Receptor epidermalnog faktora rasta

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Receptor epidermalnog faktora rasta

Extracellular domain of Epidermal growth factor receptor in complex with EGF. PDB 1nql[1]
Dostupne strukture
1IVO, 1M14, 1M17, 1MOX, 1NQL, 1XKK, 1YY9, 1Z9I, 2EB2, 2EB3, 2GS2, 2GS7, 2ITN, 2ITO, 2ITP, 2ITQ, 2ITT, 2ITU, 2ITV, 2ITW, 2ITX, 2ITY, 2ITZ, 2J5E, 2J5F, 2J6M, 2JIT, 2JIU, 2JIV, 2KS1, 2M0B, 2M20, 2RF9, 2RFD, 2RFE, 2RGP, 3B2U, 3B2V, 3BEL, 3BUO, 3C09, 3G5V, 3G5Y, 3GOP, 3GT8, 3IKA, 3LZB, 3NJP, 3OB2, 3OP0, 3P0Y, 3PFV, 3POZ, 3QWQ, 3UG1, 3UG2, 3VJN, 3VJO, 3VRP, 3VRR, 3W2O, 3W2P, 3W2Q, 3W2R, 3W2S, 3W32, 3W33, 4G5J, 4G5P, 4HJO, 4I1Z, 4I20, 4I21, 4I22, 4I23, 4I24, 4JQ7, 4JQ8, 4JR3, 4JRV, 4KRL, 4KRM, 4KRO, 4KRP, 4LI5, 4LL0
Identifikatori
SimboliEGFR; ERBB; ERBB1; HER1; PIG61; mENA
Vanjski IDOMIM: 131550 MGI: 95294 HomoloGene: 74545 GeneCards: EGFR Gene
EC broj2.7.10.1
Pregled RNK izražavanja
podaci
Ortolozi
VrstaČovekMiš
Entrez195613649
EnsemblENSG00000146648ENSMUSG00000020122
UniProtP00533Q01279
RefSeq (mRNA)NM_005228NM_007912
RefSeq (protein)NP_005219NP_031938
Lokacija (UCSC)Chr 7:
55.09 - 55.32 Mb		Chr 11:
16.75 - 16.92 Mb
PubMed pretraga[1][2]

Receptor epidermalnog faktora rasta (EGFR; ErbB-1; HER1 kod ljudi) je receptor ćelijske površine članova familije epidermalnih faktora rasta (EGF-familija) ekstracelularnih proteina liganda.[2]

Receptor epidermalnog faktora rasta je član ErbB familije receptora, subfamilije sa četiri blisko srodna receptora tirozinske kinaze: EGFR (ErbB-1), HER2/c-neu (ErbB-2), Her 3 (ErbB-3) i Her 4 (ErbB-4). Mutacije koje utiču na izražavanje ili aktivnost EGFR mogu da dovedu do kancera.[3]

Epidermalni faktor rasta i njegov receptor je otkrio Stanli Kohen na Vanderbilt univerzitetu. Kohen je podelio Nobelovu nagradu za fiziologiju ili medicinu 1986. sa Ritom Levi-Montalcini za njihovo otkriće faktora rasta.

Patologija[uredi | uredi kod]

Mutacije zametka[uredi | uredi kod]

  • V843I : Predispozicija za rak pluća[4]

Interakcija[uredi | uredi kod]

Poznato je da receptor epidermalnog faktora rasta formira interakcije sa:

Reference[uredi | uredi kod]

