{"database":"BioModels","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Other":["https://www.ebi.ac.uk/biomodels/model/download/MODEL1505130001?filename=paper_figs_Jalil_Sacktor_Shouval.m"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"submitter":["Sajiya Jalil"],"curationStatus":["Non-curated"],"modellingApproach":["ordinary differential equation model"],"levelVersion":["*"],"full_dataset_link":["https://www.ebi.ac.uk/biomodels/MODEL1505130001"],"publication_pubmed":["26077687"],"isPrivate":["false"],"repository":["BioModels"],"modelFormat":["MATLAB (Octave)"],"omics_type":["Models"],"tokenised_name":["Jalil2015   Atypical protein kinase C isoforms in memory maintenance (Model2)"],"publication_year":["2015"],"submissionId":["MODEL1505130001"],"publication_authors":["Sajiya J Jalil, Todd Charlton Sacktor, Harel Z Shouval"],"first_author":["Sajiya J Jalil"],"publication":["26077687,\n                            Memories that last a lifetime are thought to be stored, at least in part, as persistent enhancement of the strength of particular synapses. The synaptic mechanism of these persistent changes, late long-term potentiation (L-LTP), depends on the state and number of specific synaptic proteins. Synaptic proteins, however, have limited dwell times due to molecular turnover and diffusion, leading to a fundamental question: how can this transient molecular machinery store memories lasting a lifetime? Because the persistent changes in efficacy are synapse-specific, the underlying molecular mechanisms must to a degree reside locally in synapses. Extensive experimental evidence points to atypical protein kinase C (aPKC) isoforms as key components involved in memory maintenance. Furthermore, it is evident that establishing long-term memory requires new protein synthesis. However, a comprehensive model has not been developed describing how these components work to preserve synaptic efficacies over time. We propose a molecular model that can account for key empirical properties of L-LTP, including its protein synthesis dependence, dependence on aPKCs, and synapse-specificity. Simulations and empirical data suggest that either of the two aPKC subtypes in hippocampal neurons, PKMζ and PKCι/λ, can maintain L-LTP, making the system more robust. Given genetic compensation at the level of synthesis of these PKC subtypes as in knockout mice, this system is able to maintain L-LTP and memory when one of the pathways is eliminated.. 7, 22.\n                            Department of Neurobiology and Anatomy, The University of Texas Medical School at Houston, Houston, Texas 77030, USA."],"submitter_mail":["Sajiya.J.Jalil@uth.tmc.edu"],"submitter_affiliation":["Medical School, UTHealth"],"pubmed_abstract":["Memories that last a lifetime are thought to be stored, at least in part, as persistent enhancement of the strength of particular synapses. The synaptic mechanism of these persistent changes, late long-term potentiation (L-LTP), depends on the state and number of specific synaptic proteins. Synaptic proteins, however, have limited dwell times due to molecular turnover and diffusion, leading to a fundamental question: how can this transient molecular machinery store memories lasting a lifetime? Because the persistent changes in efficacy are synapse-specific, the underlying molecular mechanisms must to a degree reside locally in synapses. Extensive experimental evidence points to atypical protein kinase C (aPKC) isoforms as key components involved in memory maintenance. Furthermore, it is evident that establishing long-term memory requires new protein synthesis. However, a comprehensive model has not been developed describing how these components work to preserve synaptic efficacies over time. We propose a molecular model that can account for key empirical properties of L-LTP, including its protein synthesis dependence, dependence on aPKCs, and synapse-specificity. Simulations and empirical data suggest that either of the two aPKC subtypes in hippocampal neurons, PKMζ and PKCι/λ, can maintain L-LTP, making the system more robust. Given