Skip to main content
SpringerLink
Log in

Alternative dimerization of receptor tyrosine kinases with signal transduction through a cellular membrane

  • Mini-Review
  • Published:
Russian Journal of Bioorganic Chemistry Aims and scope Submit manuscript

Abstract

Receptor tyrosine kinases (RTKs) occupy a separate functional niche among membrane receptors, which is determined by the special features of mechanisms of the signal transduction through a cellular membrane. RTKs are involved in the regulation of development and homeostasis of all the tissues of a human organism, playing a central role in cell proliferation, differentiation, and adhesion. A necessary condition of the biochemical signal transduction through a plasmatic membrane is a ligand-dependent or a ligand-independent dimerization (and/or an oligomerization) of RTKs which is accompanied by conformational rearrangements of all the RTK domains, including the α-helical transmembrane segments. In this review, the main aspects of structure-function relationship for RTKs from various receptor subfamilies are briefly discussed. It is shown in the light of the recently obtained biophysical and biochemical data that functioning of RTK receptors is mediated not only by protein–protein interactions, but by the state of the lipid environment as one of the main components of a self-consistent signal transduction system as well. The new principles of intercellular signal transduction through a membrane replenish the molecular mechanisms of the RTK functioning that have been earlier proposed and explain a number of paradoxes which are observed upon activation of wild-type receptors and the receptors with pathogenic transmembrane mutations. Understanding of the complex mechanisms of the signaling processes can facilitate the successful search for new opportunities of influence on the RTK biological functions with potential therapeutic consequences.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

Abbreviations

RTK:

receptor tyrosine kinases

TM:

transmembrane

EGFR/ErbB/HER:

receptors from the family of the human epidermal growth factor

EphR:

ephrin receptor

FGFR:

receptor of the fibroblast growth factors

IR:

insulin receptor

IGF1R:

receptor of the insulin-like growth factor 1

IRR:

receptor similar to the insulin receptor

TGFß:

the ß-transforming growth factors

TßR:

receptors of the ß-transforming growth factors

VEGFR:

receptor of the endothelial factor of the vessel growth.

References

  1. Overington, J.P., Al-Lazikani, B., and Hopkins, A.L., Nat. Rev. Drug Discov., 2006, vol. 5, pp. 993–996.

    Article  CAS  PubMed  Google Scholar 

  2. Trenker, R., Call, M.J., and Call, M.E., Curr. Opin. Struct. Biol., 2016, vol. 39, pp. 115–123.

    Article  CAS  PubMed  Google Scholar 

  3. Lemmon, M.A. and Schlessinger, J., Cell, 2010, vol. 141, pp. 1117–1134.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  4. Schlessinger, J., Cold Spring Harb. Perspect. Biol., 2014, vol. 6, pii:a008912.

  5. Volinsky, N. and Kholodenko, B.N., Cold Spring Harb. Perspect. Biol., 2013, vol. 5, p. a009043.

    Article  PubMed  PubMed Central  Google Scholar 

  6. Delcourt, N., Bockaert, J., and Marin, P., Trends Pharmacol. Sci., 2007, vol. 28, pp. 602–607.

    Article  CAS  PubMed  Google Scholar 

  7. Rahman, M.S., Akhtar, N., Jamil, H.M., Banik, R.S., and Asaduzzaman, S.M., Bone Res., 2015, vol. 3, p. 15005.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  8. Uversky, V.N., FEBS Lett., 2015, vol. 589, pp. 2498–2506.

