Molecular Switches at the Synapse Emerge from Receptor and Kinase Traffic
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{"title"=>"Molecular switches at the synapse emerge from receptor and kinase traffic", "type"=>"journal", "authors"=>[{"first_name"=>"Arnold", "last_name"=>"Hayer", "scopus_author_id"=>"8546094600"}, {"first_name"=>"Upinder S.", "last_name"=>"Bhalla", "scopus_author_id"=>"7003761732"}], "year"=>2005, "source"=>"PLoS Computational Biology", "identifiers"=>{"sgr"=>"33749370872", "doi"=>"10.1371/journal.pcbi.0010020", "pui"=>"135774915", "pmid"=>"16110334", "scopus"=>"2-s2.0-33749370872", "issn"=>"1553734X", "isbn"=>"1553-734X (Print)\\r1553-734X (Linking)"}, "id"=>"fea1d6eb-775a-31f6-a58b-0ba7fd3ca190", "abstract"=>"Changes in the synaptic connection strengths between neurons are believed to play a role in memory formation. An important mechanism for changing synaptic strength is through movement of neurotransmitter receptors and regulatory proteins to and from the synapse. Several activity-triggered biochemical events control these movements. Here we use computer models to explore how these putative memory-related changes can be stabilised long after the initial trigger, and beyond the lifetime of synaptic molecules. We base our models on published biochemical data and experiments on the activity-dependent movement of a glutamate receptor, AMPAR, and a calcium-dependent kinase, CaMKII. We find that both of these molecules participate in distinct bistable switches. These simulated switches are effective for long periods despite molecular turnover and biochemical fluctuations arising from the small numbers of molecules in the synapse. The AMPAR switch arises from a novel self-recruitment process where the presence of sufficient receptors biases the receptor movement cycle to insert still more receptors into the synapse. The CaMKII switch arises from autophosphorylation of the kinase. The switches may function in a tightly coupled manner, or relatively independently. The latter case leads to multiple stable states of the synapse. We propose that similar self-recruitment cycles may be important for maintaining levels of many molecules that undergo regulated movement, and that these may lead to combinatorial possible stable states of systems like the synapse.", "link"=>"http://www.mendeley.com/research/molecular-switches-synapse-emerge-receptor-kinase-traffic", "reader_count"=>96, "reader_count_by_academic_status"=>{"Unspecified"=>2, "Professor > Associate Professor"=>9, "Researcher"=>22, "Student > Doctoral Student"=>4, "Student > Ph. D. Student"=>31, "Student > Postgraduate"=>2, "Student > Master"=>11, "Other"=>3, "Student > Bachelor"=>2, "Lecturer"=>1, "Professor"=>9}, "reader_count_by_user_role"=>{"Unspecified"=>2, "Professor > Associate Professor"=>9, "Researcher"=>22, "Student > Doctoral Student"=>4, "Student > Ph. D. Student"=>31, "Student > Postgraduate"=>2, "Student > Master"=>11, "Other"=>3, "Student > Bachelor"=>2, "Lecturer"=>1, "Professor"=>9}, "reader_count_by_subject_area"=>{"Engineering"=>7, "Unspecified"=>4, "Biochemistry, Genetics and Molecular Biology"=>5, "Mathematics"=>2, "Agricultural and Biological Sciences"=>54, "Medicine and Dentistry"=>2, "Neuroscience"=>6, "Physics and Astronomy"=>5, "Chemistry"=>1, "Computer Science"=>10}, "reader_count_by_subdiscipline"=>{"Engineering"=>{"Engineering"=>7}, "Medicine and Dentistry"=>{"Medicine and Dentistry"=>2}, "Neuroscience"=>{"Neuroscience"=>6}, "Chemistry"=>{"Chemistry"=>1}, "Physics and Astronomy"=>{"Physics and Astronomy"=>5}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>54}, "Computer Science"=>{"Computer Science"=>10}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>5}, "Mathematics"=>{"Mathematics"=>2}, "Unspecified"=>{"Unspecified"=>4}}, "reader_count_by_country"=>{"Greece"=>1, "United States"=>2, "Japan"=>4, "Taiwan"=>1, "United Kingdom"=>6, "Switzerland"=>3, "Germany"=>1, "India"=>1}, "group_count"=>4}