genetic compensation at the level of synthesis of these PKC subtypes as in knockout mice, this system is able to maintain L-LTP and memory when one of the pathways is eliminated."],"pubmed_title":["Atypical PKCs in memory maintenance: the roles of feedback and redundancy."],"pubmed_authors":["Jalil Sajiya J SJ, Sacktor Todd Charlton TC, Shouval Harel Z HZ"],"name_synonyms":["Phospholipid Sensitive Calcium Dependent Protein Kinase, atypia, Phospholipid-Dependent Kinase, Serine-Threonine Kinase, PKC, aberrant, Protein Kinase M, Maintenances., Phospholipid-Sensitive Calcium-Dependent Protein Kinase, atypical, defective, PKC Serine-Threonine Kinase, Calcium-Activated, PKC Serine Threonine Kinase, Calcium-Activated Phospholipid-Dependent Kinase, Calcium Phospholipid Dependent Protein Kinase, Calcium Phospholipid-Dependent Protein Kinase, Calcium Activated Phospholipid Dependent Kinase"],"pubmed_title_synonyms":["atypia, Lys-Arg-Ala-Lys-Ala-Lys-Thr-Thr-Lys-Lys-Arg, atypical, defective, aberrant, Maintenances, Feedbacks., PKCS"],"description_synonyms":["Desc, DESCR., Description, Descriptive, Descriptor, description, Product Description/Appearance"],"pubmed_abstract_synonyms":["DaPKC, glycogen synthase kinase activity, protein translation, Memory, degree (angle), protein kinase A activity, Laboratory, PKC-53B, CG42783, Mus domesticus, cPKCgamma, CASP-14, sci, House Mouse, Calcium Phospholipid-Dependent Protein Kinase, nPKCepsilon, Long Term, Prp4 protein kinase activity, Serine-Threonine Kinase, InaC, INAC, ATP-protein transphosphorylase activity, ATP:protein phosphotransferase (non-specific) activity, HOW, How, Protein Kinase M, Synapse, IFITMD1, mitogen-activated protein kinase activity, Prkcc, cPKCbeta, CG10261, Effect, l(3)j5D5, IKKg, KEY, Key, multicellular organismal biosynthetic process, cPKCalpha, 24B, nPKCdelta, single-organism biosynthetic process, nPKCtheta, BFIS2, Migrant Worker, nPKC, RATPKCI, cPKC, Molecular, anabolism, Nonmigrant, stru, PKCbeta, Swiss 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protein kinase activity, Migrants and Transients, diacylglycerol-activated phospholipid-dependent protein kinase C activity, Molecular Models, Mus musculus, phosphorylase B kinase kinase activity, DPKC, PKCdelta, Nerve Cells, protein glutamyl kinase activity, Caspase-14 subunit p10, mice, IKK-gamma, PKC-98F, Swiss Mouse, psu, non-specific serine/threonine protein kinase activity, aPKCzeta, Caspase-14 subunit p19, ICCA, MICE, Calcium Phospholipid Dependent Protein Kinase, Prkc, domesticus, synaptic junction, hydroxyalkyl-protein kinase activity, WEE1Hu, DmelCG16910, protein synthesis, dPKC, serine-specific protein kinase activity, epsilon PKC, Cells, HIPK2, cytidine 3', electrotonic synapse, Dmel_CG10261, anon-EST:Liang-2.39, Migrants, inherited genetic, Mouse, eye-PKC, Wee 1-like kinase activity, CG30475, PKCgamma, 3.4.22.-, atypia, ribosomal S6 protein kinase activity, calcium/phospholipid-dependent protein kinase activity, 98F, glycogen synthase A kinase activity, Effects, ePKC, P62, glycogen synthase kinase 3 activity, Nerve, number, PKC activity, Gene, Remote Memory, mini-ICE, biosynthesis, PKCalpha, Migrant Workers, dIKK-gamma, phosphorylase b kinase kinase activity, DmelCG42783, PKC 98F, House, diacylglycerol-activated phospholipid-dependent PKC activity, DmIKK-gamma, Gene Products, pkc-2, Mus musculus domesticus, pkc-3, CG6622, serine(threonine) protein kinase activity, atypical, dmIKKgamma, Long Term Potentiation, IKK[[gamma]], ribosomal protein S6 kinase II activity, Mice, Aggravating interaction, T-antigen kinase activity, PKC 53B, galactosyltransferase-associated kinase activity, PKC 53E, protein-serine kinase activity, LTP., anatomical systems, l(3)s2612, Longterm, formation, Swiss, Transients, a-PKC, STK32, Nonmigrants, PKCzeta, Long-Term, Worker, dependence, DYT10, Maintenances, synthesis, Squatter, protein kinase (phosphorylating) activity, protein kinase Cepsilon activity, IKK, protein-cysteine kinase activity, DmelCG6518, Raf-1, nPKCeta, Nc98F, Hpr 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