  1. ↑ Ferguson Km, B. M.; Berger, M. B.; Mendrola, J. M.; Cho, H. S.; Leahy, D. J.; Lemmon, M. A. (2003). „EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization”. Molecular Cell 11 (2): 507–517. DOI:10.1016/S1097-2765(03)00047-9. PMID 12620237.  edit
  2. ↑ Herbst RS (2004). „Review of epidermal growth factor receptor biology”. Int. J. Radiat. Oncol. Biol. Phys. 59 (2 Suppl): 21–6. DOI:10.1016/j.ijrobp.2003.11.041. PMID 15142631. 
  3. ↑ Zhang H, Berezov A, Wang Q, Zhang G, Drebin J, Murali R, Greene MI (August 2007). „ErbB receptors: from oncogenes to targeted cancer therapies”. J. Clin. Invest. 117 (8): 2051–8. DOI:10.1172/JCI32278. PMC 1934579. PMID 17671639. 
  4. ↑ Ikeda, K; Nomori, H; Mori, T; Sasaki, J; Kobayashi, T (2008). „Novel germline mutation: EGFR V843I in patient with multiple lung adenocarcinomas and family members with lung cancer”. The Annals of Thoracic Surgery 85 (4): 1430-2. DOI:10.1016/j.athoracsur.2007.10.012. PMID 18355544.  edit
  5. ↑ Bonaccorsi L, Carloni Vinicio, Muratori Monica, Formigli Lucia, Zecchi Sandra, Forti Gianni, Baldi Elisabetta (Oct 2004). „EGF receptor (EGFR) signaling promoting invasion is disrupted in androgen-sensitive prostate cancer cells by an interaction between EGFR and androgen receptor (AR)”. Int. J. Cancer 112 (1): 78–86. DOI:10.1002/ijc.20362. PMID 15305378. 
  6. ↑ Bonaccorsi L, Muratori M, Carloni V, Marchiani S, Formigli L, Forti G, Baldi E (Aug 2004). „The androgen receptor associates with the epidermal growth factor receptor in androgen-sensitive prostate cancer cells”. Steroids 69 (8-9): 549–52. DOI:10.1016/j.steroids.2004.05.011. PMID 15288768. 
  7. ↑ Kim S-W, Hayashi Masaaki, Lo Jeng-Fan, Yang Young, Yoo Jin-San, Lee Jiing-Dwan (Jan 2003). „ADP-ribosylation factor 4 small GTPase mediates epidermal growth factor receptor-dependent phospholipase D2 activation”. J. Biol. Chem. 278 (4): 2661–8. DOI:10.1074/jbc.M205819200. PMID 12446727. 
  8. ↑ 8,0 8,1 Couet J, Sargiacomo M, Lisanti M P (Nov 1997). „Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities”. J. Biol. Chem. 272 (48): 30429–38. DOI:10.1074/jbc.272.48.30429. PMID 9374534. 
  9. ↑ 9,0 9,1 Tvorogov D, Carpenter Graham (Jul 2002). „EGF-dependent association of phospholipase C-gamma1 with c-Cbl”. Exp. Cell Res. 277 (1): 86–94. DOI:10.1006/excr.2002.5545. PMID 12061819. 
  10. ↑ 10,0 10,1 Ettenberg SA, Keane M M, Nau M M, Frankel M, Wang L M, Pierce J H, Lipkowitz S (Mar 1999). „cbl-b inhibits epidermal growth factor receptor signaling”. Oncogene 18 (10): 1855–66. DOI:10.1038/sj.onc.1202499. PMID 10086340. 
  11. ↑ 11,0 11,1 Pennock S, Wang Zhixiang (May 2008). „A tale of two Cbls: interplay of c-Cbl and Cbl-b in epidermal growth factor receptor downregulation”. Mol. Cell. Biol. 28 (9): 3020–37. DOI:10.1128/MCB.01809-07. PMC 2293090. PMID 18316398. 
  12. ↑ 12,0 12,1 Umebayashi K, Stenmark Harald, Yoshimori Tamotsu (Aug 2008). „Ubc4/5 and c-Cbl continue to ubiquitinate EGF receptor after internalization to facilitate polyubiquitination and degradation”. Mol. Biol. Cell 19 (8): 3454–62. DOI:10.1091/mbc.E07-10-0988. PMC 2488299. PMID 18508924. 
  13. ↑ Ng C, Jackson Rebecca A, Buschdorf Jan P, Sun Qingxiang, Guy Graeme R, Sivaraman J (Mar 2008). „Structural basis for a novel intrapeptidyl H-bond and reverse binding of c-Cbl-TKB domain substrates”. EMBO J. 27 (5): 804–16. DOI:10.1038/emboj.2008.18. PMC 2265755. PMID 18273061. 
