NM_203506
NM_002086

NM_008163
NM_001313936
NM_001313937

RefSeq
(タンパク質)

NP_002077
NP_987102

NP_001300865
NP_001300866
NP_032189

場所
(UCSC)		Chr 17: 75.32 – 75.41 MbChr 17: 115.53 – 115.6 Mb
PubMed検索[3][4]
ウィキデータ
閲覧/編集 ヒト閲覧/編集 マウス

GRB2（growth factor receptor bound protein 2）は、シグナル伝達に関与するアダプタータンパク質である。ヒトでは、GRB2タンパク質はGRB2遺伝子によってコードされている[5][6]。

GRB2は上皮成長因子受容体などの受容体に結合するタンパク質で、1つのSH2ドメインと2つのSH3ドメインを有する。2つのSH3ドメインは他のタンパク質のプロリンリッチ領域と直接的に相互作用して複合体形成へ差し向け、SH2ドメインはリン酸化されたチロシンを含む配列に結合する。GRB2遺伝子はCaenorhabditis elegansにおいてシグナル伝達経路に関与しているsem-5遺伝子と類似している。GRB2遺伝子には、異なるアイソフォームをコードする2種類の選択的スプライシングバリアントが発見されている[7]。

機能

GRB2は複数の細胞機能に必要不可欠な役割を果たしている。GRB2の機能の阻害によって、さまざまな生物種で発生過程が損なわれ、またさまざまな細胞種で形質転換や増殖が遮断される。GRB2は上皮成長因子受容体と、Rasやその下流のキナーゼであるERK1/2とを関連づける役割が最もよく知られている。一方で、GRB2はHER2の場合には他のキナーゼAKTに対して関連づける。このように、さまざまな受容体型チロシンキナーゼのシグナルがGRB2へ収束する可能性があるものの、これらのシグナルは必ずしも同じ下流キナーゼの活性化を引き起こすためにGRB2を利用しているわけではない[8]。

ドメイン

GRB2はSH2ドメインの両側にSH3ドメインが隣接した構成をしている[9]。

GRB2のSH2ドメインは、受容体やアダプタータンパク質に存在するリン酸化チロシン（pY）含有モチーフに結合する。pY-X-N-X配列（Xは任意のアミノ酸）に対して選択的に結合するが、pY-(L/V)-N-(V/P)配列に対してより高い親和性で結合する[10]。

