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• W2015305274 startingPage "e1002831" @default.
• W2015305274 abstract "The Rho family of GTPases control actin organization during diverse cellular responses (migration, cytokinesis and endocytosis). Although the primary members of this family (RhoA, Rac and Cdc42) have different downstream effects on actin remodeling, the basic mechanism involves targeting to the plasma membrane and activation by GTP binding. Our hypothesis is that the details of GTPase cycling between membrane and cytosol are key to the differential upstream regulation of these biochemical switches. Accordingly, we developed a modeling framework to analyze experimental data for these systems. This analysis can reveal details of GDI-mediated cycling and help distinguish between GDI-dependent and -independent mechanisms, including vesicle trafficking and direct association-dissociation of GTPase with membrane molecules. Analysis of experimental data for Rac membrane cycling reveals that the lower apparent affinity of GDI for RacGTP compared to RacGDP can be fully explained by the faster dissociation of the latter from the membrane. Non-dimensional steady-state solutions for membrane fraction of GTPase are presented in multidimensional charts. This methodology is then used to analyze glucose stimulated Rac cycling in pancreatic β-cells. The charts are used to illustrate the effects of GEFs/GAPs and regulated affinities between GTPases and membrane and/or GDI on the amount of membrane bound GTPase. In a similar fashion, the charts can be used as a guide in assessing how targeted modifications may compensate for altered GTPase-GDI balance in disease scenarios." @default.
• W2015305274 created "2016-06-24" @default.
• W2015305274 creator A5004997277 @default.
• W2015305274 creator A5019048997 @default.
• W2015305274 date "2013-01-10" @default.
• W2015305274 modified "2023-10-13" @default.
• W2015305274 title "Computational Analysis of Rho GTPase Cycling" @default.
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• W2015305274 doi "https://doi.org/10.1371/journal.pcbi.1002831" @default.
• W2015305274 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3542069" @default.
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