  14. ↑ 14,0 14,1 14,2 14,3 14,4 14,5 Schulze WX, Deng Lei, Mann Matthias (2005). „Phosphotyrosine interactome of the ErbB-receptor kinase family”. Mol. Syst. Biol. 1 (1): 2005.0008. DOI:10.1038/msb4100012. PMC 1681463. PMID 16729043. 
  15. ↑ Kim M, Tezuka T, Suziki Y, Sugano S, Hirai M, Yamamoto T (Oct 1999). „Molecular cloning and characterization of a novel cbl-family gene, cbl-c”. Gene 239 (1): 145–54. DOI:10.1016/S0378-1119(99)00356-X. PMID 10571044. 
  16. ↑ Keane MM, Ettenberg S A, Nau M M, Banerjee P, Cuello M, Penninger J, Lipkowitz S (Jun 1999). „cbl-3: a new mammalian cbl family protein”. Oncogene 18 (22): 3365–75. DOI:10.1038/sj.onc.1202753. PMID 10362357. 
  17. ↑ Wang Z, Wang Meifang, Lazo John S, Carr Brian I (May 2002). „Identification of epidermal growth factor receptor as a target of Cdc25A protein phosphatase”. J. Biol. Chem. 277 (22): 19470–5. DOI:10.1074/jbc.M201097200. PMID 11912208. 
  18. ↑ Hashimoto Y, Katayama H, Kiyokawa E, Ota S, Kurata T, Gotoh N, Otsuka N, Shibata M, Matsuda M (Jul 1998). „Phosphorylation of CrkII adaptor protein at tyrosine 221 by epidermal growth factor receptor”. J. Biol. Chem. 273 (27): 17186–91. DOI:10.1074/jbc.273.27.17186. PMID 9642287. 
  19. ↑ Hazan RB, Norton L (Apr 1998). „The epidermal growth factor receptor modulates the interaction of E-cadherin with the actin cytoskeleton”. J. Biol. Chem. 273 (15): 9078–84. DOI:10.1074/jbc.273.15.9078. PMID 9535896. 
  20. ↑ Schroeder JA, Adriance Melissa C, McConnell Elizabeth J, Thompson Melissa C, Pockaj Barbara, Gendler Sandra J (Jun 2002). „ErbB-beta-catenin complexes are associated with human infiltrating ductal breast and murine mammary tumor virus (MMTV)-Wnt-1 and MMTV-c-Neu transgenic carcinomas”. J. Biol. Chem. 277 (25): 22692–8. DOI:10.1074/jbc.M201975200. PMID 11950845. 
  21. ↑ Takahashi K, Suzuki K, Tsukatani Y (Jul 1997). „Induction of tyrosine phosphorylation and association of beta-catenin with EGF receptor upon tryptic digestion of quiescent cells at confluence”. Oncogene 15 (1): 71–8. DOI:10.1038/sj.onc.1201160. PMID 9233779. 
  22. ↑ Santra M, Reed Charles C, Iozzo Renato V (Sep 2002). „Decorin binds to a narrow region of the epidermal growth factor (EGF) receptor, partially overlapping but distinct from the EGF-binding epitope”. J. Biol. Chem. 277 (38): 35671–81. DOI:10.1074/jbc.M205317200. PMID 12105206. 
  23. ↑ Iozzo RV, Moscatello D K, McQuillan D J, Eichstetter I (Feb 1999). „Decorin is a biological ligand for the epidermal growth factor receptor”. J. Biol. Chem. 274 (8): 4489–92. DOI:10.1074/jbc.274.8.4489. PMID 9988678. 
  24. ↑ 24,0 24,1 Wong L, Deb T B, Thompson S A, Wells A, Johnson G R (Mar 1999). „A differential requirement for the COOH-terminal region of the epidermal growth factor (EGF) receptor in amphiregulin and EGF mitogenic signaling”. J. Biol. Chem. 274 (13): 8900–9. DOI:10.1074/jbc.274.13.8900. PMID 10085134. 
  25. ↑ Stortelers C, Souriau Christelle, van Liempt Ellis, van de Poll Monique L M, van Zoelen Everardus J J (Jul 2002). „Role of the N-terminus of epidermal growth factor in ErbB-2/ErbB-3 binding studied by phage display”. Biochemistry 41 (27): 8732–41. DOI:10.1021/bi025878c. PMID 12093292. 