N末端側のSH3ドメインはプロリンに富むペプチドに結合し、Rasのグアニンヌクレオチド交換因子であるSos（英語版）に結合することができる[11]。

C末端側のSH3ドメインはP-X-X-X-Rモチーフを有するペプチドに結合し、GAB1（英語版）などのタンパク質への特異的結合を可能にしている[12]。

相互作用

GRB2は次に挙げる因子と相互作用することが示されている。

出典

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000177885 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000059923 - Ensembl, May 2017
  3. ↑ Human PubMed Reference:
  4. ↑ Mouse PubMed Reference:
  5. ↑ “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. (Oct 1992). Bibcode: 1992PNAS...89.9015M. doi:10.1073/pnas.89.19.9015. PMC 50055. PMID 1384039.
  6. 1 2 “The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling”. Cell 70 (3): 431–42. (Aug 1992). doi:10.1016/0092-8674(92)90167-B. PMID 1322798.
  7. ↑ “Entrez Gene: GRB2 growth factor receptor-bound protein 2”. 2024年9月29日閲覧。
  8. ↑ Tari, A. M.; Lopez-Berestein, G. (2001-10). “GRB2: a pivotal protein in signal transduction”. Seminars in Oncology 28 (5 Suppl 16): 142–147. doi:10.1016/s0093-7754(01)90291-x. ISSN 0093-7754. PMID 11706405.
  9. ↑ Yablonski, Deborah (2019). “Bridging the Gap: Modulatory Roles of the Grb2-Family Adaptor, Gads, in Cellular and Allergic Immune Responses”. Frontiers in Immunology 10: 1704. doi:10.3389/fimmu.2019.01704. ISSN 1664-3224. PMC 6669380. PMID 31402911.
  10. ↑ Higo, Kunitake; Ikura, Teikichi; Oda, Masayuki; Morii, Hisayuki; Takahashi, Jun; Abe, Ryo; Ito, Nobutoshi (2013). “High resolution crystal structure of the Grb2 SH2 domain with a phosphopeptide derived from CD28”. PloS One 8 (9): e74482. doi:10.1371/journal.pone.0074482. ISSN 1932-6203. PMC 3787023. PMID 24098653.
  11. ↑ Ogura, Kenji; Okamura, Hideyasu (2013-10-09). “Conformational change of Sos-derived proline-rich peptide upon binding Grb2 N-terminal SH3 domain probed by NMR”. Scientific Reports 3: 2913. doi:10.1038/srep02913. ISSN 2045-2322. PMC 6505672. PMID 24105423.
  12. ↑ Lock, L. S.; Royal, I.; Naujokas, M. A.; Park, M. (2000-10-06). “Identification of an atypical Grb2 carboxyl-terminal SH3 domain binding site in Gab docking proteins reveals Grb2-dependent and -independent recruitment of Gab1 to receptor tyrosine kinases”. The Journal of Biological Chemistry 275 (40): 31536–31545. doi:10.1074/jbc.M003597200. ISSN 0021-9258. PMID 10913131.
  13. ↑ “Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases”. The Journal of Biological Chemistry 277 (7): 4999–5007. (Feb 2002). doi:10.1074/jbc.M107430200. PMID 11741929.
  14. ↑ “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. (Dec 1997). doi:10.1074/jbc.272.52.33260. PMID 9407116.
  15. ↑ “Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites”. Genes & Development 8 (7): 783–95. (Apr 1994). doi:10.1101/gad.8.7.783. PMID 7926767.
  16. ↑ “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. (Sep 1995). doi:10.1006/abio.1995.1444. PMID 8585605.
  17. ↑ “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. (Sep 1994). doi:10.1016/S0021-9258(19)51063-8. PMID 7929073.
  18. ↑ “BLNK: a central linker protein in B cell activation”. Immunity 9 (1): 93–103. (Jul 1998). doi:10.1016/S1074-7613(00)80591-9. PMID 9697839.
  19. ↑ “Association of SLP-65/BLNK with the B cell antigen receptor through a non-ITAM tyrosine of Ig-alpha”. European Journal of Immunology 31 (7): 2126–34. (Jul 2001). doi:10.1002/1521-4141(200107)31:7<2126::aid-immu2126>3.0.co;2-o. PMID 11449366.
  20. ↑ “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. (May 2000). doi:10.1002/(sici)1521-4141(200005)30:5<1326::aid-immu1326>3.0.co;2-q. PMID 10820378.
