3. Gingras AC, Kennedy SG, O’Leary MA et al
(1998) 4E-BP1, a repressor of mRNA translation, is phosphorylated and inactivated by the
Akt(PKB) signaling pathway. Genes Dev 12
(4):502–513
4. Holz MK, Ballif BA, Gygi SP et al (2005)
mTOR and S6K1 mediate assembly of the
translation preinitiation complex through
dynamic protein interchange and ordered
phosphorylation events. Cell 123(4):569–580
5. Arif A, Terenzi F, Potdar AA et al (2017) EPRS
is a critical mTORC1–S6K1 effector that influences adiposity in mice. Nature 542:357–361
6. Caccamo A, Branca C, Talboom JS et al (2015)
Reducing ribosomal protein S6 kinase 1 expression improves spatial memory and synaptic
plasticity in a mouse model of Alzheimer ‘s
disease. J Neurosci 35:14042–14056
7. Kim SY, Baik KH, Baek KH et al (2014) S6K1
negatively regulates TAK1 activity in the tolllike receptor. Mol Cell Biol 34:510–521
8. Marabita M, Baraldo M, Solagna F et al (2016)
S6K1 is required for increasing skeletal muscle
force during hypertrophy article S6K1 is
required for increasing skeletal muscle force
during hypertrophy. Cell Rep 17:501–513
9. Choo AY, Yoon SO, Kim SG et al (2008)
Rapamycin differentially inhibits S6Ks and
4E-BP1 to mediate cell-type-specific repression
of mRNA translation. Proc Natl Acad Sci U S A
105(45):17414–17419. https://doi.org/10.
1073/pnas.0809136105
10. Choo AY, Blenis J (2009) Not all substrates are
treated equally implications for mTOR,
rapamycin-resistance and cancer therapy. Cell
Cycle 8:567–572. https://doi.org/10.4161/
cc.8.4.7659
11. Fo ¨rster T (1948) Zwischenmolekulare Energiewanderung und Fluoreszenz [Intermolecular energy migration and fluorescence].
Annalen der Physik (in German). 437: 55–75.
B Fo ¨r s t e r T (1946) Energiewanderung und
Fluoreszenz.
Naturwissenschaften
33:166–175? (Translation: by Klaus Suhling).
J Biomed Opt 17:011002
12. Pawley JB (2006) Handbook of biological confocal microscopy, 3rd edn. Springer, New York,
NY, pp 1–985. https://doi.org/10.1007/
978-0-387-45524-2_8. ISBN 978-0-38725921-5
13. Fa ´bia ´n A ´ I, Rente T, Szo ¨llo ˝si J et al (2010)
Strength in numbers: effects of acceptor abundance on FRET efficiency. ChemPhysChem
11:3713–3721.
https://doi.org/10.1002/
cphc.201000568
14. Maliwal BP, Raut S, Fudala R et al (2012)
Extending Fo ¨rster resonance energy transfer
measurements beyond 100 A ˚ using common
organic fluorophores: enhanced transfer in the
presence of multiple acceptors. J Biomed Opt
17:11006. https://doi.org/10.1117/1.JBO.
17.1.011006
15. Walczewska-Szewc K, Bojarski P, d’Auria S
(2013) Extending the range of FRET—the
Monte Carlo study of the antenna effect. J
Mol Model 19:4195–4201. https://doi.org/
10.1007/s00894-013-1810-3
16. Koushik SV, Blank PS, Vogel SS (2009) Anomalous surplus energy transfer observed with
multiple FRET acceptors. PLoS One 4(11):
e8031.
https://doi.org/10.1371/journal.
pone.0008031
17. Bunt G, Wouters FS (2017) FRET from single
to multiplexed signaling events. Biophys Rev
9:119–129.
https://doi.org/10.1007/
s12551-017-0252-z
18. Wolfgang B (2015) Advanced single photon
counting applications. Springer, New York, pp
1–624. https://doi.org/10.1007/978-3-31914929-5
19. Botchway SW, Scherer KM, Hook S et al
(2015) A series of flexible design adaptations
to the Nikon E-C1 and E-C2 confocal microscope systems for UV, multiphoton and FLIM
imaging. J Microsc 258(1):68–78. https://doi.
org/10.1111/jmi.12218
20. Scully AD, Macrobert AJ, Botchway S et al
(1996) Development of a laser-based fluorescence microscope with subnanosecond time
resolution. J Fluoresc 6(2):119–125. https://
doi.org/10.1007/BF00732051
21. Suhling K, Siegel J, Phillips D et al (2002)
Imaging the environment of green fluorescent
protein. Biophys J 83(3589–3595):2002
22. Marcu L, French PMW, Elson DS (2014)
Fluorescence lifetime spectroscopy and imaging—principles and applications in biomedical
diagnostics. CRC Press, Boca Raton, Florida,
pp 1–570. SBN 9781439861677—CAT#
K12851
23. Estandarte AK, Botchway S, Lynch C et al
(2016) The use of DAPI fluorescence lifetime
imaging for investigating chromatin condensation in human chromosomes. Sci Rep 6:31417.
https://doi.org/10.1038/srep31417
24. Yadav RB, Burgos P, Parker AW et al (2013)
mTOR direct interactions with Rheb-GTPase
and raptor: sub-cellular localization using fluorescence lifetime imaging. BMC Cell Biol 14:3.
https://doi.org/10.1186/1471-2121-14-3
25. Stubbs CD, Botchway SW, Slater SJ et al
(2005) The use of time-resolved fluorescence
imaging in the study of protein kinase C localisation in cells. BMC Cell Biol 6(1):22
300
Abdullah Ahmed et al.