    Article  CAS  PubMed  Google Scholar 

  9. Chen, P.H., Unger, V., and He, X., J. Mol. Biol., 2015, vol. 427, pp. 3921–3934.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  10. Lu, C., Mi, L.-Z., Schurpf, T., Walz, T., and Springer, T.A., J. Biol. Chem., 2012, vol. 287, pp. 38244–38253.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  11. Cherezov, V., Rosenbaum, D.M., Hanson, M.A., Rasmussen, S.G., Thian, F.S., Kobilka, T.S., Choi, H.J., Kuhn, P., Weis, W.I., Kobilka, B.K., and Stevens, R.C., Science, 2007, vol. 318, pp. 1258–1265.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  12. Cherezov, V., Curr. Opin. Struct. Biol., 2011, vol. 21, pp. 559–566.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  13. Lu, C., Mi, L.-Z., Grey, M.J., Zhu, J., Graef, E., Yokoyama, S., and Springer, T.A., Mol. Cell. Biol., 2010, vol. 30, pp. 5432–5443.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  14. Li, E., Wimley, W.C., and Hristova, K., Biochim. Biophys. Acta, 2012, vol. 1818, pp. 183–193.

    Article  CAS  PubMed  Google Scholar 

  15. Stangl, M. and Schneider, D., Biochim. Biophys. Acta, 2015, vol. 1848, pp. 1886–1896.

    Article  CAS  PubMed  Google Scholar 

  16. Cymer, F., Veerappan, A., and Schneider, D., Biochim. Biophys. Acta, 2012, vol. 1818, pp. 963–973.

    Article  CAS  PubMed  Google Scholar 

  17. Hedger, G., Sansom, M.S.P., and Koldso, H., Sci. Rep., 2015, vol. 5, p. 9198.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  18. Schmidt, T., Ye, F., Situ, A.J., An, W., Ginsberg, M.H., and Ulmer, T.S., J. Biol. Chem., 2016, vol. 291, pp. 17536–17546.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  19. MacKenzie, K.R., Chem. Rev., 2006, vol. 106, pp. 1931–1977.

    Article  CAS  PubMed  Google Scholar 

  20. Walters, R.F.S. and DeGrado, W.F., Proc. Natl. Acad. Sci. U. S. A., 2006, vol. 103, pp. 13658–13663.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  21. Teese, M.G. and Langosch, D., Biochemistry, 2015, vol. 54, pp. 5125–5135.

    Article  CAS  PubMed  Google Scholar 

  22. Bocharov, E.V., Mineev, K.S., Pavlov, K.V., Akimov, S.A., Kuznetsov, A.S., Efremov, R.G., and Arseniev, A.S., Biochim. Biophys. Acta, 2017, vol. 1859, pp. 561–576.

    Article  CAS  PubMed  Google Scholar 

  23. Maruyama, I.N., Cells, 2014, vol. 3, pp. 304–330.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  24. He, L. and Hristova, K., Biochim. Biophys. Acta, 2012, vol. 1818, pp. 995–1005.

    Article  CAS  PubMed  Google Scholar 

  25. Maruyama, I.N., BioEssays, 2015, vol. 37, pp. 959–967.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  26. Belov, A.A. and Mohammadi, M., Sci. Signal., 2012, vol. 5, p. pe49.

  27. Landau, M. and Ben-Tal, N., Biochim. Biophys. Acta, 2008, vol. 1785, pp. 12–31.

    CAS  PubMed  Google Scholar 

  28. Cymer, F. and Schneider, D., Cell. Adh. Migr., 2010, vol. 4, pp. 299–312.

    Article  PubMed  PubMed Central  Google Scholar 

  29. Bocharov, E.V., Lesovoy, D.M., Goncharuk, S.A., Goncharuk, M.V., Hristova, K., and Arseniev, A.S., Structure, 2013, vol. 21, pp. 2087–2093.

    Article  CAS  PubMed  Google Scholar 

  30. Arkhipov, A. Shan, Y., Das, R., Endres, N.F., Eastwood, M.P., Wemmer, D.E., Kuriyan, J., and Shaw, D.E., Cell, 2013, vol. 152, pp. 557–569.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  31. Lelimousin, M., Limongelli, V., and Sansom, M.S., J. Am. Chem. Soc., 2016, vol. 138, pp. 10611–1022.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  32. Mineev, K.S., Panova, S.V., Bocharova, O.V., Bocharov, E.V., and Arseniev, A.S., Biochemistry, 2015, vol. 54, pp. 6295–6298.