  26. ↑ 26,0 26,1 Daly RJ, Sanderson G M, Janes P W, Sutherland R L (May 1996). „Cloning and characterization of GRB14, a novel member of the GRB7 gene family”. J. Biol. Chem. 271 (21): 12502–10. DOI:10.1074/jbc.271.21.12502. PMID 8647858. 
  27. ↑ 27,0 27,1 27,2 Braverman LE, Quilliam L A (Feb 1999). „Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck”. J. Biol. Chem. 274 (9): 5542–9. DOI:10.1074/jbc.274.9.5542. PMID 10026169. 
  28. ↑ Blagoev B, 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. 21 (3): 315–8. DOI:10.1038/nbt790. PMID 12577067. 
  29. ↑ Oneyama C, Nakano Hirofumi, Sharma Sreenath V (Mar 2002). „UCS15A, a novel small molecule, SH3 domain-mediated protein-protein interaction blocking drug”. Oncogene 21 (13): 2037–50. DOI:10.1038/sj.onc.1205271. PMID 11960376. 
  30. ↑ Okutani T, Okabayashi Y, Kido Y, Sugimoto Y, Sakaguchi K, Matuoka K, Takenawa T, Kasuga M (Dec 1994). „Grb2/Ash binds directly to tyrosines 1068 and 1086 and indirectly to tyrosine 1148 of activated human epidermal growth factor receptors in intact cells”. J. Biol. Chem. 269 (49): 31310–4. PMID 7527043. 
  31. ↑ Tortora G, Damiano V, Bianco C, Baldassarre G, Bianco A R, Lanfrancone L, Pelicci P G, Ciardiello F (Feb 1997). „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. DOI:10.1038/sj.onc.1200906. PMID 9050991. 
  32. ↑ 32,0 32,1 Buday L, Egan S E, Rodriguez Viciana P, Cantrell D A, Downward J (Mar 1994). „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”. J. Biol. Chem. 269 (12): 9019–23. PMID 7510700. 
  33. ↑ Lowenstein EJ, Daly R J, Batzer A G, Li W, Margolis B, Lammers R, Ullrich A, Skolnik E Y, 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. 
  34. ↑ 34,0 34,1 34,2 34,3 34,4 Olayioye MA, Beuvink I, Horsch K, Daly J M, Hynes N E (Jun 1999). „ErbB receptor-induced activation of stat transcription factors is mediated by Src tyrosine kinases”. J. Biol. Chem. 274 (24): 17209–18. DOI:10.1074/jbc.274.24.17209. PMID 10358079. 
  35. ↑ Schroeder JA, Thompson M C, Gardner M M, Gendler S J (Apr 2001). „Transgenic MUC1 interacts with epidermal growth factor receptor and correlates with mitogen-activated protein kinase activation in the mouse mammary gland”. J. Biol. Chem. 276 (16): 13057–64. DOI:10.1074/jbc.M011248200. PMID 11278868. 
  36. ↑ Li Y, Ren J, Yu W, Li Q, Kuwahara H, Yin L, Carraway K L, Kufe D (Sep 2001). „The epidermal growth factor receptor regulates interaction of the human DF3/MUC1 carcinoma antigen with c-Src and beta-catenin”. J. Biol. Chem. 276 (38): 35239–42. DOI:10.1074/jbc.C100359200. PMID 11483589. 
  37. ↑ Tang J, Feng G S, Li W (Oct 1997). „Induced direct binding of the adapter protein Nck to the GTPase-activating protein-associated protein p62 by epidermal growth factor”. Oncogene 15 (15): 1823–32. DOI:10.1038/sj.onc.1201351. PMID 9362449. 
  38. ↑ Li W, Hu P, Skolnik E Y, Ullrich A, Schlessinger J (Dec 1992). „The SH2 and SH3 domain-containing Nck protein is oncogenic and a common target for phosphorylation by different surface receptors”. Mol. Cell. Biol. 12 (12): 5824–33. DOI:10.1128/MCB.12.12.5824. PMC 360522. PMID 1333047. 
  39. ↑ Chen M, She H, Davis E M, Spicer C M, Kim L, Ren R, Le Beau M M, Li W (Sep 1998). „Identification of Nck family genes, chromosomal localization, expression, and signaling specificity”. J. Biol. Chem. 273 (39): 25171–8. DOI:10.1074/jbc.273.39.25171. PMID 9737977. 