(1998) 4E-BP1, a repressor of mRNA translation, is phosphorylated and inactivated by the
Akt(PKB) signaling pathway. Genes Dev 12
(4):502–513
4. Holz MK, Ballif BA, Gygi SP et al (2005)
mTOR and S6K1 mediate assembly of the
translation preinitiation complex through
dynamic protein interchange and ordered
phosphorylation events. Cell 123(4):569–580
5. Arif A, Terenzi F, Potdar AA et al (2017) EPRS
is a critical mTORC1–S6K1 effector that influences adiposity in mice. Nature 542:357–361
6. Caccamo A, Branca C, Talboom JS et al (2015)
Reducing ribosomal protein S6 kinase 1 expression improves spatial memory and synaptic
plasticity in a mouse model of Alzheimer ‘s
disease. J Neurosci 35:14042–14056
7. Kim SY, Baik KH, Baek KH et al (2014) S6K1
negatively regulates TAK1 activity in the tolllike receptor. Mol Cell Biol 34:510–521
8. Marabita M, Baraldo M, Solagna F et al (2016)
S6K1 is required for increasing skeletal muscle
force during hypertrophy article S6K1 is
required for increasing skeletal muscle force
during hypertrophy. Cell Rep 17:501–513
9. Choo AY, Yoon SO, Kim SG et al (2008)
Rapamycin differentially inhibits S6Ks and
4E-BP1 to mediate cell-type-specific repression
of mRNA translation. Proc Natl Acad Sci U S A
105(45):17414–17419. https://doi.org/10.
1073/pnas.0809136105
10. Choo AY, Blenis J (2009) Not all substrates are
treated equally implications for mTOR,
rapamycin-resistance and cancer therapy. Cell
Cycle 8:567–572. https://doi.org/10.4161/
cc.8.4.7659
11. Fo ¨rster T (1948) Zwischenmolekulare Energiewanderung und Fluoreszenz [Intermolecular energy migration and fluorescence].
Annalen der Physik (in German). 437: 55–75.
B Fo ¨r s t e r T (1946) Energiewanderung und
Fluoreszenz.
Naturwissenschaften
33:166–175? (Translation: by Klaus Suhling).
J Biomed Opt 17:011002
12. Pawley JB (2006) Handbook of biological confocal microscopy, 3rd edn. Springer, New York,
NY, pp 1–985. https://doi.org/10.1007/
978-0-387-45524-2_8. ISBN 978-0-38725921-5
13. Fa ´bia ´n A ´ I, Rente T, Szo ¨llo ˝si J et al (2010)
Strength in numbers: effects of acceptor abundance on FRET efficiency. ChemPhysChem
11:3713–3721.
https://doi.org/10.1002/
cphc.201000568
14. Maliwal BP, Raut S, Fudala R et al (2012)
Extending Fo ¨rster resonance energy transfer
measurements beyond 100 A ˚ using common
organic fluorophores: enhanced transfer in the
presence of multiple acceptors. J Biomed Opt
17:11006. https://doi.org/10.1117/1.JBO.
17.1.011006
15. Walczewska-Szewc K, Bojarski P, d’Auria S
(2013) Extending the range of FRET—the
Monte Carlo study of the antenna effect. J
Mol Model 19:4195–4201. https://doi.org/
10.1007/s00894-013-1810-3
16. Koushik SV, Blank PS, Vogel SS (2009) Anomalous surplus energy transfer observed with
multiple FRET acceptors. PLoS One 4(11):
e8031.
https://doi.org/10.1371/journal.
pone.0008031
17. Bunt G, Wouters FS (2017) FRET from single
to multiplexed signaling events. Biophys Rev
9:119–129.
https://doi.org/10.1007/
s12551-017-0252-z
18. Wolfgang B (2015) Advanced single photon
counting applications. Springer, New York, pp
1–624. https://doi.org/10.1007/978-3-31914929-5
19. Botchway SW, Scherer KM, Hook S et al
(2015) A series of flexible design adaptations
to the Nikon E-C1 and E-C2 confocal microscope systems for UV, multiphoton and FLIM
imaging. J Microsc 258(1):68–78. https://doi.
org/10.1111/jmi.12218
20. Scully AD, Macrobert AJ, Botchway S et al
(1996) Development of a laser-based fluorescence microscope with subnanosecond time
resolution. J Fluoresc 6(2):119–125. https://
doi.org/10.1007/BF00732051
21. Suhling K, Siegel J, Phillips D et al (2002)
Imaging the environment of green fluorescent
protein. Biophys J 83(3589–3595):2002
22. Marcu L, French PMW, Elson DS (2014)
Fluorescence lifetime spectroscopy and imaging—principles and applications in biomedical
diagnostics. CRC Press, Boca Raton, Florida,
pp 1–570. SBN 9781439861677—CAT#
K12851
23. Estandarte AK, Botchway S, Lynch C et al
(2016) The use of DAPI fluorescence lifetime
imaging for investigating chromatin condensation in human chromosomes. Sci Rep 6:31417.
https://doi.org/10.1038/srep31417
24. Yadav RB, Burgos P, Parker AW et al (2013)
mTOR direct interactions with Rheb-GTPase
and raptor: sub-cellular localization using fluorescence lifetime imaging. BMC Cell Biol 14:3.
https://doi.org/10.1186/1471-2121-14-3
25. Stubbs CD, Botchway SW, Slater SJ et al
(2005) The use of time-resolved fluorescence
imaging in the study of protein kinase C localisation in cells. BMC Cell Biol 6(1):22
300
Abdullah Ahmed et al.