    Article  CAS  PubMed  Google Scholar 

  33. Bugge, K., Papaleo, E., Haxholm, G.W., Hopper, J.T., Robinson, C.V., Olsen, J.G., Lindorff-Larsen, K., and Kragelund, B.B., Nat. Commun., 2016, vol. 7, p. 11578.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  34. Haxholm, G.W., Nikolajsen, L.F., Olsen, J.G., Fredsted, J., Larsen, F.H., Goffin, V., Pedersen, S.F., Brooks, A.J., Waters, M.J., and Kragelund, B.B., Biochem. J., 2015, vol. 468, pp. 495–506.

    Article  CAS  PubMed  Google Scholar 

  35. Kovacs, E., Das, R., Wang, Q., Collier, T.S., Cantor, A., Huang, Y., Wong, K., Mirza, A., Barros, T., Grob, P., Jura, N., Bose, R., and Kuriyan, J., Mol. Cell. Biol., 2015, vol. 35, pp. 3083–3102.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  36. Hunter, T., Cold Spring Harb. Perspect. Biol., 2014, vol. 6, p. a020644.

    Article  PubMed  PubMed Central  Google Scholar 

  37. Hinck, A.P., Mueller, T.D., and Springer, T.A., Cold Spring Harb. Perspect. Biol., 2016, vol. 8, pii:a022103.

  38. Carpenter, G. and Liao, H.J., Cold Spring Harb. Perspect. Biol., 2013, vol. 5, p. a008979.

    Article  PubMed  PubMed Central  Google Scholar 

  39. Lemmon, M.A., Schlessinger, J., and Ferguson, K.M., Cold Spring Harb. Perspect. Biol., 2014, vol. 6, p. a020768.

    Article  PubMed  PubMed Central  Google Scholar 

  40. Kovacs, E., Zorn, J.A., Huang, Y., Barros, T., and Kuriyan, J., Annu. Rev. Biochem., 2015, vol. 84, pp. 13.1–13.26.

    Article  Google Scholar 

  41. Tao, R.H. and Maruyama, I.N., J. Cell Sci., 2008, vol. 121, pp. 3207–3217.

    Article  CAS  PubMed  Google Scholar 

  42. Nevoltris, D., Lombard, B., Dupuis, E., Mathis, G., Chames, P., and Baty, D., ACS Nano, 2015, vol. 9, pp. 1388–1399.

    Article  CAS  PubMed  Google Scholar 

  43. Bessman, N.J., Bagchi, A., Ferguson, K.M., and Lemmon, M.A., Cell. Rep., 2014, vol. 9, pp. 1306–1317.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  44. Jura, N., Endres, N.F., Engel, K., Deindl, S., Das, R., Lamers, M.H., Wemmer, D.E., Zhang, X., and Kuriyan, J., Cell, 2009, vol. 137, pp. 1293–1307.

    Article  PubMed  PubMed Central  Google Scholar 

  45. Doerner, A., Scheck, R., and Schepartz, A., Chem. Biol., 2015, vol. 22, pp. 776–784.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  46. Fleishman, S.J., Schlessinger, J., and Ben-Tal, N., Proc. Natl. Acad. Sci. U. S. A., 2002, vol. 99, pp. 15937–15940.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  47. Bocharov, E.V., Mineev, K.S., Volynsky, P.E., Ermolyuk, Y.S., Tkach, E.N., Sobol., A.G., Chupin, V.V., Kirpichnikov, M.P., Efremov, R.G., and Arseniev, A.S., J. Biol. Chem., 2008, vol. 283, pp. 6950–6956.

    Article  CAS  PubMed  Google Scholar 

  48. Mineev, K.S., Bocharov, E.V., Pustovalova, Y.E., Bocharova, O.V., Chupin, V.V., and Arseniev, A.S., J. Mol. Biol., 2010, vol. 400, pp. 231–243.

