Review Article of Journal of Pharmaceutical Research and Reviews
Progress in the application of LOV2 domain in protein interaction
College of Medical , China Three Gorges University, Yichang, 443002, China.
Protein-protein interactions (PPIs) and protein complexes formed by interactions are the main accomplishers of various functions of cells. As an important component of biological networks, protein interaction plays an important role in determining life processes such as signal transduction in cells. Although the experimental methods for studying protein interactions are endless, there are still many shortcomings and gaps in the research on the interaction of precisely regulated protein molecules. LOV (Light Oxygen Voltage) is a light-sensitive protein domain originally discovered in the photo of plants for receiving blue light stimulation, transmitting signals, and causing a series of reactions in plants. The LOV domain belongs to a member of the PAS (Per-Arnt-Sim) superfamily and contains two subunits, LOV1 and LOV2. LOV2 is thought to cause a conformational change after receiving light stimulation, primarily responsible for activating the kinase domain. It plays an important role in intracellular signal transduction. In view of the light control and sensitivity of LOV2, which can be used as a research tool in protein interaction processes, the mechanism of action and structural advantages of signal transduction in LOV2 domain in protein interactions are reviewed.
Keywords: Protein interaction; LOV2 domain; Optogenetics; Light-sensitive protein; Photon
How to cite this article:
Xiao Shao. Progress in the applicat-ion of LOV2 domain in protein inter-action. Journal of Pharmaceutical Research and Reviews, 2019; 3:17. DOI:10.28933/jprr-2019-05-1806
1. Geng Guorong. Biomacromolecular Interaction [J]. Life Science, 1994(03): 1-4.
2. Wu Jian, Zhu Haixia, Zhao Zhiwei, et al. Protein Interaction Research Techniques[J].Progress in Animal Medicine, 2016, 37(02): 109-115.
3. Guo Rui, Liu Quanzhong. New Progress in Pro-ein Interaction Research Technology[J]. Jour-nal of Tianjin Medical University, 2015, 21(06): 542-544.
4. Shen Yaoyao, Yan Qingfeng. Advances in pro-tein Interaction Research[J]. Life Science, 2013,
5. Durech M, Trcka F, Vojtesek B, et al. [Methods
for analysis of protein-protein and protein-ligan-d interactions] [J]. Klin Onkol, 2014, 27 Suppl 1: S75-S81.
6. Liu Ziqiang, Wang Wei. Techniques and appli-cations of optogenetics[J]. Medical Review, 201 6, 22(14): 2720-2724.
7. Arinkin V, Granzin J, Rollen K, et al. Structure of a LOV protein in apo-state and implications for construction of LOV-based optical tools [J]. Sci Rep, 2017, 7: 42971.
8. Qiao Xinrong, Duan Hongbin, Ye Zhaowei. Re-search Progress of Plant Transluminescence Receptor and Signal Transduction Mecha-nism[J]. Biotechnology Bulletin, 2014(08): 1-7.
9. Christie JM, Swartz TE, Bogomolni RA, et al. Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function [J].PLANT J, 2002, 32(2): 205-219.
10. Harper SM, Christie JM, Gardner KH. Disrup-tion of the LOV-Jalpha helix interaction acti-vates phototropin kinase activity [J]. BIO-CHEMISTRY-US, 2004, 43(51): 16184-16192.
11. Crosson S, Rajagopal S, Moffat K. The LOV domain family: photoresponsive signaling mo-dules coupled to diverse output domains[J].BI-OCHEMISTRY-US, 2003, 42(1): 2-10.
12. Ziegler T, Moglich A. Photoreceptor engineer-ing [J]. Front Mol Biosci, 2015, 2: 30.
13. Song SH, Freddolino PL, Nash AI, et al. Mod-ulating LOV domain photodynamics with a resi-due alteration outside the chromophore bindingsite[J].BIOCHEMISTRY-US, 2011, 50(13): 241 1-2423.
14. Yin Lengpeng. Design of fluorescent probe ba-sed on LOV2 domain and study of interaction between biliverdin and DNA. Huazhong Agri-cultural University; 2016. p 76.
