Fast Decay of CaMKII FRET Sensor Signal in Spines after LTP Induction Is Not Due to Its Dephosphorylation
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{"title"=>"Fast decay of CaMKII FRET sensor signal in spines after LTP induction is not due to its dephosphorylation", "type"=>"journal", "authors"=>[{"first_name"=>"Nikolai", "last_name"=>"Otmakhov", "scopus_author_id"=>"6701401217"}, {"first_name"=>"Shaurav", "last_name"=>"Regmi", "scopus_author_id"=>"56578085900"}, {"first_name"=>"John E.", "last_name"=>"Lisman", "scopus_author_id"=>"7006481671"}], "year"=>2015, "source"=>"PLoS ONE", "identifiers"=>{"pui"=>"605585991", "pmid"=>"26086939", "issn"=>"19326203", "doi"=>"10.1371/journal.pone.0130457", "isbn"=>"1932-6203 (Electronic)\r1932-6203 (Linking)", "scopus"=>"2-s2.0-84939196271", "sgr"=>"84939196271"}, "id"=>"d1bc59ed-c716-3c65-ae6a-96f0069bf3bb", "abstract"=>"Because CaMKII is the critical Ca2+ sensor that triggers long-term\\npotentiation (LTP), understanding its activation and deactivation is\\nimportant. A major advance has been the development of a FRET indicator\\nof the conformational state of CaMKII called Camui. Experiments using\\nCamui have demonstrated that the open (active) conformation increases\\nduring LTP induction and then decays in tens of seconds, with the major\\nfast component decaying with a time-constant of similar to 6 sec (tau1).\\nBecause this decay is faster if autophosphorylation of T286 is prevented\\n(the autophosphorylation prolongs activity by making the enzyme active\\neven after Ca2+ falls), it seemed likely that the fast decay is due to\\nthe T286 dephosphorylation. To test this interpretation, we studied the\\neffect of phosphatase inhibitors on the single-spine Camui signal evoked\\nby two-photon glutamate uncaging. We applied inhibitors of PP1 and PP2A,\\ntwo phosphatases that are present at synapses and that have been shown\\nto dephosphorylate CaMKII in vitro. The inhibitors increased the basal\\nCamui activation state, indicating their effectiveness in cells.\\nHowever, in no case did we find that tau1 was prolonged, contrary to\\nwhat would be expected if the decay was phosphatase-dependent. This\\ncould either mean that decay was due to some unknown phosphatase or that\\nthe decay was not due to dephosphorylation. To distinguish between these\\npossibilities, we expressed pseudo-phosphorylated Camui (T286D) (plus\\nadditional mutations {[}T/A] that prevented inhibitory 305/306\\nphosphorylation). This form had an elevated basal activation state, but\\nwas further activated during glutamate uncaging; importantly the\\nactivation state decayed with tau1 nearly the same as that of WT Camui.\\nTherefore, the data strongly indicate that tau1 is not due to T286\\ndephosphorylation. We conclude that, although Camui is an excellent tool\\nfor observing CaMKII signaling, further experimentation is needed to\\ndetermine how CaMKII is turned off by its dephosphorylation.", "link"=>"http://www.mendeley.com/research/fast-decay-camkii-fret-sensor-signal-spines-after-ltp-induction-not-due-dephosphorylation", "reader_count"=>18, "reader_count_by_academic_status"=>{"Unspecified"=>1, "Researcher"=>2, "Student > Ph. D. Student"=>6, "Student > Postgraduate"=>2, "Student > Master"=>5, "Professor"=>2}, "reader_count_by_user_role"=>{"Unspecified"=>1, "Researcher"=>2, "Student > Ph. D. Student"=>6, "Student > Postgraduate"=>2, "Student > Master"=>5, "Professor"=>2}, "reader_count_by_subject_area"=>{"Unspecified"=>1, "Biochemistry, Genetics and Molecular Biology"=>2, "Agricultural and Biological Sciences"=>9, "Neuroscience"=>4, "Pharmacology, Toxicology and Pharmaceutical