    Article  CAS  PubMed  Google Scholar 

  49. Bocharov, E.V., Mineev, K.S., Goncharuk, M.V., and Arseniev, A.S., Biochim. Biophys. Acta, 2012, vol. 1818, pp. 2158–2170.

    Article  CAS  PubMed  Google Scholar 

  50. Bocharov, E.V., Lesovoy, D.M., Pavlov, K.V., Pustovalova, Y.E., Bocharova, O.V., and Arseniev, A.S., Biochim. Biophys. Acta, 2016, vol. 1858, pp. 1254–1261.

    Article  CAS  PubMed  Google Scholar 

  51. Bragin, P.E., Mineev, K.S., Bocharova, O.V., Volynsky, P.E., Bocharov, E.V., and Arseniev, A.S., J. Mol. Biol., 2016, vol. 428, pp. 52–61.

    Article  CAS  PubMed  Google Scholar 

  52. Endres, N.F., Das, R., Smith, A.W., Arkhipov, A., Kovacs, E., Huang, Y., Pelton, J.G., Shan, Y., Shaw, D.E., Wemmer, D.E., Groves, J.T., and Kuriyan, J., Cell, 2013, vol. 152, pp. 543–556.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  53. Volynsky, P.E., Polyansky, A.A., Fakhrutdinova, G.N., Bocharov, E.V., and Efremov, R.G., J. Am. Chem. Soc., 2013, vol. 135, pp. 8105–8108.

    Article  CAS  PubMed  Google Scholar 

  54. Bennasroune, A., Fickova, M., Gardin, A., Dirrig-Grosch, S., Aunis, D., Cremel, G., and Hubert, P., Mol. Biol. Cell, 2004, vol. 15, pp. 3464–3474.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  55. Arpel, A., Sawma, P., Spenle, C., Fritz, J., Meyer, L., Garnier, N., Velazquez-Quesada, I., Hussenet, T., Aci-Seche, S., Baumlin, N., Genest, M., Brasse, D., Hubert, P., Cremel, G., Orend, G., Laquerriere, P., and Bagnard, D., Cell. Rep., 2014, vol. 8, pp. 1714–1721.

    Article  CAS  PubMed  Google Scholar 

  56. Bublil, E.M., Cohen, T., Arnusch, C.J., Peleg, A., Pines, G., Lavi, S., Yarden, Y., and Shai, Y., Biochemistry, 2016, vol. 55, pp. 5520–5530.

    Article  CAS  PubMed  Google Scholar 

  57. Sinclair, J.K., Denton, E.V., and Schepartz, A., J. Am. Chem. Soc., 2014, vol. 136, pp. 11232–11235.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  58. Belov, A.A. and Mohammadi, M., Cold Spring Harb. Perspect. Biol., 2013, vol. 5.

  59. Plotnikov, A.N., Schlessinger, J., Hubbard, S.R., and Mohammadi, M., Cell, 1999, vol. 98, pp. 641–650.

    Article  CAS  PubMed  Google Scholar 

  60. Pellegrini, L., Burke, D.F., von Delft, F., Mulloy, B., and Blundell, T.L., Nature, 2000, vol. 407, pp. 1029–1034.

    Article  CAS  PubMed  Google Scholar 

  61. Sarabipour, S. and Hristova, K., Nat. Commun., 2016, vol. 7, p. 10262.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  62. Shibuya, M., Cold Spring Harb. Perspect. Biol., 2013, vol. 5, p. a009092.

    Article  PubMed  PubMed Central  Google Scholar 

  63. Sarabipour, S., Ballmer-Hofer, K., and Hristova, K., Elife, 2016, vol. 5, p. e13876.

    Article  PubMed  PubMed Central  Google Scholar 

  64. Manni, S., Mineev, K.S., Usmanova, D., Lyukmanova, E.N., Shulepko, M.A., Kirpichnikov, M.P., Winter, J., Matkovic, M., Deupi, X., Arseniev, A.S., and Ballmer-Hofer, K., Structure, 2014, vol. 22, pp. 1077–1089.