  21. ↑ “SLP-65: a new signaling component in B lymphocytes which requires expression of the antigen receptor for phosphorylation”. The Journal of Experimental Medicine 188 (4): 791–5. (Aug 1998). doi:10.1084/jem.188.4.791. PMC 2213353. PMID 9705962.
  22. 1 2 “Protein tyrosine phosphatase-PEST regulates focal adhesion disassembly, migration, and cytokinesis in fibroblasts”. The Journal of Cell Biology 144 (5): 1019–31. (Mar 1999). doi:10.1083/jcb.144.5.1019. PMC 2148201. PMID 10085298.
  23. ↑ “Specific inhibition of FGF-induced MAPK activation by the receptor-like protein tyrosine phosphatase LAR”. Oncogene 19 (19): 2346–53. (May 2000). doi:10.1038/sj.onc.1203558. PMID 10822386.
  24. 1 2 3 “A direct binding site for Grb2 contributes to transformation and leukemogenesis by the Tel-Abl (ETV6-Abl) tyrosine kinase”. Molecular and Cellular Biology 24 (11): 4685–95. (Jun 2004). doi:10.1128/MCB.24.11.4685-4695.2004. PMC 416425. PMID 15143164.
  25. 1 2 3 “Bcr-Abl oncoproteins bind directly to activators of the Ras signalling pathway”. The EMBO Journal 13 (4): 764–73. (Feb 1994). doi:10.1002/j.1460-2075.1994.tb06319.x. PMC 394874. PMID 8112292.
  26. ↑ “The Grb2 binding site is required for the induction of chronic myeloid leukemia-like disease in mice by the Bcr/Abl tyrosine kinase”. Blood 96 (2): 664–70. (Jul 2000). doi:10.1182/blood.V96.2.664. PMID 10887132.
  27. ↑ “The SH2-containing adapter protein GRB10 interacts with BCR-ABL”. Oncogene 17 (8): 941–8. (Aug 1998). doi:10.1038/sj.onc.1202024. PMID 9747873.
  28. ↑ “Bcr phosphorylated on tyrosine 177 binds Grb2”. Oncogene 14 (19): 2367–72. (May 1997). doi:10.1038/sj.onc.1201053. PMID 9178913.
  29. ↑ “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. (Feb 1995). doi:10.1128/mcb.15.2.835. PMC 231961. PMID 7529874.
  30. ↑ “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. (Dec 1998). doi:10.1074/jbc.273.49.33035. PMID 9830057.
  31. ↑ “Specific uncoupling of GRB2 from the Met receptor. Differential effects on transformation and motility”. The Journal of Biological Chemistry 271 (24): 14119–23. (Jun 1996). doi:10.1074/jbc.271.24.14119. PMID 8662889.
  32. ↑ “Signaling by HGF and KGF in corneal epithelial cells: Ras/MAP kinase and Jak-STAT pathways”. Investigative Ophthalmology & Visual Science 39 (8): 1329–38. (Jul 1998). PMID 9660480.
  33. 1 2 “cbl-b inhibits epidermal growth factor receptor signaling”. Oncogene 18 (10): 1855–66. (Mar 1999). doi:10.1038/sj.onc.1202499. PMID 10086340.
  34. ↑ “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. (Jun 1998). doi:10.1074/jbc.273.24.14962. PMID 9614102.
  35. ↑ “Tyrosine phosphorylation and complex formation of Cbl-b upon T cell receptor stimulation”. Oncogene 18 (5): 1147–56. (Feb 1999). doi:10.1038/sj.onc.1202411. PMID 10022120.
  36. 1 2 “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. (May 1996). doi:10.1074/jbc.271.21.12129. PMID 8647802.
  37. ↑ “Socs1 binds to multiple signalling proteins and suppresses steel factor-dependent proliferation”. The EMBO Journal 18 (4): 904–15. (Feb 1999). doi:10.1093/emboj/18.4.904. PMC 1171183. PMID 10022833.
  38. ↑ “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. (Jul 1999). doi:10.1042/0264-6021:3410211. PMC 1220349. PMID 10377264.
  39. ↑ “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. (Jun 2000). doi:10.1074/jbc.M001892200. PMID 10748054.
