In situ characterization of Bak clusters responsible for cell death using single molecule localization microscopy

Scientific Reports

Volumn 6, Issue , 2016, Pages

  Nasu, Yusuke ^a   Benke, Alexander ^b   Arakawa, Satoko ^c   Yoshida, Go J ^c   Kawamura, Genki ^a   Manley, Suliana ^b   Shimizu, Shigeomi ^c   Ozawa, Takeaki ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b EPFL   (Switzerland)

^c TOKYO MEDICAL AND DENTAL UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BAK1 PROTEIN, HUMAN; PROTEIN BAK;

ANIMAL; APOPTOSIS; CELL DEATH; CELL LINE; CYTOSOL; HUMAN; METABOLISM; MICROSCOPY; MITOCHONDRIAL MEMBRANE; MITOCHONDRION; MOUSE; PHYSIOLOGY; PROCEDURES; PROTEIN TRANSPORT;

ANIMALS; APOPTOSIS; BCL-2 HOMOLOGOUS ANTAGONIST-KILLER PROTEIN; CELL DEATH; CELL LINE; CYTOSOL; HUMANS; MICE; MICROSCOPY; MITOCHONDRIA; MITOCHONDRIAL MEMBRANES; PROTEIN TRANSPORT;

EID: 84974814522     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep27505     Document Type: Article

References (35)

