Time-resolved luminescence resonance energy transfer imaging of protein-protein interactions in living cells

Proceedings of the National Academy of Sciences of the United States of America

Volumn 107, Issue 31, 2010, Pages 13582-13587

  Rajapakse, Harsha E ^a   Gahlaut, Nivriti ^a   Mohandessi, Shabnam ^a   Yu, Dan ^b   Turner, Jerrold R ^b   Miller, Lawrence W ^a  

^a UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

^b UNIVERSITY OF CHICAGO   (United States)

Author keywords

Cellular imaging; Dihydrofolate reductase; Forster resonance energy transfer; Lanthanide luminescence; Protein labeling

Indexed keywords

CLAUDIN 1; DIHYDROFOLATE REDUCTASE; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; PROTEIN ZO1; TERBIUM; TRIMETHOPRIM; PROTEIN;

ANIMAL CELL; ARTICLE; AUTOFLUORESCENCE; CELL CULTURE; CELL PERMEABILIZATION; CHEMICAL STRUCTURE; CONTROLLED STUDY; ESCHERICHIA COLI; FLUORESCENCE RESONANCE ENERGY TRANSFER; LUMINESCENCE RESONANCE ENERGY TRANSFER; MICROSCOPY; NONHUMAN; PINOCYTOSIS; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; ANIMAL; CELL LINE; CELL SURVIVAL; DOG; FLUORESCENCE MICROSCOPY; METABOLISM; METHODOLOGY; MOUSE; PROTEIN BINDING; TIME;

ESCHERICHIA COLI;

ANIMALS; CELL LINE; CELL SURVIVAL; DOGS; FLUORESCENCE RESONANCE ENERGY TRANSFER; MICE; MICROSCOPY, FLUORESCENCE; PROTEIN BINDING; PROTEINS; TIME FACTORS;

EID: 77956386037     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1002025107     Document Type: Article

References (48)