    Article  CAS  PubMed  Google Scholar 

  65. Hubbard, S.R., Cold Spring Harb. Perspect. Biol., 2013, vol. 5, p. a008946.

    Article  PubMed  PubMed Central  Google Scholar 

  66. Wu, J., Li, W., Craddock, B.P., Foreman, K.W., Mulvihill, M.J., Ji, Q.S., Miller, W.T., and Hubbard, S.R., EMBO J., 2008, vol. 27, pp. 1985–1994.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  67. Kavran, J.M., McCabe, J.M., Byrne, P.O., Connacher, M.K., Wang, Z., Ramek, A., Sarabipour, S., Shan, Y., Shaw, D.E., Hristova, K., Cole, P.A., and Leahy, D.J., Elife, 2014, vol. 3, p. e03772.

    Article  PubMed Central  Google Scholar 

  68. Lee, J., Miyazaki, M., Romeo, G.R., and Shoelson, S.E., J. Biol. Chem., 2014, vol. 289, pp. 19769–19777.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  69. Deyev, I.E., Sohet, F., Vassilenko, K.P., Serova, O.V., Popova, N.V., Zozulya, S.A., Burova, E.B., Houillier, P., Rzhevsky, D.I., Berchatova, A.A., Murashev, A.N., Chugunov, A.O., Efremov, R.G., Nikol’sky, N.N., Bertelli, E., Eladari, D., and Petrenko, A.G., Cell Metabolism, 2011, vol. 13, pp. 679–689.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  70. Deyev, I.E., Chachina, N.A., Shayahmetova, D.M., Serova, O.V., and Petrenko, A.G., Biochimie, 2015, vol. 92, pp. 1–9.

    Article  Google Scholar 

  71. Ehrlich, M., Horbelt, D., Marom, B., Knaus, P., and Henis, Y.I., Cell. Signal., 2011, vol. 23, pp. 1424–1432.

    Article  CAS  PubMed  Google Scholar 

  72. Bocharov, E.V., Korzhnev, D.M., Blommers, M.J., Arvinte, T., Orekhov, V.Y., Billeter, M., and Arseniev, A.S., J. Biol. Chem., 2002, vol. 277, pp. 46273–46279.

    Article  CAS  PubMed  Google Scholar 

  73. Bocharov, E.V., Pavlov, K.V., Blommers, M.J.J., Arvinte, T., and Arseniev, A.S., Top. Curr. Chem., 2008, vol. 273, pp. 155–181.

    Article  CAS  PubMed  Google Scholar 

  74. Chaikuad, A. and Bullock, A.N., Cold Spring Harb. Perspect. Biol., 2016, vol. 8, pii:a022111.

  75. Bethani, I., Skanland, S.S., Dikic, I., and Acker-Palmer, A., EMBO J., 2010, vol. 29, pp. 2677–2688.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  76. Lisabeth, E.M., Falivelli, G., and Pasquale, E.B., Cold Spring Harb. Perspect. Biol., 2013, vol. 5, pii:a009159.

  77. Nikolov, D.B., Xu, K., and Himanen, J.P., Biochim. Biophys. Acta, 2013, vol. 1834, pp. 2160–2165.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  78. Sharonov, G.V., Bocharov, E.V., Kolosov, P.M., Astapova, M.V., Arseniev, A.S., and Feofanov, A.V., J. Biol. Chem., 2014, vol. 289, pp. 14955–14964.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  79. Warner, N., Wybenga-Groot, L.E., and Pawson, T., FEBS J., 2008, vol. 275, pp. 2561–2573.