Science"=>1, "Psychology"=>1}, "reader_count_by_subdiscipline"=>{"Neuroscience"=>{"Neuroscience"=>4}, "Psychology"=>{"Psychology"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>9}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>2}, "Unspecified"=>{"Unspecified"=>1}, "Pharmacology, Toxicology and Pharmaceutical Science"=>{"Pharmacology, Toxicology and Pharmaceutical Science"=>1}}, "reader_count_by_country"=>{"United Kingdom"=>1, "Chile"=>1}, "group_count"=>0}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/2125264"], "description"=>"<p>(A) Top panel: lifetime images before, during, and after uncaging showing that the lifetime change of Camui (Camui, LT) is restricted to the stimulated spine, as indicated by the change of pseudo-color from orange to yellow; the location of glutamate uncaging is indicated by an asterisk. Middle panel: Camui content of spines, as measured by single-photon counting of GFP fluorescence (Camui, SPC), dramatically increased in stimulated spine. Bottom panel: fluorescent images of the volume marker mCherry (Cherry, F) showing spine enlargement after glutamate uncaging. Scale bar units: top–ns/pixel, middle–photons/pixel, bottom–AU. (B) Fluorescence lifetime response of WT Camui produced by glutamate uncaging (average of 35 spine experiments, filled black circles) overlapped with fitted double exponential (green) and underlying the first (dash red) and the second (dash blue) exponentials; dendritic response–black squires. (C–E) Graphs showing effects of Calyculin A (open symbols) on WT Camui fluorescence lifetime (raw, C and scaled, D) and spine size (E) in comparison to control conditions (filled symbols). Glutamate uncaging protocol (eight pulses at 0.5 Hz) was started at time 0 (horizontal black bar).</p>", "links"=>[], "tags"=>["wt", "decay", "2a", "pp", "basal activation state", "phosphatase", "tau 1", "CaMKII FRET Sensor Signal", "basal Camui activation state", "ltp", "inhibitor", "T 286 dephosphorylation", "286D"], "article_id"=>1453648, "categories"=>["Biological Sciences"], "users"=>["Nikolai Otmakhov", "Shaurav Regmi", "John E. Lisman"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0130457.g001", "stats"=>{"downloads"=>0, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Fast_decay_of_Camui_signal_is_not_affected_by_Calyculin_A_an_inhibitor_of_PP1_PP2A_/1453648", "title"=>"Fast decay of Camui signal is not affected by Calyculin A, an inhibitor of PP1/PP2A.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-06-18 03:50:05"}
  • {"files"=>["https://ndownloader.figshare.com/files/2125266"], "description"=>"<p>(A, B, and D) Graphs of fluorescent lifetime change after glutamate uncaging of WT Camui (filled symbols), T286D/T305A/T306A and T305A/T306A Camui mutants (open symbols), T286D/T305D/T306D—gray symbols; (A) and (D), raw and (B), scaled data. (C) Change in spine size. Glutamate uncaging protocol (eight pulses at 0.5 Hz, horizontal black bar) started at time 0. (E) Bar diagram of basal fluorescence lifetime change in different experimental conditions in comparison to basal lifetime of WT Camui. Shadow line at the bottom indicates SE of basal lifetime for WT Camui. Stars indicate statistical significance change relative the basal lifetime of WT Camui.</p>", "links"=>[], "tags"=>["wt", "decay", "2a", "pp", "basal activation state", "phosphatase", "tau 1", "CaMKII FRET Sensor Signal", "basal Camui activation state", "ltp", "inhibitor", "T 286 dephosphorylation", "286D"], "article_id"=>1453650, "categories"=>["Biological Sciences"], "users"=>["Nikolai Otmakhov", "Shaurav Regmi", "John E. Lisman"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0130457.g002", "stats"=>{"downloads"=>1, "page_views"=>24, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_T286D_T305A_T306A_Camui_mutant_is_further_activated_by_spine_stimulation_and_has_deactivation_similar_to_that_of_WT_Camui_/1453650", "title"=>"T286D/T305A/T306A Camui mutant is further activated by spine stimulation and has deactivation similar to that of WT Camui.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-06-18 03:50:05"}
