Multisolitons-like patterns in a one-dimensional MARCKS protein cyclic model

被引:1
|
作者
Fouedji, Chenceline [1 ]
Eteme, Armand Sylvin [1 ]
Tabi, Conrad Bertrand [2 ]
Fouda, Henri Paul Ekobena [1 ]
Kofane, Timoleon Crepin [3 ]
机构
[1] Univ Yaounde I, Fac Sci, Dept Phys, Lab Biophys, POB 812, Yaounde, Cameroon
[2] Botswana Int Univ Sci & Technol, P-Bag 16, Palapye, Botswana
[3] Univ Yaounde I, Fac Sci, Dept Phys, Lab Mech, POB 812, Yaounde, Cameroon
关键词
MARCKS protein; Long wavelength instability; Patterns formation; Multisolitons; C-KINASE SUBSTRATE; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE; BISOLITON MECHANISM; EFFECTOR DOMAIN; PHOSPHORYLATION; PEPTIDE; BINDING; CA2+; INHIBITION; PRESSURE;
D O I
10.1016/j.jtbi.2023.111702
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
In this paper, we study the nonlinear dynamics of the MARCKS protein between cytosol and cytoplasmic membrane through the modulational instability phenomenon. The reaction-diffusion generic model used here is firstly transformed into a cubic complex Ginzburg-Landau equation. Then, modulational instability (MI) is carried out in order to derive the MI criteria. We find the domains of some parameter space where nonlinear patterns are expected in the model. The analytical results on the MI growth rate predict that phosphorylation and binding rates affect MARCKS dynamics in opposite way: while the phosphorylation rate tends to support highly localized structures of MARCKS, the binding rate in turn tends to slow down such features. On the other hand, self-diffusion process always amplifies the MI phenomenon. These predictions are confirmed by numerical simulations. As a result, the cyclic transport of MARCKS protein from membrane to cytosol may be done by means of multisolitons-like patterns.
引用
收藏
页数:9
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