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  • {"month"=>"12", "year"=>"2016", "pdf_views"=>"5", "xml_views"=>"0", "html_views"=>"32"}
  • {"month"=>"1", "year"=>"2017", "pdf_views"=>"4", "xml_views"=>"0", "html_views"=>"34"}
  • {"month"=>"2", "year"=>"2017", "pdf_views"=>"10", "xml_views"=>"1", "html_views"=>"39"}
  • {"month"=>"3", "year"=>"2017", "pdf_views"=>"4", "xml_views"=>"0", "html_views"=>"34"}
  • {"month"=>"4", "year"=>"2017", "pdf_views"=>"7", "xml_views"=>"0", "html_views"=>"58"}
  • {"month"=>"5", "year"=>"2017", "pdf_views"=>"3", "xml_views"=>"0", "html_views"=>"31"}
  • {"month"=>"6", "year"=>"2017", "pdf_views"=>"1", "xml_views"=>"0", "html_views"=>"14"}
  • {"month"=>"7", "year"=>"2017", "pdf_views"=>"9", "xml_views"=>"0", "html_views"=>"27"}
  • {"month"=>"8", "year"=>"2017", "pdf_views"=>"9", "xml_views"=>"1", "html_views"=>"24"}
  • {"month"=>"9", "year"=>"2017", "pdf_views"=>"7", "xml_views"=>"2", "html_views"=>"26"}
  • {"month"=>"10", "year"=>"2017", "pdf_views"=>"1", "xml_views"=>"1", "html_views"=>"16"}
  • {"month"=>"11", "year"=>"2017", "pdf_views"=>"6", "xml_views"=>"1", "html_views"=>"24"}
  • {"month"=>"12", "year"=>"2017", "pdf_views"=>"3", "xml_views"=>"0", "html_views"=>"13"}
  • {"month"=>"1", "year"=>"2018", "pdf_views"=>"0", "xml_views"=>"0", "html_views"=>"7"}
  • {"month"=>"2", "year"=>"2018", "pdf_views"=>"3", "xml_views"=>"0", "html_views"=>"7"}
  • {"month"=>"3", "year"=>"2018", "pdf_views"=>"1", "xml_views"=>"0", "html_views"=>"3"}
  • {"month"=>"4", "year"=>"2018", "pdf_views"=>"3", "xml_views"=>"0", "html_views"=>"6"}
  • {"month"=>"5", "year"=>"2018", "pdf_views"=>"6", "xml_views"=>"0", "html_views"=>"7"}
  • {"month"=>"6", "year"=>"2018", "pdf_views"=>"7", "xml_views"=>"0", "html_views"=>"12"}
  • {"month"=>"7", "year"=>"2018", "pdf_views"=>"4", "xml_views"=>"4", "html_views"=>"4"}
  • {"month"=>"8", "year"=>"2018", "pdf_views"=>"1", "xml_views"=>"1", "html_views"=>"18"}
  • {"month"=>"9", "year"=>"2018", "pdf_views"=>"8", "xml_views"=>"0", "html_views"=>"6"}
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  • {"month"=>"8", "year"=>"2019", "pdf_views"=>"5", "xml_views"=>"0", "html_views"=>"17"}

Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/472864", "https://ndownloader.figshare.com/files/472872", "https://ndownloader.figshare.com/files/472881"], "description"=>"<div><p>Changes in the synaptic connection strengths between neurons are believed to play a role in memory formation. An important mechanism for changing synaptic strength is through movement of neurotransmitter receptors and regulatory proteins to and from the synapse. Several activity-triggered biochemical events control these movements. Here we use computer models to explore how these putative memory-related changes can be stabilised long after the initial trigger, and beyond the lifetime of synaptic molecules. We base our models on published biochemical data and experiments on the activity-dependent movement of a glutamate receptor, AMPAR, and a calcium-dependent kinase, CaMKII. We find that both of these molecules participate in distinct bistable switches. These simulated switches are effective for long periods despite molecular turnover and biochemical fluctuations arising from the small numbers of molecules in the synapse. The AMPAR switch arises from a novel self-recruitment process where the presence of sufficient receptors biases the receptor movement cycle to insert still more receptors into the synapse. The CaMKII switch arises from autophosphorylation of the kinase. The switches may function in a tightly coupled manner, or relatively independently. The latter case leads to multiple stable states of the synapse. We propose that similar self-recruitment cycles may be important for maintaining levels of many molecules that undergo regulated movement, and that these may lead to combinatorial possible stable states of systems like the synapse.