Enhancement of Tunability of MAPK Cascade Due to Coexistence of Processive and Distributive Phosphorylation Mechanisms
文献类型:期刊论文
作者 | Sun, Jianqiang1,2; Yi, Ming1,3; Yang, Lijian4,5; Wei, Wenbin4,5; Ding, Yiming1; Jia, Ya4,5 |
刊名 | BIOPHYSICAL JOURNAL
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出版日期 | 2014-03-04 |
卷号 | 106期号:5页码:1215-1226 |
英文摘要 | The processive phosphorylation mechanism becomes important when there is macromolecular crowding in the cytoplasm. Integrating the processive phosphorylation mechanism with the traditional distributive one, we propose a mixed dual-site phosphorylation (MDP) mechanism in a single-layer phosphorylation cycle. Further, we build a degree model by applying the MDP mechanism to a three-layer mitogen-activated protein kinase (MAPK) cascade. By bifurcation analysis, our study suggests that the crowded-environment-induced pseudoprocessive mechanism can qualitatively change the response of this biological network. By adjusting the degree of processivity in our model, we find that the MAPK cascade is able to switch between the ultrasensitivity, bistability, and oscillatory dynamical states. Sensitivity analysis shows that the theoretical results remain unchanged within a reasonably chosen variation of parameter perturbation. By scaling the reaction rates and also introducing new connections into the kinetic scheme, we further construct a proportion model of the MAPK cascade to validate our findings. Finally, it is illustrated that the spatial propagation of the activated MAPK signal can be improved (or attenuated) by increasing the degree of processivity of kinase (or phosphatase). Our research implies that the MDP mechanism makes the MAPK cascade become a flexible signal module, and the coexistence of processive and distributive phosphorylation mechanisms enhances the tunability of the MAPK cascade. |
WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
类目[WOS] | Biophysics |
研究领域[WOS] | Biophysics |
关键词[WOS] | PROTEIN-KINASE CASCADES ; MULTISITE PHOSPHORYLATION ; POSTTRANSLATIONAL MODIFICATION ; COMPETITIVE-INHIBITION ; MOLECULAR-MECHANISMS ; ALPHA-SYNUCLEIN ; CELL-CYCLE ; BISTABILITY ; DYNAMICS ; ULTRASENSITIVITY |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000332501300024 |
公开日期 | 2015-07-14 |
源URL | [http://ir.wipm.ac.cn/handle/112942/1484] ![]() |
专题 | 武汉物理与数学研究所_数学物理与应用研究部 |
作者单位 | 1.Chinese Acad Sci, Key Lab Magnet Resonance Biol Syst, Wuhan Inst Phys & Math, Wuhan, Peoples R China 2.Univ Chinese Acad Sci, Beijing, Peoples R China 3.Chinese Acad Sci, Natl Ctr Math & Interdisciplinary Sci, Beijing, Peoples R China 4.Huazhong Normal Univ, Dept Phys, Wuhan 430070, Peoples R China 5.Huazhong Normal Univ, Inst Biophys, Wuhan, Peoples R China |
推荐引用方式 GB/T 7714 | Sun, Jianqiang,Yi, Ming,Yang, Lijian,et al. Enhancement of Tunability of MAPK Cascade Due to Coexistence of Processive and Distributive Phosphorylation Mechanisms[J]. BIOPHYSICAL JOURNAL,2014,106(5):1215-1226. |
APA | Sun, Jianqiang,Yi, Ming,Yang, Lijian,Wei, Wenbin,Ding, Yiming,&Jia, Ya.(2014).Enhancement of Tunability of MAPK Cascade Due to Coexistence of Processive and Distributive Phosphorylation Mechanisms.BIOPHYSICAL JOURNAL,106(5),1215-1226. |
MLA | Sun, Jianqiang,et al."Enhancement of Tunability of MAPK Cascade Due to Coexistence of Processive and Distributive Phosphorylation Mechanisms".BIOPHYSICAL JOURNAL 106.5(2014):1215-1226. |
入库方式: OAI收割
来源:武汉物理与数学研究所
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