15. Crosson S, Moffat K. Structure of a flavin-bindi-ng plant photoreceptor domain: insights into lig-ht-mediated signal transduction [J]. Proc Natl Acad Sci U S A, 2001, 98(6): 2995-3000.
16. Nakasone Y, Ohshima M, Okajima K, et al. Ph-otoreaction Dynamics of LOV1 and LOV2 of Phototropin from Chlamydomonas reinhardtii [J]. J PHYS CHEM B, 2018, 122(6):1801-1815.
17. Crosson S, Moffat K. Photoexcited structure of a plant photoreceptor domain reveals a light-dr-iven molecular switch [J].PLANT CELL, 2002, 14(5): 1067-1075.
18. Harper SM, Christie JM, Gardner KH. Disrup-tion of the LOV-Jalpha helix interaction acti-vates phototropin kinase activity [J]. BIO-CHEMISTRY-US, 2004, 43(51): 16184-16192.
19. Aihara Y, Yamamoto T, Okajima K, et al. Muta-tions in N-terminal flanking region of blue light-sensing light-oxygen and voltage 2 (LOV2) domain disrupt its repressive activity on kinase
domain in the Chlamydomonas phototropin [J].
J BIOL CHEM, 2012, 287(13): 9901-9909.
20. Kashojiya S, Yoshihara S, Okajima K, et al. The linker between LOV2-Jalpha and STK plays an essential role in the kinase activation by blue light in Arabidopsis phototropin1, a plant blue light receptor[J].FEBS LETT, 2016 , 590(1): 139-147.
21. Konold PE, Mathes T, Weibetaenborn J, et al. Unfolding of the C-Terminal Jalpha Helix in the LOV2 Photoreceptor Domain Observed by Tim-e-Resolved Vibrational Spectroscopy [J]. J PH-YS CHEM LETT, 2016, 7(17): 3472-3476.
22. Kashojiya S, Okajima K, Shimada T, et al. Es-sential role of the A’alpha/Abeta gap in the N-t-erminal upstream of LOV2 for the blue light signaling from LOV2 to kinase in Arabidopsis photototropin1, a plant blue light receptor [J]. PLOS ONE, 2015, 10(4): e124284.
23. Halavaty AS, Moffat K. Coiled-coil dimerization of the LOV2 domain of the blue-light photore-ceptor phototropin 1 from Arabidopsis thaliana [J]. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2013, 69(Pt 12): 1316 -1321.
24. Bubeck F, Hoffmann MD, Harteveld Z, et al. En-gineered anti-CRISPR proteins for optogenetic control of CRISPR-Cas9 [J]. NAT METHODS, 2018, 15(11): 924-927.
25. Qudrat A, Mosabbir A, Truong K.LOV2-Contro-lled Photoactivation of Protein Trans-Splicing [J]. Methods Mol Biol, 2017, 1495: 227-237.
26. Wong S, Mosabbir AA, Truong K. An Engi-neered Split Intein for Photoactivated Protein Trans-Splicing [J]. PLOS ONE, 2015, 10(8):e13 5965.
27. Zimmerman SP, Kuhlman B, Yumerefendi H. Engineering and Application of LOV2-Based Photoswitches [J]. Methods Enzymol, 2016,580: 169-190.
28. Lungu OI, Hallett RA, Choi EJ, et al. Designing photoswitchable peptides using the AsLOV2 domain[J].CHEM BIOL, 2012, 19(4): 507-517.
29. Renicke C, Schuster D, Usherenko S, et al. A LOV2 domain-based optogenetic tool to control protein degradation and cellular function [J]. CHEM BIOL, 2013, 20(4): 619-626.
30. Lutz AP, Renicke C, Taxis C. Controlling Pro-tein Activity and Degradation Using Blue Light [J]. Methods Mol Biol, 2016, 1408: 67-78.
31. Taxis C. Development of a Synthetic Switch to Control Protein Stability in Eukaryotic Cells with Light [J]. Methods Mol Biol, 2017, 1596:241-25 5.
This work and its PDF file(s) are licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.