</p></div>", "links"=>[], "tags"=>["molecular", "switches", "synapse", "receptor", "kinase"], "article_id"=>153178, "categories"=>["Biological Sciences", "Biochemistry", "Neuroscience", "Cell Biology", "Medicine"], "users"=>["Arnold Hayer", "Upinder S Bhalla"], "doi"=>["https://dx.doi.org/10.1371/journal.pcbi.0010020.sg001", "https://dx.doi.org/10.1371/journal.pcbi.0010020.sg002", "https://dx.doi.org/10.1371/journal.pcbi.0010020.sd001"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Molecular_Switches_at_the_Synapse_Emerge_from_Receptor_and_Kinase_Traffic/153178", "title"=>"Molecular Switches at the Synapse Emerge from Receptor and Kinase Traffic", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2013-01-20 10:57:04"}
  • {"files"=>["https://ndownloader.figshare.com/files/962414"], "description"=>"<div><p>(A) Overview of model, indicating key trafficking steps for AMPAR and CaMKII.</p><p>(B–H) Chemical reaction schemes for pathways in model. Curved lines with arrows are enzymatic reactions catalyzed by molecules at the curves. Straight lines represent binding or unimolecular reactions.</p><p>(B) Details of AMPAR model. The modelled AMPAR is a tetramer with two subunits each of GluR1 (circles) and GluR2 (triangles). There are 16 phosphorylation states each in the cytosol and synaptic membrane. These are represented in expanded form in the lower portion of (B), which shows the internalised pools of receptors. Black filling of the left half of the GluR1 circle indicates phosphorylation of Ser845, and of the right half indicates phosphorylation of Ser831. Endocytosis occurs for the receptors with no GluR1-Ser845 phosphorylation, and exocytosis and degradation occur for the receptors with both GluR1 subunits phosphorylated on the Ser845 site. Exchange of receptors with the bulk AMPAR pool occurs for the unphosphorylated state only, outlined in black.</p><p>(C) CaMKII model. The dashed line for phosphorylation of CaMKII–PSD is applicable only for the bistable CaMKII models described in <a href=\"http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.0010020#pcbi-0010020-g007\" target=\"_blank\">Figure 7</a>.</p><p>(D) CaM activation.</p><p>(E) PP1 activation.</p><p>(F) PP2B (calcineurin) activation.</p><p>(G) cAMP formation. The unstimulated phosphodiesterase molecules (PDEs) also degrade cAMP, but at a lower rate than the activated forms illustrated. In the cAMP model we include diffusive exchange of cAMP with a dendritic compartment.</p><p>(H) PKA activation.</p><p>AMP, adenosine monophosphate; ATP, adenosine triphosphate; I1, inhibitor of PP1; Ng, neurogranin; PKA_inhib, inhibitor of PKA; PKC, protein kinase C; PP2A, protein phosphatase 2A.</p></div>", "links"=>[], "tags"=>["Biochemistry", "Computational biology", "cell biology", "neuroscience", "computational biology/systems biology"], "article_id"=>632399, "categories"=>["Biological Sciences", "Biochemistry", "Neuroscience", "Cell Biology", "Medicine"], "users"=>["Arnold Hayer", "Upinder S Bhalla"], "doi"=>["https://dx.doi.org/10.1371/journal.pcbi.0010020.g001"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Model_Structure_/632399", "title"=>"Model Structure", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-22 09:04:10"}
  • {"files"=>["https://ndownloader.figshare.com/files/962545"], "description"=>"<div><p>(A) AMPAR exocytosis time course; experiments from [<a href=\"http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.0010020#pcbi-0010020-b10\" target=\"_blank\">10</a>,<a href=\"http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.0010020#pcbi-0010020-b20\" target=\"_blank\">20</a>].</p><p>(B) AMPAR endocytosis time course; experiments from [<a href=\"http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.0010020#pcbi-0010020-b10\" target=\"_blank\">10</a>,<a href=\"http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.0010020#pcbi-0010020-b21\" target=\"_blank\">21</a>].</p><p>(C) CaMKII internalisation time course; experiments from [<a href=\"http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.0010020#pcbi-0010020-b14\" target=\"_blank\">14</a>].