1. Pawson T, Nash P (2003) Assembly of cell regulatory systems through protein interaction domains. Science 300(5618):445-452.
2. Fields S, Song O (1989) A novel genetic system to detect protein-protein interactions. Nature 340(6230):245-246.
3. Phizicky EM, Fields S (1995) Protein-protein interactions: Methods for detection and analysis. Microbiol Rev 59(1):94-123.
4. Baudendistel N, Muller G, Waldeck W, Angel P, Langowski J (2005) Two-hybrid fluorescence cross-correlation spectroscopy detects protein-protein interactions in vivo. Chemphyschem 6(5):984-990.
5. Kim SA, Heinze KG, Waxham MN, Schwille P (2004) Intracellular calmodulin availability accessed with two-photon cross-correlation. Proc Natl Acad Sci USA 101(1):105-110.
6. Kerppola TK (2006) Visualization of molecular interactions by fluorescence complementation. Nat Rev Mol Cell Biol 7(6):449-456.
7. Heydorn A, Lundholt BK, Praestegaard M, Pagliaro L (2006) Protein translocation assays: Key tools for accessing new biological information with high-throughput microscopy. Methods Enzymol 414:513-530.
8. Knauer SK, Stauber RH (2005) Development of an autofluorescent translocation biosensor system to investigate protein-protein interactions in living cells. Anal Chem 77(15):4815-4820.
9. Piljic A, Schultz C (2008) Analysis of protein complex hierarchy in living cells. ACS Chem Biol 3(12):749-755.
10. Jares-Erijman EA, Jovin TM (2003) FRET imaging. Nat Biotechnol 21(11):1387-1395.
11. Piston DW, Kremers GJ (2007) Fluorescent protein FRET: The good, the bad, and the ugly. Trends Biochem Sci 32(9):407-414.
12. Vogel SS, Thaler C, Koushik SV (2006) Fanciful FRET. Sci STKE(331):re2.
13. Zhang J, Campbell RE, Ting AY, Tsien RY (2002) Creating new fluorescent probes for cell biology. Nat Rev Mol Cell Biol 3(12):906-918.
14. Kunkel MT, Garcia EL, Kajimoto T, Hall RA, Newton AC (2009) The protein scaffold NHERF-1 controls the amplitude and duration of localized protein kinase D activity. J Biol Chem 284(36):24653-24661.
15. Llopis J, et al. (2000) Ligand-dependent interactions of coactivators steroid receptor coactivator-1 and peroxisome proliferator-activated receptor binding protein with nuclear hormone receptors can be imaged in live cells and are required for transcription. Proc Natl Acad Sci USA 97(8):4363-4368.
16. Berney C, Danuser G (2003) FRET or no FRET: A quantitative comparison. Biophys J 84(6):3992-4010.
17. Gordon GW, Berry G, Liang XH, Levine B, Herman B (1998) Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy. Biophys J 74(5):2702-2713.
18. Nguyen AW, Daugherty PS (2005) Evolutionary optimization of fluorescent proteins for intracellular FRET. Nat Biotechnol 23(3):355-360.
19. Mathis G (1993) Rare earth cryptates and homogeneous fluoroimmunoassays with human sera. Clin Chem 39(9):1953-1959.
20. Prat O, Lopez E, Mathis G (1991) Europium(III) cryptate: A fluorescent label for the detection of DNA hybrids on solid support. Anal Biochem 195(2):283-289.
21. Selvin PR (2002) Principles and biophysical applications of lanthanide-based probes. Annu Rev Biophys Biomol Struct 31:275-302.
22. Selvin PR, Hearst JE (1994) Luminescence energy transfer using a terbium chelate: Improvements on fluorescence energy transfer. Proc Natl Acad Sci USA 91(21): 10024-10028.
23. Leblanc V, et al. (2002) Homogeneous time-resolved fluorescence assay for identifying p53 interactions with its protein partners, directly in a cellular extract. Anal Biochem 308(2):247-254.
24. Maurel D, et al. (2008) Cell-surface protein-protein interaction analysis with time-resolved FRET and snap-tag technologies: Application to GPCR oligomerization. Nat Methods 5(6):561-567.
25. Hanaoka K, Kikuchi K, Kobayashi S, Nagano T (2007) Time-resolved long-lived luminescence imaging method employing luminescent lanthanide probes with a new microscopy system. J Am Chem Soc 129(44):13502-13509.
26. Law GL, et al. (2008) Emissive terbium probe for multiphoton in vitro cell imaging. J Am Chem Soc 130(12):3714-3715.
27. Montgomery CP, Murray BS, New EJ, Pal R, Parker D (2009) Cell-penetrating metal complex optical probes: Targeted and responsive systems based on lanthanide luminescence. Acc Chem Res 42(7):925-937.
28. Song B, Vandevyver CD, Chauvin AS, Bunzli JC (2008) Time-resolved luminescence microscopy of bimetallic lanthanide helicates in living cells. Org Biomol Chem 6(22): 4125-4133.
29. Botchway SW, et al. (2008) Time-resolved and two-photon emission imaging microscopy of live cells with inert platinum complexes. Proc Natl Acad Sci USA 105(42):16071-16076.
30. de Haas RR, et al. (1999) Phosphorescent platinum/palladium coproporphyrins for time-resolved luminescence microscopy. J Histochem Cytochem 47(2):183-196.
31. de Haas RR, et al. (1997) Platinum porphyrins as phosphorescent label for time-resolved microscopy. J Histochem Cytochem 45(9):1279-1292.
32. Rajapakse HE, Reddy DR, Mohandessi S, Butlin NG, Miller LW (2009) Luminescent terbium protein labels for time-resolved microscopy and screening. Angew Chem Int Ed Engl 48(27):4990-4992.
33. Calloway NT, et al. (2007) Optimized fluorescent trimethoprim derivatives for in vivo protein labeling. Chembiochem 8(7):767-774.
34. Gallagher SS, Sable JE, Sheetz MP, Cornish VW (2009) An in vivo covalent TMP-tag based on proximity-induced reactivity. ACS Chem Biol 4(7):547-556.
35. Miller LW, Cai Y, Sheetz MP, Cornish VW (2005) In vivo protein labeling with trimethoprim conjugates: A flexible chemical tag. Nat Methods 2(4):255-257.
36. Petoud S, Cohen SM, Bunzli JC, Raymond KN (2003) Stable lanthanide luminescence agents highly emissive in aqueous solution: multidentate 2-hydroxyisophthalamide complexes of Sm(3+), Eu(3+), Tb(3+), Dy(3+). J Am Chem Soc 125(44):13324-13325.
37. Ahnert-Hilger G, Bader MF, Bhakdi S, Gratzl M (1989) Introduction of macromolecules into bovine adrenal medullary chromaffin cells and rat pheochromocytoma cells (PC12) by permeabilization with streptolysin O: Inhibitory effect of tetanus toxin on catecholamine secretion. J Neurochem 52(6):1751-1758.
38. Okada CY, Rechsteiner M (1982) Introduction of macromolecules into cultured mammalian cells by osmotic lysis of pinocytic vesicles. Cell 29(1):33-41.
39. Rechsteiner M (1987) Osmotic lysis of pinosomes. Methods Enzymol 149:42-48.
40. Tsien RY (1998) The green fluorescent protein. Annu Rev Biochem 67:509-544.
41. Songyang Z, et al. (1997) Recognition of unique carboxyl-terminal motifs by distinct PDZ domains. Science 275(5296):73-77.
42. Doyle DA, et al. (1996) Crystal structures of a complexed and peptide-free membrane protein-binding domain: Molecular basis of peptide recognition by PDZ. Cell 85(7):1067-1076.
43. Itoh M, et al. (1999) Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins. J Cell Biol 147(6):1351-1363.
44. Carlton VE, et al. (2003) Complex inheritance of familial hypercholanemia with associated mutations in TJP2 and BAAT. Nat Genet 34(1):91-96.
45. Hadj-Rabia S, et al. (2004) Claudin-1 gene mutations in neonatal sclerosing cholangitis associated with ichthyosis: A tight junction disease. Gastroenterology 127(5):1386-1390.
46. Umeda K, et al. (2006) ZO-1 and ZO-2 independently determine where claudins are polymerized in tight-junction strand formation. Cell 126(4):741-754.
47. Elangovan M, Day RN, Periasamy A (2002) Nanosecond fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy to localize the protein interactions in a single living cell. J Microsc 205(1):3-14.
48. Heyduk T, Heyduk E (2001) Luminescence energy transfer with lanthanide chelates: interpretation of sensitized acceptor decay amplitudes. Anal Biochem 289(1):60-67.