  40. ↑ “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. (Nov 2001). doi:10.1074/jbc.M105446200. PMID 11551923.
  41. ↑ “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. (Aug 1998). doi:10.1074/jbc.273.33.21194. PMID 9694876.
  42. ↑ “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. (Jan 1996). doi:10.1074/jbc.271.3.1591. PMID 8576157.
  43. ↑ “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. (Apr 2001). doi:10.1074/jbc.M010811200. PMID 11278754.
  44. ↑ “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. (Sep 2000). doi:10.1042/0264-6021:3500925. PMC 1221328. PMID 10970810.
  45. ↑ “Interaction between the amino-terminal SH3 domain of CRK and its natural target proteins”. The Journal of Biological Chemistry 271 (24): 14468–72. (Jun 1996). doi:10.1074/jbc.271.24.14468. PMID 8662907.
  46. 1 2 “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. (Oct 1996). doi:10.1074/jbc.271.41.25533. PMID 8810325.
  47. 1 2 “Cbl functions downstream of Src kinases in Fc gamma RI signaling in primary human macrophages”. Journal of Leukocyte Biology 65 (4): 523–34. (Apr 1999). doi:10.1002/jlb.65.4.523. PMID 10204582.
  48. 1 2 3 “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. (May 2002). Bibcode: 2002PNAS...99.6684W. doi:10.1073/pnas.052138899. PMC 124463. PMID 11997436.
  49. 1 2 3 4 5 6 “Differential effect of the inhibition of Grb2-SH3 interactions in platelet activation induced by thrombin and by Fc receptor engagement”. The Biochemical Journal 363 (Pt 3): 717–25. (May 2002). doi:10.1042/0264-6021:3630717. PMC 1222524. PMID 11964172.
  50. 1 2 3 “Gads is a novel SH2 and SH3 domain-containing adaptor protein that binds to tyrosine-phosphorylated Shc”. Oncogene 17 (24): 3073–82. (Dec 1998). doi:10.1038/sj.onc.1202337. PMID 9872323.
  51. 1 2 3 “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. (Dec 1999). doi:10.4049/jimmunol.163.11.6023. PMID 10570290.
  52. ↑ “Tyrosine phosphorylation of p120cbl in BCR/abl transformed hematopoietic cells mediates enhanced association with phosphatidylinositol 3-kinase”. Oncogene 14 (18): 2217–28. (May 1997). doi:10.1038/sj.onc.1201049. PMID 9174058.
  53. ↑ “A c-Cbl yeast two hybrid screen reveals interactions with 14-3-3 isoforms and cytoskeletal components”. Biochemical and Biophysical Research Communications 240 (1): 46–50. (Nov 1997). doi:10.1006/bbrc.1997.7608. PMID 9367879.
  54. ↑ “The protein product of the c-cbl protooncogene is the 120-kDa tyrosine-phosphorylated protein in Jurkat cells activated via the T cell antigen receptor”. The Journal of Biological Chemistry 269 (37): 22921–4. (Sep 1994). doi:10.1016/S0021-9258(17)31595-8. PMID 8083187.
  55. ↑ “Interleukin-2 stimulation induces tyrosine phosphorylation of p120-Cbl and CrkL and formation of multimolecular signaling complexes in T lymphocytes and natural killer cells”. The Journal of Biological Chemistry 273 (7): 3986–93. (Feb 1998). doi:10.1074/jbc.273.7.3986. PMID 9461587.
  56. ↑ “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. (May 1997). doi:10.1038/sj.onc.1201074. PMID 9178909.
  57. ↑ “Purification and molecular cloning of SH2- and SH3-containing inositol polyphosphate-5-phosphatase, which is involved in the signaling pathway of granulocyte-macrophage colony-stimulating factor, erythropoietin, and Bcr-Abl”. Blood 89 (8): 2745–56. (Apr 1997). doi:10.1182/blood.V89.8.2745. PMID 9108392.
  58. ↑ “Structural basis for a novel intrapeptidyl H-bond and reverse binding of c-Cbl-TKB domain substrates”. The EMBO Journal 27 (5): 804–16. (Mar 2008). doi:10.1038/emboj.2008.18. PMC 2265755. PMID 18273061.