</p><p>(D) CaMKII traffic to PSD; experiments from [<a href=\"http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.0010020#pcbi-0010020-b14\" target=\"_blank\">14</a>].</p></div>", "links"=>[], "tags"=>["trafficking"], "article_id"=>632535, "categories"=>["Biological Sciences", "Biochemistry", "Neuroscience", "Cell Biology", "Medicine"], "users"=>["Arnold Hayer", "Upinder S Bhalla"], "doi"=>["https://dx.doi.org/10.1371/journal.pcbi.0010020.g002"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Matching_Models_to_Trafficking_Time_Course_/632535", "title"=>"Matching Models to Trafficking Time Course", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-22 09:05:09"}
  • {"files"=>["https://ndownloader.figshare.com/files/962661"], "description"=>"<div><p>(A) Number of AMPARs in internal and synaptic membrane pools; AMPARs complexed to enzymes are not counted.</p><p>(B) Number of CaMKII molecules in the cytosol and PSD. The activity in the cytosol and PSD starts to rise at about 0.5 μM Ca<sup>2+</sup>, but translocation occurs around 1 μM.</p><p>(C) Conductance of membrane-inserted AMPARs. Receptor conductance is calculated by assuming that CaMKII phosphorylation of a single GluR1-Ser831 of the tetramer gives 1.5-fold basal conductance, and of two Ser831 gives 2-fold basal conductance. The conductance dips at around 300 nM Ca<sup>2+</sup>, when PP2B is active but CaMKII has yet to become fully active.</p></div>", "links"=>[], "tags"=>["camkii", "trafficking", "dependence"], "article_id"=>632643, "categories"=>["Biological Sciences", "Biochemistry", "Neuroscience", "Cell Biology", "Medicine"], "users"=>["Arnold Hayer", "Upinder S Bhalla"], "doi"=>["https://dx.doi.org/10.1371/journal.pcbi.0010020.g003"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_AMPAR_and_CaMKII_Trafficking_and_Dependence_on_Steady_Ca_2_Concentrations_/632643", "title"=>"AMPAR and CaMKII Trafficking and Dependence on Steady Ca<sup>2+</sup> Concentrations", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-22 09:05:57"}
  • {"files"=>["https://ndownloader.figshare.com/files/962770"], "description"=>"<div><p>Each panel is computed from a series of steady-state calculations where the activity of the selected input pathway was scaled with respect to its basal activity. The <i>x</i>-axis is this scaling ratio. The conductance is calculated as in <a href=\"http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.0010020#pcbi-0010020-g003\" target=\"_blank\">Figure 3</a> and is expressed as the secondary <i>y</i>-axis, as a percentage of maximal conductance (see <a href=\"http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.0010020#s4\" target=\"_blank\">Materials and Methods</a>).</p><p>(A) Changing activity of CaMKII leads to small changes in synaptic membrane localisation of AMPARs, but phosphorylation of GluR1 on Ser831 gives a doubling of synaptic conductance when CaMKII activity is scaled above basal levels.</p><p>(B) Low concentrations of PKA result in reduced exocytosis of AMPAR. Basal concentrations of PKA (ratio ~ 1) are required to localise AMPAR to the synaptic membrane, and higher concentrations cause a conductance increase. This occurs because of phosphatase saturation leading indirectly to a rise in Ser831 phosphorylation due to CaMKII. The net effect is that changes in PKA activity can lead to a large change in AMPAR conductance in either direction.</p><p>(C) Changes in PP1 concentrations have little effect on AMPAR localisation. However, low PP1 leads to high phosphorylation of GluR1-Ser831 by CaMKII, and hence high conductance.</p><p>(D) Lower rates of receptor recycling to the internal pool lead to a small increase in synaptic membrane localisation. High rates bring most of the receptor to the internal pool.</p></div>", "links"=>[], "tags"=>["synaptic", "membrane", "localisation", "conductance", "sustained"], "article_id"=>632741, "categories"=>["Biological Sciences", "Biochemistry", "Neuroscience", "Cell Biology", "Medicine"], "users"=>["Arnold Hayer", "Upinder S Bhalla"], "doi"=>["https://dx.doi.org/10.1371/journal.pcbi.0010020.g004"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_AMPAR_Synaptic_Membrane_Localisation_and_Conductance_in_Response_to_Sustained_Inputs_/632741", "title"=>"AMPAR Synaptic Membrane Localisation and Conductance in Response to Sustained Inputs", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-22 09:06:43"}