1. Danial, N. N., & Korsmeyer, S. J. Cell Death: Critical Control Points. Cell 116, 205-219 (2004
2. Czabotar, P. E., Lessene, G., Strasser, A., & Adams, J. M. Control of apoptosis by The BCL-2 protein family: implications for physiology and therapy. Nat Rev Mol Cell Biol. 15, 49-63 (2014
3. Dewson, G., et al. Bak activation for apoptosis involves oligomerization of dimers via their alpha6 helices. Mol Cell 36, 696-703 (2009
4. Dewson, G., et al. To trigger apoptosis, Bak exposes its BH3 domain and homodimerizes via BH3: groove interactions. Mol Cell 30, 369-380 (2008
5. Moldoveanu, T., et al. BID-induced structural changes in BAK promote apoptosis. Nat Struct Mol Biol. 20, 589-597 (2013
6. Zhou, L., & Chang, D. C. Dynamics and structure of The Bax-Bak complex responsible for releasing mitochondrial proteins during apoptosis. J Cell Sci. 121, 2186-2196 (2008
7. Nechushtan, A., Smith, C. L., Lamensdorf, I., Yoon, S.-H., & Youle, R. J. Bax and Bak Coalesce into Novel Mitochondria-Associated Clusters during Apoptosis. J Cell Biol. 153, 1265-1276 (2001
8. Betzig, E., et al. Imaging intracellular fluorescent proteins at nanometer resolution. Science 313, 1642-1645 (2006
9. Rust, M. J., Bates, M., & Zhuang, X. Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM). Nat Methods 3, 793-796 (2006
10. Hess, S. T., Girirajan, T. P. K., & Mason, M. D. Ultra-High Resolution Imaging by Fluorescence Photoactivation Localization Microscopy. Biophys J. 91, 4258-4272 (2006
11. Greenfield, D., et al. Self-organization of The Escherichia coli chemotaxis network imaged with super-resolution light microscopy. PLoS Biol. 7, e1000137 (2009
12. Gunzenhauser, J., Olivier, N., Pengo, T., & Manley, S. Quantitative super-resolution imaging reveals protein stoichiometry and nanoscale morphology of assembling HIV-Gag virions. Nano Lett. 12, 4705-4710 (2012
13. Muranyi, W., Malkusch, S., Muller, B., Heilemann, M., & Krausslich, H. G. Super-resolution microscopy reveals specific recruitment of HIV-1 envelope proteins to viral assembly sites dependent on The envelope C-Terminal tail. PLoS Pathog 9, e1003198 (2013
14. Endesfelder, U., et al. Multiscale spatial organization of RNA polymerase in Escherichia coli. Biophys. J. 105, 172-181 (2013
15. Cisse, I. I., et al. Real-Time dynamics of RNA polymerase II clustering in live human cells. Science 341, 664-667 (2013
16. Zhang, M., et al. Rational design of true monomeric and bright photoactivatable fluorescent proteins. Nat Methods 9, 727-729 (2012
17. Dewson, G., & Kluck, R. M. Mechanisms by which Bak and Bax permeabilise mitochondria during apoptosis. J Cell Sci. 122, 2801-2808 (2009
18. Ester, M., Kriegel, H.-P., & Sander, J. Proc. Second Internat. Conf. on Knowledge Discovery and Data Mining (KDD-96) 226-231 (Munich, Germany, 1996
19. Bushell, G. C., Yan, Y. D., Woodfield, D., Raper, J., & Amal, R. On techniques for The measurement of The mass fractal dimension of aggregates. Adv Colloid Interface Sci. 95, 1-50 (2002
20. Pippa, N., Dokoumetzidis, A., Demetzos, C., & Macheras, P. On The ubiquitous presence of fractals and fractal concepts in pharmaceutical sciences: a review. Int J Pharm 456, 340-352 (2013
21. Shimizu, S., & Tsujimoto, Y. Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity. Proc Natl Acad Sci USA 97, 577-582 (2000
22. Durisic, N., Laparra-Cuervo, L., Sandoval-Alvarez, A., Borbely, J. S., & Lakadamyali, M. Single-molecule evaluation of fluorescent protein photoactivation efficiency using an in vivo nanotemplate. Nat Methods 11, 156-162 (2014
23. Saito, M., Korsmeyer, S. J., & Schlesinger, P. H. BAX-dependent transport of cytochrome c reconstituted in pure liposomes. Nat Cell Biol 2, 553-555 (2000
24. Bleicken, S., et al. Molecular details of Bax activation, oligomerization, and membrane insertion. J Biol Chem 285, 6636-6647 (2010
25. Oh, K. J., et al. Conformational changes in BAK, a pore-forming proapoptotic Bcl-2 family member, upon membrane insertion and direct evidence for The existence of BH3-BH3 contact interface in BAK homo-oligomers. J Biol Chem 285, 28924-28937 (2010
26. Westphal, D., Kluck, R. M., & Dewson, G. Building blocks of The apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis. Cell Death Differ 21, 196-205 (2014
27. Bleicken, S., Landeta, O., Landajuela, A., Basanez, G., & Garcia-Saez, A. J. Proapoptotic Bax and Bak proteins form stable proteinpermeable pores of tunable size. J Biol Chem 288, 33241-33252 (2013
28. Salvador-Gallego, R., et al. Bax assembly into rings and arcs in apoptotic mitochondria is linked to membrane pores. EMBO J 35, 389-401 (2016
29. Große, L., et al. Bax assembles into large ring-like structures remodeling The mitochondrial outer membrane in apoptosis. EMBO J. 35, 402-413 (2016
30. Tokunaga, M., Imamoto, N., & Sakata-Sogawa, K. Highly inclined thin illumination enables clear single-molecule imaging in cells. Nat Methods 5, 159-161 (2008
31. Thompson, R. E., Larson, D. R., & Webb, W. W. Precise Nanometer Localization Analysis for Individual Fluorescent Probes. Biophys J. 82, 2775-2783 (2002
32. Renz, M., Daniels, B. R., Vamosi, G., Arias, I. M., & Lippincott-Schwartz, J. Plasticity of The asialoglycoprotein receptor deciphered by ensemble FRET imaging and single-molecule counting PALM imaging. Proc Natl Acad Sci USA 109, E2989-2997 (2012
33. Annibale, P., Vanni, S., Scarselli, M., Rothlisberger, U., & Radenovic, A. Quantitative photo activated localization microscopy: unraveling The effects of photoblinking. PLoS One 6, e22678 (2011
34. Lee, S.-H., Shin, J. Y., Lee, A., & Bustamante, C. Counting single photoactivatable fluorescent molecules by photoactivated localization microscopy (PALM). Proc Natl Acad Sci USA 109, 17436-17441 (2012
35. Niu, L., & Yu, J. Investigating Intracellular Dynamics of FtsZ Cytoskeleton with Photoactivation Single-Molecule Tracking. Biophys J. 95, 2009-2016 (2008