  59. ↑ “Identification of a second Grb2 binding site in the v-Fms tyrosine kinase”. Oncogene 15 (13): 1565–72. (Sep 1997). doi:10.1038/sj.onc.1201518. PMID 9380408.
  60. ↑ “Identification of a novel 135-kDa Grb2-binding protein in osteoclasts”. The Journal of Biological Chemistry 271 (51): 33141–7. (Dec 1996). doi:10.1074/jbc.271.51.33141. PMID 8955163.
  61. ↑ “Association of Ash/Grb-2 with dynamin through the Src homology 3 domain”. The Journal of Biological Chemistry 269 (8): 5489–92. (Feb 1994). doi:10.1016/S0021-9258(17)37484-7. PMID 8119878.
  62. 1 2 “Multiple Grb2-protein complexes in human cancer cells”. International Journal of Cancer 70 (2): 208–13. (Jan 1997). doi:10.1002/(sici)1097-0215(19970117)70:2<208::aid-ijc12>3.0.co;2-e. PMID 9009162.
  63. ↑ “Differential regulation of cell motility and invasion by FAK”. The Journal of Cell Biology 160 (5): 753–67. (Mar 2003). doi:10.1083/jcb.200212114. PMC 2173366. PMID 12615911.
  64. ↑ “DOCK180, a major CRK-binding protein, alters cell morphology upon translocation to the cell membrane”. Molecular and Cellular Biology 16 (4): 1770–6. (Apr 1996). doi:10.1128/mcb.16.4.1770. PMC 231163. PMID 8657152.
  65. ↑ “SH3 domain-mediated interaction of dystroglycan and Grb2”. The Journal of Biological Chemistry 270 (20): 11711–4. (May 1995). doi:10.1074/jbc.270.20.11711. PMID 7744812.
  66. ↑ “Activation of the EphA2 tyrosine kinase stimulates the MAP/ERK kinase signaling cascade”. Oncogene 21 (50): 7690–9. (Oct 2002). doi:10.1038/sj.onc.1205758. PMID 12400011.
  67. 1 2 3 4 “UCS15A, a novel small molecule, SH3 domain-mediated protein-protein interaction blocking drug”. Oncogene 21 (13): 2037–50. (Mar 2002). doi:10.1038/sj.onc.1205271. PMID 11960376.
  68. 1 2 3 4 5 “A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling”. Nature Biotechnology 21 (3): 315–8. (Mar 2003). doi:10.1038/nbt790. PMID 12577067.
  69. 1 2 “Phosphotyrosine interactome of the ErbB-receptor kinase family”. Molecular Systems Biology 1: E1–E13. (2005). doi:10.1038/msb4100012. PMC 1681463. PMID 16729043.
  70. ↑ “A differential requirement for the COOH-terminal region of the epidermal growth factor (EGF) receptor in amphiregulin and EGF mitogenic signaling”. The Journal of Biological Chemistry 274 (13): 8900–9. (Mar 1999). doi:10.1074/jbc.274.13.8900. PMID 10085134.
  71. ↑ “Grb2/Ash binds directly to tyrosines 1068 and 1086 and indirectly to tyrosine 1148 of activated human epidermal growth factor receptors in intact cells”. The Journal of Biological Chemistry 269 (49): 31310–4. (Dec 1994). doi:10.1016/S0021-9258(18)47424-8. hdl:20.500.14094/D2001922. PMID 7527043.
  72. 1 2 “The RIalpha subunit of protein kinase A (PKA) binds to Grb2 and allows PKA interaction with the activated EGF-receptor”. Oncogene 14 (8): 923–8. (Feb 1997). doi:10.1038/sj.onc.1200906. PMID 9050991.
  73. ↑ “Cloning and characterization of GRB14, a novel member of the GRB7 gene family”. The Journal of Biological Chemistry 271 (21): 12502–10. (May 1996). doi:10.1074/jbc.271.21.12502. PMID 8647858.
  74. 1 2 “A complex of Grb2 adaptor protein, Sos exchange factor, and a 36-kDa membrane-bound tyrosine phosphoprotein is implicated in ras activation in T cells”. The Journal of Biological Chemistry 269 (12): 9019–23. (Mar 1994). doi:10.1016/S0021-9258(17)37070-9. PMID 7510700.
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