  40. ↑ Tu Y, Li F, Wu C (Dec 1998). „Nck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways”. Mol. Biol. Cell 9 (12): 3367–82. PMC 25640. PMID 9843575. 
  41. ↑ Gauthier ML, Torretto Cheryl, Ly John, Francescutti Valerie, O'Day Danton H (Aug 2003). „Protein kinase Calpha negatively regulates cell spreading and motility in MDA-MB-231 human breast cancer cells downstream of epidermal growth factor receptor”. Biochem. Biophys. Res. Commun. 307 (4): 839–46. DOI:10.1016/S0006-291X(03)01273-7. PMID 12878187. 
  42. ↑ Bedrin MS, Abolafia C M, Thompson J F (Jul 1997). „Cytoskeletal association of epidermal growth factor receptor and associated signaling proteins is regulated by cell density in IEC-6 intestinal cells”. J. Cell. Physiol. 172 (1): 126–36. DOI:10.1002/(SICI)1097-4652(199707)172:1<126::AID-JCP14>3.0.CO;2-A. PMID 9207933. 
  43. ↑ Sun J, Nanjundan Meera, Pike Linda J, Wiedmer Therese, Sims Peter J (May 2002). „Plasma membrane phospholipid scramblase 1 is enriched in lipid rafts and interacts with the epidermal growth factor receptor”. Biochemistry 41 (20): 6338–45. DOI:10.1021/bi025610l. PMID 12009895. 
  44. ↑ Sarmiento M, Puius Y A, Vetter S W, Keng Y F, Wu L, Zhao Y, Lawrence D S, Almo S C, Zhang Z Y (Jul 2000). „Structural basis of plasticity in protein tyrosine phosphatase 1B substrate recognition”. Biochemistry 39 (28): 8171–9. DOI:10.1021/bi000319w. PMID 10889023. 
  45. ↑ Zhang ZY, Walsh A B, Wu L, McNamara D J, Dobrusin E M, Miller W T (Mar 1996). „Determinants of substrate recognition in the protein-tyrosine phosphatase, PTP1”. J. Biol. Chem. 271 (10): 5386–92. DOI:10.1074/jbc.271.10.5386. PMID 8621392. 
  46. ↑ 46,0 46,1 Tomic S, Greiser U, Lammers R, Kharitonenkov A, Imyanitov E, Ullrich A, Böhmer F D (Sep 1995). „Association of SH2 domain protein tyrosine phosphatases with the epidermal growth factor receptor in human tumor cells. Phosphatidic acid activates receptor dephosphorylation by PTP1C”. J. Biol. Chem. 270 (36): 21277–84. DOI:10.1074/jbc.270.36.21277. PMID 7673163. 
  47. ↑ Keilhack H, Tenev T, Nyakatura E, Godovac-Zimmermann J, Nielsen L, Seedorf K, Böhmer F D (Sep 1998). „Phosphotyrosine 1173 mediates binding of the protein-tyrosine phosphatase SHP-1 to the epidermal growth factor receptor and attenuation of receptor signaling”. J. Biol. Chem. 273 (38): 24839–46. DOI:10.1074/jbc.273.38.24839. PMID 9733788. 
  48. ↑ Wang SE, Wu FY, Shin I, Qu S, Arteaga CL (2005). „Transforming growth factor {beta} (TGF-{beta})-Smad target gene protein tyrosine phosphatase receptor type kappa is required for TGF-{beta} function.”. Mol Cell Biol 25 (11): 4703–15. DOI:10.1128/MCB.25.11.4703-4715.2005. PMC 1140650. PMID 15899872. 
  49. ↑ Lu Y, Brush J, Stewart T A (Apr 1999). „NSP1 defines a novel family of adaptor proteins linking integrin and tyrosine kinase receptors to the c-Jun N-terminal kinase/stress-activated protein kinase signaling pathway”. J. Biol. Chem. 274 (15): 10047–52. DOI:10.1074/jbc.274.15.10047. PMID 10187783. 
  50. ↑ Soubeyran P, Kowanetz Katarzyna, Szymkiewicz Iwona, Langdon Wallace Y, Dikic Ivan (Mar 2002). „Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors”. Nature 416 (6877): 183–7. DOI:10.1038/416183a. PMID 11894095. 
