Group “Protein-protein interactions”

Nikolai N. Sluchanko
Ph.D. (Biology)
Head of the Group
INBI, build. 1, room 335
Телефон+7 (495) 660-34-30 ext. 462
E-Mail nikolai.sluchanko@mail.ru

Main achievements:

The main focus of studies on universal adaptor proteins of the 14-3-3 family is on investigation of their interaction with different medically relevant protein partners and its regulation by phosphorylation, from biochemical and structural point of view, with a perspective of therapeutic intervention in a long run. The research interests also include structural-functional studies of the steroidogenic acute regulatory protein (StAR), responsible for the delivery of cholesterol to mitochondria during steroidogenesis, and its ligand selectivity; alpha-synuclein and tau protein involved in the process of neurodegeneration accompanying a range of human disorders.

The second direction is devoted i) to studies of protein-protein interactions in the context of the cyanobacterial photoprotection mechanism regulated by the orange carotenoid protein (OCP) and fluorescence recovery protein (FRP), ii) to the unique protein-to-protein carotenoid transfer process discovered in 2017 and iii) to the structural rearrangements within OCP upon its photoactivation.

 

Selected publications:

  1. Slonimskiy YB, Muzzopappa F, Maksimov EG, Wilson A, Friedrich T, Kirilovsky D, Sluchanko NN., Light-controlled carotenoid transfer between water-soluble proteins related to cyanobacterial photoprotection. FEBS J. 2019 Mar 7. doi: 10.1111/febs.14803.
  2. Chebotareva NA, Eronina TB, Roman SG, Mikhaylova VV, Sluchanko NN, Gusev NB, Kurganov BI., Oligomeric state of αB-crystallin under crowded conditions. Biochem Biophys Res Commun. 2019 Jan 22;508(4):1101-1105. doi: 10.1016/j.bbrc.2018.12.015.
  3. Klementiev KE, Maksimov EG, Gvozdev DA, Tsoraev GV, Protopopov FF, Elanskaya IV, Abramov SM, Dyakov MY, Ilyin VK, Nikolaeva NA, Moisenovich MM, Moisenovich AM, Slonimskiy YB, Sluchanko NN, Lebedev VM, Spassky AV, Friedrich T, Maksimov GV, Paschenko VZ, Rubin AB., Radioprotective role of cyanobacterial phycobilisomes. Biochim Biophys Acta Bioenerg. 2019 Feb 1;1860(2):121-128. doi: 10.1016/j.bbabio.2018.11.018.
  4. Sluchanko NN, Slonimskiy YB, Shirshin EA, Moldenhauer M, Friedrich T, Maksimov EG, OCP–FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria, Nature communications (2018) 9: 3869, doi: 10.1038/s41467-018-06195-0.
  5. Harris D, Wilson A, Muzzopappa F, Sluchanko NN, Friedrich T, Maksimov EG, Kirilovsky D, Adir N. Structural rearrangements in the C-terminal domain homolog of Orange Carotenoid Protein are crucial for carotenoid transfer, Communications Biology (2018) 1: 125, doi: 10.1038/s42003-018-0132-5.
  6. Klychnikov OI, Shamorkina TM, Weeks SD, van Leeuwen HC, Corver J, Drijfhout JW, van Veelen PA, Sluchanko NN, Strelkov SV, Hensbergen PJ (2018) Discovery of a new Pro-Pro endopeptidase, PPEP-2, provides mechanistic insights into the differences in substrate specificity within the PPEP family. J Biol Chem 293: 11154-11165
  7. Rovnyagina NR, Sluchanko NN, Tikhonova TN, Fadeev VV, Litskevich AY, Maskevich AA, Shirshin EA (2018) Binding of thioflavin T by albumins: An underestimated role of protein oligomeric heterogeneity. Int J Biol Macromol 108: 284-290