  • {"files"=>["https://ndownloader.figshare.com/files/962899"], "description"=>"<div><p>(A) Simplified schematic of receptor recycling.</p><p>(B) Bistability analysis. The flux of AMPARs from the bulk AMPAR pool to the native AMPAR pool is plotted against the total number of synaptic receptors. Receptor influx into the spine occurs both at very low and at high numbers of synaptic AMPARs.</p><p>(C) States of the system as a function of Ca<sup>2+</sup> concentration. Upper curve is obtained by starting system in state with high numbers of AMPARs in the synapse; lower curve with low numbers of AMPARs. The intermediate threshold curve is calculated using successive bisection as described in the Materials and Methods. Bistability is present when Ca<sup>2+</sup> concentration is less than 0.12 μM. Between 0.12 and 0.6 μM the system settles to a state of low AMPAR numbers. Above 0.8 μM the system is in the high state.</p><p>(D) States of the system as a function of cAMP concentration. Steady-state number of AMPARs is calculated as in (C). There is hysteresis as the high and low states coexist for the bistable region of the curve. Threshold points (open circles) complete the characteristic S-shaped curve for a bistable system.</p><p>(E) Parameter sensitivity analysis. The bars represent the range of parameter values over which the system remains bistable. Other than key regulators, the system tolerates a 2-fold or greater range of most parameters without losing bistability.</p><p>(F) Time course of AMPAR showing two stable states. A pulse of 0.2 μM cAMP is applied for 1,000 s to trigger translocation of AMPARs to the synaptic membrane. Following this, cAMP is restored to resting levels, and the system settles to the state of high membrane AMPAR. The “off” stimulus is provided by reducing cAMP to 0 μM for 6,000 s. Following this, the system settles back to the basal state of AMPAR.</p><p>(G) Stochastic runs in low and high states. The high state is triggered by an initial cAMP pulse from <i>t</i> = 0 to 4,000 s. The state spontaneously turns off at around 20 h in this run, but the low state does not flip.</p><p>(H) Average stability time of low and high states for different numbers of bulk receptors (mean ± standard error of the mean). Twenty-four simulations for each state were run, as in (G). Stability time is calculated as total simulation time in selected state, divided by number of transitions out of that state. Large symbols represent cases where no transitions occurred over the entire set of simulations. As expected, a higher level of bulk receptor increases the likelihood that the spine will spontaneously turn “on”, and vice versa.</p><p>(I) Stability time in low and high states for different numbers of anchor proteins. As the number of anchor proteins increases the stability time for both states also rises. At very large numbers of anchor proteins the synapse occasionally turns “on” spontaneously. Symbols and calculations as in (H).</p></div>", "links"=>[], "tags"=>["translocation", "bistability"], "article_id"=>632867, "categories"=>["Biological Sciences", "Biochemistry", "Neuroscience", "Cell Biology", "Medicine"], "users"=>["Arnold Hayer", "Upinder S Bhalla"], "doi"=>["https://dx.doi.org/10.1371/journal.pcbi.0010020.g005"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_AMPAR_Translocation_and_Bistability_for_Model_1_/632867", "title"=>"AMPAR Translocation and Bistability for Model 1", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-22 09:07:38"}
