Group of Molecular Physiology

Department of Peptide and Protein Technologies

Head: Igor Deyev, Ph.D.
deyevie@ibch.ru+7(495)335-41-77, +7(916)354-83-57

The group is looking for tyrosine kinase receptors, which activated by changes in extracellular pH.

Using the AcalPred computer program researchers predict receptors which have the activation potential after some changes of extracellular pH. As a result, the researchers were able to find a variety of receptors, some of which are phosphorylated at alkalization extracellular environment. Some receptors have a direct impact oncology and perform as tumor markers.

The group was established in 2013.

NamePositionContacts
Igor Deyev, Ph.D.depart. dir.deyevie@ibch.ru+7(495)335-41-77, +7(916)354-83-57
Egor Zhevlenevj. r. f.egor.zhevlenev@gmail.com+7(495)335-41-77

Selected publications

  1. Martynov VI, Pakhomov AA, Deyev IE, Petrenko AG (2018). Genetically encoded fluorescent indicators for live cell pH imaging. BIOCHIM BIOPHYS ACTA 1862 (12), 2924–2939
  2. Zubkov EA, Morozova AY, Chachina NA, Shayakhmetova DM, Mozhaev AA, Deyev IE, Chekhonin VP, Petrenko AG (2018). Behavioral Characteristics of Mice with Knockout of the IRR Alkali Sensor Gene. Neurosci Behav Physiol 48 (4), 483–487
  3. Deyev IE, Shayahmetova DM, Zhenilo SV, Radionov NV, Petrenko AG (2018). Profile of Gene Expression in the Kidneys of Mice with the insrr Gene Knockout. Russ. J. Bioorganic Chem. 44 (2), 256–260
  4. Zhenilo S, Deyev I, Litvinova E, Zhigalova N, Kaplun D, Sokolov A, Mazur A, Prokhortchouk E (2018). DeSUMOylation switches Kaiso from activator to repressor upon hyperosmotic stress. Cell Death Differ  (0), 1–14
  5. Pakhomov AA, Martynov VI, Orsa AN, Bondarenko AA, Chertkova RV, Lukyanov KA, Petrenko AG, Deyev IE (2017). Fluorescent protein Dendra2 as a ratiometric genetically encoded pH-sensor. Biochem Biophys Res Commun 493 (4), 1518–1521
  6. Deyev IE, Chachina NA, Zhevlenev ES, Petrenko AG (2017). Site-directed mutagenesis of the fibronectin domains in insulin receptor-related receptor. Int J Mol Sci 18 (11),
  7. Mozhaev AA, Erokhina TN, Serova OV, Deyev IE, Petrenko AG (2017). Production and immunochemical characterization of monoclonal antibody to IRR ectodomain. Russ. J. Bioorganic Chem. 43 (6), 653–657
  8. Deyev IE, Popova NV, Serova OV, Zhenilo SV, Regoli M, Bertelli E, Petrenko AG (2017). Alkaline pH induces IRR-mediated phosphorylation of IRS-1 and actin cytoskeleton remodeling in a pancreatic beta cell line. B SOC CHIM BIOL 138 (0), 62–69
  9. Можаев АА, Ерохина ТН, Серова ОВ, Деев ИЕ, Петренко АГ (2017). Получение и иммунохимическая характеристика моноклонального антитела к эктодомену рецептора, подобного рецептору инсулина (IRR). 43 (6), 631–636
  10. Pakhomov AA, Chertkova RV, Deyev IE, Petrenko AG, Martynov VI (2017). Generation of photoactivatable fluorescent protein from photoconvertible ancestor. Russ. J. Bioorganic Chem. 43 (3), 340–343
  11. Pakhomov AA, Deyev IE, Ratnikova NM, Chumakov SP, Mironiuk VB, Kononevich YN, Muzafarov AM, Martynov VI (2017). BODIPY-based dye for no-wash live-cell staining and imaging. Biotechniques 63 (2), 77–79
  12. Shayahmetova DM, Zhevlenev ES, Mozhaev AA, Deyev IE, Petrenko AG (2016). Genetic link between IRR-receptor and Ly6/PLAUR protein. Russ. J. Bioorganic Chem. 42 (4), 449–452
  13. Martynov VI, Pakhomov AA, Popova NV, Deyev IE, Petrenko AG (2016). Synthetic Fluorophores for Visualizing Biomolecules in Living Systems. Acta Naturae 8 (4), 33–46
  14. Serova OV, Radionov NV, Shayahmetova DM, Deyev IE, Petrenko AG (2015). Structural and functional analyses of the sixth site of neurexin alternative splicing. Dokl Biochem Biophys 463 (1), 239–242
  15. Deyev IE, Popova NV, Petrenko AG (2015). Determination of Alkali-Sensing Parts of the Insulin Receptor-Related Receptor Using the Bioinformatic Approach. Acta Naturae 7 (2), 80–6
  16. Deyev IE, Popova NV, Petrenko AG (2015). Determination of alkali-sensing parts of the insulin receptor-related receptor using the bioinformatic approach. Acta Naturae 7 (2), 80–86
  17. Deyev IE, Chachina NA, Shayahmetova DM, Serova OV, Petrenko AG (2015). Mapping of alkali-sensing sites of the insulin receptor-related receptor. the role of L2 and fibronectin domains. B SOC CHIM BIOL 111 (0), 1–9
  18. Deyev IE, Mitrofanova AV, Zhevlenev ES, Radionov N, Berchatova AA, Popova NV, Serova OV, Petrenko AG (2013). Structural determinants of the insulin receptor-related receptor activation by Alkali. J Biol Chem 288 (47), 33884–33893
  19. Popova NV, Deyev IE, Petrenko AG (2013). Clathrin-mediated endocytosis and adaptor proteins. Acta Naturae 5 (3), 62–73
  20. Popova NV, Deyev IE, Petrenko AG (2013). Analysis of structural determinants of alkali sensor IRR positive cooperativity. Dokl Biochem Biophys 450 (1), 160–163
  21. Petrenko AG, Zozulya SA, Deyev IE, Eladari D (2013). Insulin receptor-related receptor as an extracellular pH sensor involved in the regulation of acid-base balance. BIOCHIM BIOPHYS ACTA 1834 (10), 2170–2175
  22. Popova NV, Deyev IE, Petrenko AG (2013). Clathrin-mediated endocytosis and adaptor proteins. Acta Naturae 5 (18), 62–73
  23. Deyev IE, Rzhevsky DI, Berchatova AA, Serova OV, Popova NV, Murashev AN, Petrenko AG (2011). Deficient Response to Experimentally Induced Alkalosis in Mice with the Inactivated insrr Gene. Acta Naturae 3 (4), 114–7
  24. Popova NV, Deyev IE, Petrenko AG (2011). Association of adaptor protein TRIP8b with clathrin. J Neurochem 118 (6), 988–998
  25. Deyev IE, Sohet F, Vassilenko KP, Serova OV, Popova NV, Zozulya SA, Burova EB, Houillier P, Rzhevsky DI, Berchatova AA, Murashev AN, Chugunov AO, Efremov RG, NikolSky NN, Bertelli E, Eladari D, Petrenko AG (2011). Insulin receptor-related receptor as an extracellular alkali sensor. Cell Metab 13 (6), 679–689
  26. Serova OV, Popova NV, Petrenko AG, Deyev IE (2010). Association of the subunits of the calcium-independent receptor of α-latrotoxin. Biochem Biophys Res Commun 402 (4), 658–662
  27. Deyev IE, Petrenko AG (2010). Regulation of CIRL-1 proteolysis and trafficking. B SOC CHIM BIOL 92 (4), 418–422
  28. Serova OV, Deyev IE, Petrenko AG (2009). Novel GPS-containing G protein-coupled receptor from monosiga brevicollis. Dokl Biochem Biophys 427 (1), 191–194
  29. Krasnoperov V, Deyev IE, Serova OV, Xu C, Lu Y, Buryanovsky L, Gabibov AG, Neubert TA, Petrenko AG (2009). Dissociation of the Subunits of the calcium-independent receptor of α-Latrotoxin as a result of two-step proteolysis. Biochemistry 48 (14), 3230–3238
  30. Serova OV, Popova NV, Deyev IE, Petrenko AG (2008). Identification of proteins in complexes with α-latrotoxin receptors. Russ. J. Bioorganic Chem. 34 (6), 668–673
  31. Popova NV, Plotnikov AN, Ziganshin RK, Deyev IE, Petrenko AG (2008). Analysis of proteins interacting with TRIP8b adapter. Biochemistry (Mosc) 73 (6), 644–651