  8. Slonimskiy YB, Maksimov EG, Lukashev EP, Moldenhauer M, Jeffries CM, Svergun DI, Friedrich T, Sluchanko NN (2018) Functional interaction of low-homology FRPs from different cyanobacteria with Synechocystis OCP. Biochim Biophys Acta 1859: 382-393
  9. Sluchanko NN (2018) Association of Multiple Phosphorylated Proteins with the 14-3-3 Regulatory Hubs: Problems and Perspectives. J Mol Biol 430: 20-26
  10. Tikhonova TN, Rovnyagina NR, Zherebker AY, Sluchanko NN, Rubekina AA, Orekhov AS, Nikolaev EN, Fadeev VV, Uversky VN, Shirshin EA (2018) Dissection of the deep-blue autofluorescence changes accompanying amyloid fibrillation. Arch Biochem Biophys 651: 13-20
  11. Tugaeva KV, Faletrov YV, Allakhverdiev ES, Shkumatov VM, Maksimov EG, Sluchanko NN (2018) Effect of the NBD-group position on interaction of fluorescently-labeled cholesterol analogues with human steroidogenic acute regulatory protein STARD1. Biochem Biophys Res Commun 497: 58-64
  12. K.V. Tugaeva, P.O. Tsvetkov, N.N. Sluchanko, Bacterial co-expression of human Tau protein with protein kinase A and 14-3-3 for studies of 14-3-3/phospho-Tau interaction, PLoS One, 12 (2017) e0178933.
  13.  N.N. Sluchanko, K.V. Tugaeva, E.G. Maksimov, Solution structure of human steroidogenic acute regulatory protein STARD1 studied by small-angle X-ray scattering, Biochem Biophys Res Commun, 489 (2017) 445-450.
  14. N.N. Sluchanko, Y.B. Slonimskiy, M. Moldenhauer, T. Friedrich, E.G. Maksimov, Deletion of the short N-terminal extension in OCP reveals the main site for FRP binding, FEBS Lett, 591 (2017) 1667-1676.
  15. N.N. Sluchanko, Y.B. Slonimskiy, E.G. Maksimov, Features of Protein−Protein Interactions in the Cyanobacterial Photoprotection Mechanism, Biochemistry (Moscow), 82 (2017) 1592-1614.
  16. N.N. Sluchanko, K.E. Klementiev, E.A. Shirshin, G.V. Tsoraev, T. Friedrich, E.G. Maksimov, The purple Trp288Ala mutant of Synechocystis OCP persistently quenches phycobilisome fluorescence and tightly interacts with FRP, Biochim Biophys Acta, 1858 (2017) 1-11.
  17. N.N. Sluchanko, K.V. Tugaeva, S.J. Greive, A.A. Antson, Chimeric 14-3-3 proteins for unraveling interactions with intrinsically disordered partners, Sci Rep, 7 (2017) 12014.
  18. N.N. Sluchanko, N.B. Gusev, Moonlighting chaperone-like activity of the universal regulatory 14-3-3 proteins, FEBS J, 284 (2017) 1279-1295.
  19. N.N. Sluchanko, S. Beelen, A.A. Kulikova, S.D. Weeks, A.A. Antson, N.B. Gusev, S.V. Strelkov, Structural Basis for the Interaction of a Human Small Heat Shock Protein with the 14-3-3 Universal Signaling Regulator, Structure, 25 (2017) 305-316.
  20. E.A. Shirshin, E.E. Nikonova, F.I. Kuzminov, N.N. Sluchanko, I.V. Elanskaya, M.Y. Gorbunov, V.V. Fadeev, T. Friedrich, E.G. Maksimov, Biophysical modeling of in vitro and in vivo processes underlying regulated photoprotective mechanism in cyanobacteria, Photosynth Res, 133 (2017) 261-271.
  21. M. Moldenhauer, N.N. Sluchanko, N.N. Tavraz, C. Junghans, D. Buhrke, M. Willoweit, L. Chiappisi, F.J. Schmitt, V. Vukojevic, E.A. Shirshin, V.Y. Ponomarev, V.Z. Paschenko, M. Gradzielski, E.G. Maksimov, T. Friedrich, Interaction of the signaling state analog and the apoprotein form of the orange carotenoid protein with the fluorescence recovery protein, Photosynth Res, (2017). doi: 10.1007/s11120-017-0346-2
  22. M. Moldenhauer, N.N. Sluchanko, D. Buhrke, D.V. Zlenko, N.N. Tavraz, F.J. Schmitt, P. Hildebrandt, E.G. Maksimov, T. Friedrich, Assembly of photoactive orange carotenoid protein from its domains unravels a carotenoid shuttle mechanism, Photosynth Res, 133 (2017) 327-341.