  • {"files"=>["https://ndownloader.figshare.com/files/962986"], "description"=>"<div><p>IR represents internal receptor, MR represents synaptic-membrane-localised receptor and asterisks indicate phosphorylation at Ser845. PKA is protein kinase A.</p><p>(A) Complete reaction diagram.</p><p>(B) Bistability analysis for simplified model. AMPAR flux between the bulk AMPAR and the IR state from (A) is plotted against the total number of synaptic receptors (IR + IR* + IR** + MR + MR* + MR**). As seen in the complete AMPAR model in <a href=\"http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.0010020#pcbi-0010020-g005\" target=\"_blank\">Figure 5</a>B, there are two regions of receptor influx into the spine, at low and high numbers of synaptic AMPARs. The zero crossings are stable states where there is no net flux of receptor.</p><p>(C–F) Time courses of key molecules in simple model. After an initial settling period, PKA is raised to 40 molecules for 2,400 s to trigger receptor influx. After the system settles into the high state, PKA is set to zero molecules for 3,600 s, to return the system to basal levels. These stimuli are indicated by horizontal bars along the time axis.</p><p>(C) Internal receptor numbers. The number of receptors in the unphosphorylated form (IR) remains very close to the bulk receptor level except during transitions, when receptors enter or leave the system.</p><p>(D) Synaptic-membrane-bound receptor levels.</p><p>(E) Numbers of free PP1 decline sharply during the high state, because of enzyme saturation.</p><p>(F) Numbers of PP1 complexes with substrates. The high amount of PP1–MR** complex is complementary to the decline in free PP1, showing the saturation of the phosphatase.</p></div>", "links"=>[], "tags"=>["ampar", "bistable"], "article_id"=>632952, "categories"=>["Biological Sciences", "Biochemistry", "Neuroscience", "Cell Biology", "Medicine"], "users"=>["Arnold Hayer", "Upinder S Bhalla"], "doi"=>["https://dx.doi.org/10.1371/journal.pcbi.0010020.g006"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Simplified_AMPAR_Bistable_Model_/632952", "title"=>"Simplified AMPAR Bistable Model", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-22 09:08:12"}
  • {"files"=>["https://ndownloader.figshare.com/files/963098"], "description"=>"<div><p>CaMKII-thr286* indicates Thr286-phosphorylated CaMKII, and CaMKII-thr286*-thr305* indicates Thr286/Thr305-phosphorylated CaMKII.</p><p>(A) Schematic of CaMKII autophosphorylation in the PSD. Reactions (in bold) and PP1 concentrations are altered in the PSD from the basal model to achieve bistability. Block arrows indicate the CaMKII states that translocate. There are two shaded sets of molecules, indicating states that are summed to give rise to an enzyme activity. The Tot-CaM-CaMKII activity is the sum of concentrations of CaM-CaMKII and CaM–Thr286-phosphorylated CaMKII. The Aut-CaMKII activity is the sum of the calcium-autonomous states Thr286-phosphorylated and Thr286/Thr305-phosphorylated CaMKII.</p><p>(B) Bistability analysis. The Aut-CaMKII molecular species has been bifurcated into Aut-CaMKII enzyme, and Aut-CaMKII readout. The enzyme activity is buffered numerically (<i>x</i>-axis). The readout (<i>y</i>-axis) remains the sum of Thr286-phosphorylated and Thr286/Thr305-phosphorylated CaMKII. Fixed points are given by the intersection points of the amount of Aut-CaMKII with the 45° line. These fixed points indicate the number of Aut-CaMKII molecules that would exactly sustain their own activity through autophosphorylation. The upper and lower points are stable, and the middle point is the transition point.</p><p>(C) Time course of bistable response. The first arrow is a Ca<sup>2+</sup> stimulus of 2.7 μM for 500 s that switches on the CaMKII bistable loop. The second arrow is a 5-fold increase in <i>k</i><sub>cat</sub> of PSD-localised PP1 for a period of 500 s, which switches CaMKII off.</p><p>(D) Parameter sensitivity analysis. Key parameters are scaled up and down and the model is tested for bistability. Most parameters can be varied 2-fold or more in either direction without the model losing bistability.