DOI QR코드

DOI QR Code

Effect of salt on membrane protein Caveolin3 proved with NMR spectroscopy

  • Byoungduck Park (College of Pharmacy, Sahmyook University) ;
  • Ji-Hun Kim (College of Pharmacy, Chungbuk National University)
  • Received : 2024.07.10
  • Accepted : 2024.08.07
  • Published : 2024.09.20

Abstract

Caveolin3, mainly expressed in muscle tissue types, is a structural scaffolding protein of caveolae which are microdomains of plasma membrane. To elucidate the relationship between structure and function, several studies on the structure of caveolins using NMR have been reported. Because the ionic strength can affect the electrostatic-driven association of proteins with ligand and protein structure, the effect of salt in the structural studies has to be considered. In this work, we observed that the chemical shifts of Cav3 in the LPPG detergent change depending on salt concentration. The R2 values also show salt concentration-dependent changes. Specifically, in the N-terminal region where conformational changes and various interactions occur, the R2 values decrease. Interestingly, the R2 values of residues expected to be located in the LPPG detergent are also influenced by the salt concentration. This work suggests that the concentration of NaCl can affect interpretation of NMR data from membrane proteins.

Keywords

Acknowledgement

We thank Korea Basic Science Institute (Ochang, Korea) for allowing us to use their NMR spectrometers. This research was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (NRF-2022R1A2C1010308) and by "Regional Innovation Strategy (RIS)" through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (MOE) (2021RIS-001). This research was supported by the Korea Basic Science Institute under the R&D program (Project No. C330430) supervised by the Ministry of Science and ICT. This work was conducted during the research year of Chungbuk National University in 2023.

References

  1. D. A. Brown, E. London, Annu Rev Cell Dev Biol 14, 111 (1998) 
  2. M. O. Parat, Int Rev Cell Mol Biol 273, 117 (2009) 
  3. M. Bastiani, R. G. Parton, J Cell Sci 123, 3831 (2010) 
  4. E. Gazzerro, F. Sotgia, C. Bruno, M. P. Lisanti, C. Minetti, Eur J Hum Genet 18, 137 (2010) 
  5. C. Lamaze, N. Tardif, M. Dewulf, S. Vassilopoulos, C. M. Blouin, Current opinion in cell biology 47, 117 (2017) 
  6. U. E. Martinez-Outschoorn, F. Sotgia, M. P. Lisanti, Nat Rev Cancer 15, 225 (2015) 
  7. K. G. Rothberg, J. E. Heuser, W. C. Donzell, Y. S. Ying, J. R. Glenney, R. G. Anderson, Cell 68, 673 (1992) 
  8. Z. Tang, P. E. Scherer, T. Okamoto, K. Song, C. Chu, D. S. Kohtz, I. Nishimoto, H. F. Lodish, M. P. Lisanti, J Biol Chem 271, 2255 (1996) 
  9. P. E. Scherer, T. Okamoto, M. Chun, I. Nishimoto, H. F. Lodish, M. P. Lisanti, Proc Natl Acad Sci U S A 93, 131 (1996) 
  10. T. M. Williams, M. P. Lisanti, Ann Med 36, 584 (2004) 
  11. R. Baudrand, N. Gupta, A. E. Garza, A. Vaidya, J. A. Leopold, P. N. Hopkins, X. Jeunemaitre, C. Ferri, J. R. Romero, J. Williams, J. Loscalzo, G. K. Adler, G. H. Williams, L. H. Pojoga, J Am Heart Assoc 5, (2016) 
  12. K. Mayurasakorn, N. Hasanah, T. Homma, M. Homma, I. K. Rangel, A. E. Garza, J. R. Romero, G. K. Adler, G. H. Williams, L. H. Pojoga, Metabolism 83, 92 (2018) 
  13. Y. T. Horikawa, M. Panneerselvam, Y. Kawaraguchi, Y. M. Tsutsumi, S. S. Ali, R. C. Balijepalli, F. Murray, B. P. Head, I. R. Niesman, T. Rieg, V. Vallon, P. A. Insel, H. H. Patel, D. M. Roth, J Am Coll Cardiol 57, 2273 (2011) 
  14. C. Minetti, F. Sotgia, C. Bruno, P. Scartezzini, P. Broda, M. Bado, E. Masetti, M. Mazzocco, A. Egeo, M. A. Donati, D. Volonte, F. Galbiati, G. Cordone, F. D. Bricarelli, M. P. Lisanti, F. Zara, Nat Genet 18, 365 (1998) 
  15. J. H. Kim, J. P. Schlebach, Z. Lu, D. Peng, K. C. Reasoner, C. R. Sanders, Biophys J 110, 2475 (2016) 
  16. Y. B. Ma, D. H. Kang, M. Kim, J. H. Kim, J Korean Magn Reson 23, 67 (2019) 
  17. R. G. Parton, B. M. Collins, Sci Adv 8, eabq6985 (2022) 
  18. D. W. Sim, Y. S. Lee, M. D. Seo, H. S. Won, J. H. Kim, J Korean Magn Reson 19, 137 (2015) 
  19. J. H. Kim, D. Peng, J. P. Schlebach, A. Hadziselimovic, C. R. Sanders, Biochemistry 53, 4320 (2014) 
  20. F. Delaglio, S. Grzesiek, G. W. Vuister, G. Zhu, J. Pfeifer, A. Bax, J Biomol NMR 6, 277 (1995) 
  21. T. D. G. a. D. G. Kneller, SPARKY 3. University of California: San Francisco.