  51. ↑ Szymkiewicz I, Kowanetz Katarzyna, Soubeyran Philippe, Dinarina Ana, Lipkowitz Stanley, Dikic Ivan (Oct 2002). „CIN85 participates in Cbl-b-mediated down-regulation of receptor tyrosine kinases”. J. Biol. Chem. 277 (42): 39666–72. DOI:10.1074/jbc.M205535200. PMID 12177062. 
  52. ↑ Sakaguchi K, Okabayashi Y, Kido Y, Kimura S, Matsumura Y, Inushima K, Kasuga M (Apr 1998). „Shc phosphotyrosine-binding domain dominantly interacts with epidermal growth factor receptors and mediates Ras activation in intact cells”. Mol. Endocrinol. 12 (4): 536–43. DOI:10.1210/me.12.4.536. PMID 9544989. 
  53. ↑ Qian X, Esteban L, Vass W C, Upadhyaya C, Papageorge A G, Yienger K, Ward J M, Lowy D R, Santos E (Feb 2000). „The Sos1 and Sos2 Ras-specific exchange factors: differences in placental expression and signaling properties”. EMBO J. 19 (4): 642–54. DOI:10.1093/emboj/19.4.642. PMC 305602. PMID 10675333. 
  54. ↑ Qian X, Vass W C, Papageorge A G, Anborgh P H, Lowy D R (Feb 1998). „N terminus of Sos1 Ras exchange factor: critical roles for the Dbl and pleckstrin homology domains”. Mol. Cell. Biol. 18 (2): 771–8. PMC 108788. PMID 9447973. 
  55. ↑ Keely SJ, Calandrella S O, Barrett K E (Apr 2000). „Carbachol-stimulated transactivation of epidermal growth factor receptor and mitogen-activated protein kinase in T(84) cells is mediated by intracellular ca(2+), PYK-2, and p60(src)”. J. Biol. Chem. 275 (17): 12619–25. DOI:10.1074/jbc.275.17.12619. PMID 10777553. 
  56. ↑ Sato K, Kimoto M, Kakumoto M, Horiuchi D, Iwasaki T, Tokmakov A A, Fukami Y (Sep 2000). „Adaptor protein Shc undergoes translocation and mediates up-regulation of the tyrosine kinase c-Src in EGF-stimulated A431 cells”. Genes Cells 5 (9): 749–64. DOI:10.1046/j.1365-2443.2000.00358.x. PMID 10971656. 
  57. ↑ Xia L, Wang Lijuan, Chung Alicia S, Ivanov Stanimir S, Ling Mike Y, Dragoi Ana M, Platt Adam, Gilmer Tona M, Fu Xin-Yuan, Chin Y Eugene (Aug 2002). „Identification of both positive and negative domains within the epidermal growth factor receptor COOH-terminal region for signal transducer and activator of transcription (STAT) activation”. J. Biol. Chem. 277 (34): 30716–23. DOI:10.1074/jbc.M202823200. PMID 12070153. 
  58. ↑ Yuan Z-L, Guan Ying-Jie, Wang Lijuan, Wei Wenyi, Kane Agnes B, Chin Y Eugene (Nov 2004). „Central role of the threonine residue within the p+1 loop of receptor tyrosine kinase in STAT3 constitutive phosphorylation in metastatic cancer cells”. Mol. Cell. Biol. 24 (21): 9390–400. DOI:10.1128/MCB.24.21.9390-9400.2004. PMC 522220. PMID 15485908. 
  59. ↑ Sehat B, Andersson Sandra, Girnita Leonard, Larsson Olle (Jul 2008). „Identification of c-Cbl as a new ligase for insulin-like growth factor-I receptor with distinct roles from Mdm2 in receptor ubiquitination and endocytosis”. Cancer Res. 68 (14): 5669–77. DOI:10.1158/0008-5472.CAN-07-6364. PMID 18632619. 
  60. ↑ She HY, Rockow S, Tang J, Nishimura R, Skolnik E Y, 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”. Mol. Biol. Cell 8 (9): 1709–21. PMC 305731. PMID 9307968. 

Literatura[uredi | uredi kod]

Vanjske veze[uredi | uredi kod]

Izvor: https://sh.wikipedia.org/w/index.php?title=Receptor_epidermalnog_faktora_rasta&oldid=41442564