</p><p>(E) Stochastic run showing stability in both high and low states, when PKA is buffered.</p><p>(F) Stochastic run showing spontaneous state flips in either direction, with the complete PKA model.</p><p>(G) Statistics of spontaneous state flips with the complete PKA model. Average turn on and turn off times are both over 15 h.</p></div>", "links"=>[], "tags"=>["camkii"], "article_id"=>633059, "categories"=>["Biological Sciences", "Biochemistry", "Neuroscience", "Cell Biology", "Medicine"], "users"=>["Arnold Hayer", "Upinder S Bhalla"], "doi"=>["https://dx.doi.org/10.1371/journal.pcbi.0010020.g007"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Bistability_in_the_CaMKII_Model_/633059", "title"=>"Bistability in the CaMKII Model", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-22 09:08:58"}
  • {"files"=>["https://ndownloader.figshare.com/files/963193"], "description"=>"<div><p>(A) Schematic of PSD-localised PP1 acting on both CaMKII and AMPAR substrates in the PSD. The asterisks on CaMKII and AMPAR represent phosphate groups.</p><p>(B) Time course of response to Ca<sup>2+</sup> (2.7 μM, 500-s duration), then cAMP (0.108 μM, 2,000-s duration) stimuli. The initial Ca<sup>2+</sup> stimulus turns on CaMKII transiently, but it eventually returns to baseline. The subsequent cAMP stimulus turns on both switches.</p><p>(C) Time course of response to cAMP (0.108 μM, 2,000-s duration), then Ca<sup>2+</sup> (2.7 μM, 500-s duration) stimuli. The initial AMPAR stimulus (cAMP elevation) is sufficient to turn both the AMPAR and the CaMKII switches on.</p><p>(D) Stochastic run in the low state. The figure illustrates a transient event that did not result in complete turn on.</p><p>(E) Stochastic run in the high state. There is a spontaneous turn off, but the average on time is over 100 h.</p></div>", "links"=>[], "tags"=>["coupled"], "article_id"=>633143, "categories"=>["Biological Sciences", "Biochemistry", "Neuroscience", "Cell Biology", "Medicine"], "users"=>["Arnold Hayer", "Upinder S Bhalla"], "doi"=>["https://dx.doi.org/10.1371/journal.pcbi.0010020.g008"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Bistability_for_Tightly_Coupled_Switches_/633143", "title"=>"Bistability for Tightly Coupled Switches", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-22 09:09:37"}
  • {"files"=>["https://ndownloader.figshare.com/files/963312"], "description"=>"<div><p>(A) Schematic of independent PSD-localised PP1 enzyme activities for CaMKII and AMPAR. The two PP1 activities are labelled PP1-PSD-CaMKII and PP1-PSD-AMPAR, respectively. The asterisks represent phosphorylation.</p><p>(B) Time course of system response to Ca<sup>2+</sup> (2.7 μM, 500-s duration), then cAMP (0.108 μM, 2,000-s duration) stimulus. The initial activation of CaMKII leads to a slow turn on of the AMPAR system.</p><p>(C) Time course of system response to cAMP (0.108 μM, 2,000-s duration), then Ca<sup>2+</sup> (2.7 μM, 500-s duration) stimulus. First the AMPAR system turns on, then, following the Ca<sup>2+</sup> stimulus, the CaMKII turns on. The conductance of the synapse has different levels in each of these states.</p><p>(D) Stochastic run for 60 h, showing resting, AMPAR only, and AMPAR + CaMKII activity states.</p></div>", "links"=>[], "tags"=>["bistability", "weakly", "coupled"], "article_id"=>633261, "categories"=>["Biological Sciences", "Biochemistry", "Neuroscience", "Cell Biology", "Medicine"], "users"=>["Arnold Hayer", "Upinder S Bhalla"], "doi"=>["https://dx.doi.org/10.1371/journal.pcbi.0010020.g009"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Nested_Bistability_for_Weakly_Coupled_Switches_/633261", "title"=>"Nested Bistability for Weakly Coupled Switches", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-22 09:10:25"}

PMC Usage Stats | Further Information

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Relative Metric

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