  23. E.G. Maksimov, N.N. Sluchanko, Y.B. Slonimskiy, E.A. Slutskaya, A.V. Stepanov, A.M. Argentova-Stevens, E.A. Shirshin, G.V. Tsoraev, K.E. Klementiev, O.V. Slatinskaya, E.P. Lukashev, T. Friedrich, V.Z. Paschenko, A.B. Rubin, The photocycle of orange carotenoid protein conceals distinct intermediates and asynchronous changes in the carotenoid and protein components, Sci Rep, 7 (2017) 15548.
  24. E.G. Maksimov, N.N. Sluchanko, Y.B. Slonimskiy, K.S. Mironov, K.E. Klementiev, M. Moldenhauer, T. Friedrich, D.A. Los, V.Z. Paschenko, A.B. Rubin, The Unique Protein-to-Protein Carotenoid Transfer Mechanism, Biophys J, 113 (2017) 402-414.
  25. E.G. Maksimov, N.N. Sluchanko, K.S. Mironov, E.A. Shirshin, K.E. Klementiev, G.V. Tsoraev, M. Moldenhauer, T. Friedrich, D.A. Los, S.I. Allakhverdiev, V.Z. Paschenko, A.B. Rubin, Fluorescent Labeling Preserving OCP Photoactivity Reveals Its Reorganization during the Photocycle, Biophys J, 112 (2017) 46-56.
  26. N.N. Sluchanko, K.V. Tugaeva, Y.V. Faletrov, D.I. Levitsky, High-yield soluble expression, purification and characterization of human steroidogenic acute regulatory protein (StAR) fused to a cleavable Maltose-Binding Protein (MBP), Protein Expr Purif, 119 (2016) 27-35.
  27. E.G. Maksimov, M. Moldenhauer, E.A. Shirshin, E.A. Parshina, N.N. Sluchanko, K.E. Klementiev, G.V. Tsoraev, N.N. Tavraz, M. Willoweit, F.J. Schmitt, J. Breitenbach, G. Sandmann, V.Z. Paschenko, T. Friedrich, A.B. Rubin, A comparative study of three signaling forms of the orange carotenoid protein, Photosynth Res, 130 (2016) 389-401.
  28. A.A. Karpulevich, E.G. Maksimov, N.N. Sluchanko, A.N. Vasiliev, V.Z. Paschenko, Highly efficient energy transfer from quantum dot to allophycocyanin in hybrid structures, J Photochem Photobiol B, 160 (2016) 96-101.
  29. M.V. Sudnitsyna, N.N. Sluchanko, N.B. Gusev, HspB6 (Hsp20) as a versatile molecular regulator, Springer, Switzerland, 2015. The Big Book on Small Heat Shock Proteins, Chapter 9, pp. 229-253
  30. N.N. Sluchanko, V.N. Uversky, Hidden disorder propensity of the N-terminal segment of universal adapter protein 14-3-3 is manifested in its monomeric form: Novel insights into protein dimerization and multifunctionality, Biochim Biophys Acta, 1854 (2015) 492-504.
  31. N.N. Sluchanko, N.A. Chebotareva, N.B. Gusev, Quaternary structure of human small heat shock protein HSPB6 (Hsp20) in crowded media modeled by trimethylamine N-oxide (TMAO): Effect of protein phosphorylation, Biochimie, 108 (2015) 68-75.
  32. A.M. Matyushenko, N.V. Artemova, N.N. Sluchanko, D.I. Levitsky, Effects of two stabilizing substitutions, D137L and G126R, in the middle part of alpha-tropomyosin on the domain structure of its molecule, Biophys Chem, 196 (2015) 77-85.
  33. E.G. Maksimov, E.A. Shirshin, N.N. Sluchanko, D.V. Zlenko, E.Y. Parshina, G.V. Tsoraev, K.E. Klementiev, G.S. Budylin, F.J. Schmitt, T. Friedrich, V.V. Fadeev, V.Z. Paschenko, A.B. Rubin, The Signaling State of Orange Carotenoid Protein, Biophys J, 109 (2015) 595-607.
  34. D.S. Logvinova, D.I. Markov, O.P. Nikolaeva, N.N. Sluchanko, D.S. Ushakov, D.I. Levitsky, Does Interaction between the Motor and Regulatory Domains of the Myosin Head Occur during ATPase Cycle? Evidence from Thermal Unfolding Studies on Myosin Subfragment 1, PLoS One, 10 (2015) e0137517.
