ArticleBMC systems biology2012
Regulation of cytoplasmic polyadenylation can generate a bistable switch.
Article in BMC systems biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 13 citations in OpenAlex.
- Maintenance of memory by negative-feedback of synaptic protein elimination: Modeling KIBRA-bioRxiv : the preprint server for biology · 2025Article
- Computational analysis of memory consolidation following inhibitory avoidance (IA) training in adult and infant rats: Critical roles of CaMKIIα and MeCP2.PLoS computational biology · 2022Article
- Computational model of a positive BDNF feedback loop in hippocampal neurons following inhibitory avoidance training.Learning & memory (Cold Spring Harbor, N.Y.) · 2016Article
- The right time to learn: mechanisms and optimization of spaced learning.Nature reviews. Neuroscience · 2016Review
- Building synthetic memory.Current biology : CB · 2013Review
- Specificity factors in cytoplasmic polyadenylation.Wiley interdisciplinary reviews. RNAReview
- Maintenance of memory by negative feedback of synaptic protein elimination: modeling KIBRA-PKMζ dynamics in LTP.Learning & memory (Cold Spring Harbor, N.Y.)Article
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2 authors at 1 institution in 1 country.
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Abstract
backgroundTranslation efficiency of certain mRNAs can be regulated through a cytoplasmic polyadenylation process at the pre-initiation phase. A translational regulator controls the polyadenylation process and this regulation depends on its posttranslational modifications e.g., phosphorylation. The cytoplasmic polyadenylation binding protein (CPEB1) is one such translational regulator, which regulates the translation of some mRNAs by binding to the cytoplasmic polyadenylation element (CPE). The cytoplasmic polyadenylation process can be turned on or off by the phosphorylation or dephosphorylation state of CPEB1. A specific example could be the regulation of Calcium/Calmodulin-dependent protein kinase II (αCaMKII) translation through the phosphorylation/dephosphorylation cycle of CPEB1.
resultHere, we show that CPEB1 mediated polyadenylation of αCaMKII mRNA can result in a bistable switching mechanism. The switch for regulating the polyadenylation is based on a two state model of αCaMKII and its interaction with CPEB1. Based on elementary biochemical kinetics a high dimensional system of non-linear ordinary differential equations can describe the dynamic characteristics of the polyadenylation loop. Here, we simplified this high-dimensional system into approximate lower dimension system that can provide the understanding of dynamics and fixed points of original system. These simplified equations can be used to develop analytical bifurcation diagrams without the use of complex numerical tracking algorithm, and can further give us intuition about the parameter dependence of bistability in this system.
conclusionThis study provides a systematic method to simplify, approximate and analyze a translation/activation based positive feedback loop. This work shows how to extract low dimensional systems that can be used to obtain analytical solutions for the fixed points of the system and to describe the dynamics of the system. The methods used here have general applicability to the formulation and analysis of many molecular networks.
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