    Article  CAS  PubMed  Google Scholar 

  80. Rosenzweig, S.A., Biochem. Pharmacol., 2012, vol. 83, pp. 1041–1048.

    Article  CAS  PubMed  Google Scholar 

  81. Goh, L.K. and Sorkin, A., Cold Spring Harb. Perspect. Biol., 2013, vol. 5, p. a017459.

    Article  PubMed  PubMed Central  Google Scholar 

  82. Ariotti, N., Liang, H., Xu, Y., Zhang, Y., Yonekubo, Y., Inder, K., Du, G., Parton, R.G., Hancock, J.F., and Plowman, S.J., Mol. Cell. Biol., 2010, vol. 30, pp. 3795–3804.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  83. Himanen, J.P., Yermekbayeva, L., Janes, P.W., Walker, J.R., Xu, K., Atapattu, L., Rajashankar, K.R., Mensinga, A., Lackmann, M., Nikolov, D.B., and Dhe-Paganon, S., Proc. Natl. Acad. Sci. U. S. A., 2010, vol. 107, pp. 10860–10865.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  84. Arkhipov, A., Shan, Y., Kim, E.T., and Shaw, D.E., PLoS Comput. Biol., 2014, vol. 10, p. e1003742.

    Article  PubMed  PubMed Central  Google Scholar 

  85. Chavent, M., Seiradake, E., Jones, E.Y., and Sansom, M.S.P., Structure, 2016, vol. 24, pp. 337–347.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  86. Horner, A., Antonenko, Y.N., and Pohl, P., Biophys. J., 2009, vol. 96, pp. 2689–2695.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  87. Horner, A., Akimov, S.A., and Pohl, P., Phys. Rev. Lett., 2013, vol. 110, p. 268101.

    Article  PubMed  PubMed Central  Google Scholar 

  88. Matsushita, C., Tamagaki, H., Miyazawa, Y., Aimoto, S., Smith, S.O., and Sato, T., Proc. Natl. Acad. Sci. U. S. A., 2013, vol. 110, pp. 1646–1651.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  89. Tamagaki, H., Furukawa, Y., Yamaguchi, R., Hojo, H., Aimoto, S., Smith, S.O., and Sato, T., Biochemistry, 2014, vol. 53, pp. 5000–5007.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  90. McLaughlin, S., Smith, S.O., Hayman, M.J., and Murray, D., J. Gen. Physiol., 2005, vol. 126, pp. 41–53.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  91. Ou, S.-H.I., Schrock, A.B., Bocharov, E.V., Klempner, S.J., Haddad, C.K., Steinecker, G., Johnson, M., Gitlitz, B.J., Chung, J., Campregher, P.V., Ross, J.S., Stephens, P.J., Miller, V.A., Suh, J.H., Ali, S.M., and Velcheti, V., J. Thorac. Oncol., 2017, vol. 12, pp. 446–457.

    Article  PubMed  Google Scholar 

  92. Yamamoto, H., Higasa, K., Sakaguchi, M., Shien, K., Soh, J., Ichimura, K., Furukawa, M., Hashida, S., Tsukuda, K., Takigawa, N., Matsuo, K., Kiura, K., Miyoshi, S., Matsuda, F., and Toyooka, S., J. Natl. Cancer Inst., 2014, vol. 106, p. djt338.

    Article  PubMed  Google Scholar 

  93. Shochat, C., Tal, N., Gryshkova, V., Birger, Y., Bandapalli, O.R., Cazzaniga, G., Gershman, N., Kulozik, A.E., Biondi, A., Mansour, M.R., Twizere, J.C., Muckenthaler, M.U., Ben-Tal, N., Constantinescu, S.N., Bercovich, D., and Izraeli, S., Blood, 2014, vol. 124, pp. 106–110.

    Article  CAS  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, 117997, Russia

    E. V. Bocharov

Authors
  1. E. V. Bocharov
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to E. V. Bocharov.

Additional information

Original Russian Text © E.V. Bocharov, 2017, published in Bioorganicheskaya Khimiya, 2017, Vol. 43, No. 5, pp. 453–463.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Bocharov, E.V. Alternative dimerization of receptor tyrosine kinases with signal transduction through a cellular membrane. Russ J Bioorg Chem 43, 477–486 (2017). https://doi.org/10.1134/S1068162017050041

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1134/S1068162017050041

Keywords

Search

Navigation