  35. N.A. Chebotareva, T.B. Eronina, N.N. Sluchanko, B.I. Kurganov, Effect of Ca2+ and Mg2+ ions on oligomeric state and chaperone-like activity of alphaB-crystallin in crowded media, Int J Biol Macromol, 76 (2015) 86-93.
  36. N.N. Sluchanko, S.G. Roman, N.A. Chebotareva, N.B. Gusev, Chaperone-like activity of monomeric human 14-3-3zeta on different protein substrates, Arch Biochem Biophys, 549 (2014) 32-39.
  37. A.M. Matyushenko, N.V. Artemova, D.V. Shchepkin, G.V. Kopylova, S.Y. Bershitsky, A.K. Tsaturyan, N.N. Sluchanko, D.I. Levitsky, Structural and functional effects of two stabilizing substitutions, D137L and G126R, in the middle part of alpha-tropomyosin molecule, FEBS J, 281 (2014) 2004-2016.
  38. T.B. Eronina, N.A. Chebotareva, N.N. Sluchanko, V.V. Mikhaylova, V.F. Makeeva, S.G. Roman, S.Y. Kleymenov, B.I. Kurganov, Dual effect of arginine on aggregation of phosphorylase kinase, Int J Biol Macromol, 68 (2014) 225-232.
  39. N.N. Sluchanko, N.A. Chebotareva, N.B. Gusev, Modulation of 14-3-3/phosphotarget interaction by physiological concentrations of phosphate and glycerophosphates, PLoS One, 8 (2013) e72597.
  40. N.N. Sluchanko, N.V. Artemova, M.V. Sudnitsyna, I.V. Safenkova, A.A. Antson, D.I. Levitsky, N.B. Gusev, Monomeric 14-3-3zeta has a chaperone-like activity and is stabilized by phosphorylated HspB6, Biochemistry, 51 (2012) 6127-6138.
  41. P.N. Datskevich, E.V. Mymrikov, N.N. Sluchanko, A.A. Shemetov, M.V. Sudnitsyna, N.B. Gusev, Expression, purification and some properties of fluorescent chimeras of human small heat shock proteins, Protein Expr Purif, 82 (2012) 45-54.
  42. N.N. Sluchanko, N.B. Gusev, Oligomeric structure of 14-3-3 protein: what do we know about monomers?, FEBS Lett, 586 (2012) 4249-4256.
  43. N.N. Sluchanko, M.V. Sudnitsyna, A.S. Seit-Nebi, A.A. Antson, N.B. Gusev, Properties of the monomeric form of human 14-3-3zeta protein and its interaction with tau and HspB6, Biochemistry, 50 (2011) 9797-9808.
  44. N.N. Sluchanko, N.B. Gusev, Probable participation of 14-3-3 in tau protein oligomerization and aggregation, J Alzheimers Dis, 27 (2011) 467-476.
  45. N.N. Sluchanko, M.V. Sudnitsyna, I.S. Chernik, A.S. Seit-Nebi, N.B. Gusev, Phosphomimicking mutations of human 14-3-3zeta affect its interaction with tau protein and small heat shock protein HspB6, Arch Biochem Biophys, 506 (2011) 24-34.
  46. E.G. Maksimov, T.S. Gostev, F.I. Kuz’minov, N.N. Sluchanko, I.N. Stadnichuk, V.Z. Pashchenko, A.B. Rubin, Hybrid systems of quantum dots mixed with the photosensitive protein phycoerythrin, Nanotechnologies in Russia, 5 (2010) 531-537.
  47. N.N. Sluchanko, N.B. Gusev, 14-3-3 proteins and regulation of cytoskeleton, Biochemistry (Mosc), 75 (2010) 1528-1546.
  48. N.N. Sluchanko, A.S. Seit-Nebi, N.B. Gusev, Effect of phosphorylation on interaction of human tau protein with 14-3-3zeta, Biochem Biophys Res Commun, 379 (2009) 990-994.
  49. N.N. Sluchanko, A.S. Seit-Nebi, N.B. Gusev, Phosphorylation of more than one site is required for tight interaction of human tau protein with 14-3-3zeta, FEBS Lett, 583 (2009) 2739-2742.
  50. N.N. Sluchanko, I.S. Chernik, A.S. Seit-Nebi, A.V. Pivovarova, D.I. Levitsky, N.B. Gusev, Effect of mutations mimicking phosphorylation on the structure and properties of human 14-3-3zeta, Arch Biochem Biophys, 477 (2008) 305-312.