Rapid and Quantitative Imaging of Excitation Polarized Fluorescence Reveals Ordered Septin Dynamics in Live Yeast

Biophysical Journal

Volumn 101, Issue 4, 2011, Pages 985-994

  DeMay, Bradley S ^a   Noda, Naoki ^b   Gladfelter, Amy S ^a   Oldenbourg, Rudolf ^b,c  

^a Dartmouth College

^b MARINE BIOLOGICAL LABORATORY   (United States)

^c BROWN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; SEPTIN;

ANISOTROPY; ARTICLE; CHEMICAL STRUCTURE; CRYSTALLIZATION; CYTOLOGY; FLUORESCENCE MICROSCOPY; FLUORESCENCE POLARIZATION; METABOLISM; METHODOLOGY; SACCHAROMYCES CEREVISIAE; THREE DIMENSIONAL IMAGING;

ANISOTROPY; CRYSTALLIZATION; FLUORESCENCE POLARIZATION; GREEN FLUORESCENT PROTEINS; IMAGING, THREE-DIMENSIONAL; MICROSCOPY, FLUORESCENCE; MODELS, MOLECULAR; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE; SEPTINS;

MLCS; MLOWN;

EID: 84856395033     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.07.008     Document Type: Article

References (26)

1. Velez, M., Axelrod, D., Polarized fluorescence photobleaching recovery for measuring rotational diffusion in solutions and membranes. Biophys. J. 53 (1988), 575–591.
2. Gough, A.H., Taylor, D.L., Fluorescence anisotropy imaging microscopy maps calmodulin binding during cellular contraction and locomotion. J. Cell Biol. 121 (1993), 1095–1107.
3. Yanagida, T., Angles of nucleotides bound to cross-bridges in glycerinated muscle fiber at various concentrations of epsilon-ATP, epsilon-ADP and epsilon-AMPPNP detected by polarized fluorescence. J. Mol. Biol. 146 (1981), 539–560.
4. Rocheleau, J.V., Edidin, M., Piston, D.W., Intrasequence GFP in class I MHC molecules, a rigid probe for fluorescence anisotropy measurements of the membrane environment. Biophys. J. 84 (2003), 4078–4086.
5. Mattheyses, A.L., Kampmann, M., et al., Simon, S.M., Fluorescence anisotropy reveals order and disorder of protein domains in the nuclear pore complex. Biophys. J. 99 (2010), 1706–1717.
6. Barral, Y., Mansuy, I.M., Septins: cellular and functional barriers of neuronal activity. Curr. Biol. 17 (2007), R961–R963.
7. Bi, E., Maddox, P., et al., Pringle, J.R., Involvement of an actomyosin contractile ring in Saccharomyces cerevisiae cytokinesis. J. Cell Biol. 142 (1998), 1301–1312.
8. Dobbelaere, J., Barral, Y., Spatial coordination of cytokinetic events by compartmentalization of the cell cortex. Science 305 (2004), 393–396.
9. Kinoshita, A., Kinoshita, M., et al., Kimura, J., Identification of septins in neurofibrillary tangles in Alzheimer's disease. Am. J. Pathol. 153 (1998), 1551–1560.
10. Sitz, J.H., Baumgärtel, K., et al., Lutz, B., The Down syndrome candidate dual-specificity tyrosine phosphorylation-regulated kinase 1A phosphorylates the neurodegeneration-related septin 4. Neuroscience 157 (2008), 596–605.
11. Cerveira, N., Correia, C., et al., Teixeira, M.R., SEPT2 is a new fusion partner of MLL in acute myeloid leukemia with t(2;11)(q37;q23). Oncogene 25 (2006), 6147–6152.
12. Liu, M., Shen, S., Chen, F., Yu, W., Yu, L., Linking the septin expression with carcinogenesis. Mol. Biol. Rep. 37 (2010), 3601–3608.
13. Bertin, A., McMurray, M.A., et al., Nogales, E., Saccharomyces cerevisiae septins: supramolecular organization of heterooligomers and the mechanism of filament assembly. Proc. Natl. Acad. Sci. USA 105 (2008), 8274–8279.
14. Versele, M., Thorner, J., Septin collar formation in budding yeast requires GTP binding and direct phosphorylation by the PAK, Cla4. J. Cell Biol. 164 (2004), 701–715.
15. Tada, T., Simonetta, A., et al., Sheng, M., Role of Septin cytoskeleton in spine morphogenesis and dendrite development in neurons. Curr. Biol. 17 (2007), 1752–1758.
16. Vrabioiu, A.M., Mitchison, T.J., Structural insights into yeast septin organization from polarized fluorescence microscopy. Nature 443 (2006), 466–469.
17. Vrabioiu, A.M., Mitchison, T.J., Symmetry of septin hourglass and ring structures. J. Mol. Biol. 372 (2007), 37–49.
18. Oldenbourg, R., Mei, G., New polarized light microscope with precision universal compensator. J. Microsc. 180 (1995), 140–147.
19. Shribak, M., Oldenbourg, R., Techniques for fast and sensitive measurements of two-dimensional birefringence distributions. Appl. Opt. 42 (2003), 3009–3017.
20. Inoué, S., Shimomura, O., et al., Tran, P.T., Fluorescence polarization of green fluorescence protein. Proc. Natl. Acad. Sci. USA 99 (2002), 4272–4277.
21. Frazier, J.A., Wong, M.L., et al., Field, C., Polymerization of purified yeast septins: evidence that organized filament arrays may not be required for septin function. J. Cell Biol. 143 (1998), 737–749.
22. Demay, B.S., Bai, X., et al., Gladfelter, A.S., Septin filaments exhibit a dynamic, paired organization that is conserved from yeast to mammals. J. Cell Biol. 193 (2011), 1065–1081.
23. Axelrod, D., Fluorescence polarization microscopy. Methods Cell Biol. 30 (1989), 333–352.
24. Lakowicz, J.R., Principles of Fluorescence Spectroscopy. 1985, Plenum, New York.
25. Piston, D.W., Rizzo, M.A., FRET by fluorescence polarization microscopy. Methods Cell Biol. 85 (2008), 415–430.
26. Rosell, F.I., Boxer, S.G., Polarized absorption spectra of green fluorescent protein single crystals: transition dipole moment directions. Biochemistry 42 (2003), 177–183.