  • {"files"=>["https://ndownloader.figshare.com/files/2125268", "https://ndownloader.figshare.com/files/2125269", "https://ndownloader.figshare.com/files/2125270", "https://ndownloader.figshare.com/files/2125271", "https://ndownloader.figshare.com/files/2125272"], "description"=>"<div><p>Because CaMKII is the critical Ca<sup>2+</sup> sensor that triggers long-term potentiation (LTP), understanding its activation and deactivation is important. A major advance has been the development of a FRET indicator of the conformational state of CaMKII called Camui. Experiments using Camui have demonstrated that the open (active) conformation increases during LTP induction and then decays in tens of seconds, with the major fast component decaying with a time-constant of ~ 6 sec (tau1). Because this decay is faster if autophosphorylation of T286 is prevented (the autophosphorylation prolongs activity by making the enzyme active even after Ca<sup>2+</sup> falls), it seemed likely that the fast decay is due to the T286 dephosphorylation. To test this interpretation, we studied the effect of phosphatase inhibitors on the single-spine Camui signal evoked by two-photon glutamate uncaging. We applied inhibitors of PP1 and PP2A, two phosphatases that are present at synapses and that have been shown to dephosphorylate CaMKII <i>in vitro</i>. The inhibitors increased the basal Camui activation state, indicating their effectiveness in cells. However, in no case did we find that tau1 was prolonged, contrary to what would be expected if the decay was phosphatase-dependent. This could either mean that decay was due to some unknown phosphatase or that the decay was not due to dephosphorylation. To distinguish between these possibilities, we expressed pseudo-phosphorylated Camui (T286D) (plus additional mutations [T/A] that prevented inhibitory 305/306 phosphorylation). This form had an elevated basal activation state, but was further activated during glutamate uncaging; importantly the activation state decayed with tau1 nearly the same as that of WT Camui. Therefore, the data strongly indicate that tau1 is not due to T286 dephosphorylation. We conclude that, although Camui is an excellent tool for observing CaMKII signaling, further experimentation is needed to determine how CaMKII is turned off by its dephosphorylation.</p></div>", "links"=>[], "tags"=>["wt", "decay", "2a", "pp", "basal activation state", "phosphatase", "tau 1", "CaMKII FRET Sensor Signal", "basal Camui activation state", "ltp", "inhibitor", "T 286 dephosphorylation", "286D"], "article_id"=>1453652, "categories"=>["Biological Sciences"], "users"=>["Nikolai Otmakhov", "Shaurav Regmi", "John E. Lisman"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0130457.s001", "https://dx.doi.org/10.1371/journal.pone.0130457.s002", "https://dx.doi.org/10.1371/journal.pone.0130457.s003", "https://dx.doi.org/10.1371/journal.pone.0130457.s004", "https://dx.doi.org/10.1371/journal.pone.0130457.s005"], "stats"=>{"downloads"=>4, "page_views"=>13, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Fast_Decay_of_CaMKII_FRET_Sensor_Signal_in_Spines_after_LTP_Induction_Is_Not_Due_to_Its_Dephosphorylation_/1453652", "title"=>"Fast Decay of CaMKII FRET Sensor Signal in Spines after LTP Induction Is Not Due to Its Dephosphorylation", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2015-06-18 03:50:05"}

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Relative Metric

{"start_date"=>"2015-01-01T00:00:00Z", "end_date"=>"2015-12-31T00:00:00Z", "subject_areas"=>[]}
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