Igor Deyev

  • Russia, Moscow, Ul. Miklukho-Maklaya 16/10 — On the map
  • IBCh RAS, build. 31, office. 208
  • Phone: +7(495)335-41-77
  • E-mail: deyevie@ibch.ru

Site-directed mutagenesis of the fibronectin domains in insulin receptor-related receptor (2017-11-26)

We have previously demonstrated that IRR activation is defined by its extracellular region, involves multiple domains and show positive cooperativity with two synergistic sites. By the analyses of point mutants and chimeras of IRR with IR, we now address the role of the FnIII repeats in the IRR pH-sensing. We found that the first activation site includes the intrinsically disordered subdomain ID (646-716) within the FnIII-2 domain at the C-terminus of IRR alpha subunit together with closely located residues L135, G188, R244, H318, K319 of L1 and C domains of the second subunit. The second site involves residue T582 of FnIII-1 domain at the top of IRR lambda-shape pyramid together with M406, V407, D408 from L2 domain within the second subunit. A possible importance of the IRR carbohydrate moiety for its activation was also assessed. IRR is normally less glycosylated than IR and IGF-IR. Swapping both FnIII-2 and FnIII-3 IRR domains with those of IR shifted beta-subunit mass from 68 kDa for IRR to about 100 kDa due to increased glycosylation and abolished the IRR pH response. However, mutations of four asparagine residues, potential glycosylation sites in chimera IRR with swapped FnIII-2/3 domains of IR, decreased the chimera glycosylation and resulted in a partial restoration of IRR pH-sensing activity suggesting that the extensive glycosylation of FnIII-2/3 provides steric hindrance for the alkali-induced rearrangement of the IRR ectodomain.