Protein Domains of GTPases on Membranes: Do They Rely on Turings Mechanism?

Research output: Contribution to book/conference proceedings/anthology/reportChapter in book/anthology/reportContributedpeer-review



We evaluate different mechanisms for spatial domain formation of guanosine triphosphatases (GTPases) on cellular membranes. A kinetic model of the basic guanine-nucleotide cycle common to all GTPases is developed and coupled along a one-dimensional axis by diffusion of inactive and activated GTPases. We ask whether a parameter set exists such that domain formation is possible by Turing’s mechanism, i.e., purely by reactions and diffusion, and show that the Turing instability does not occur in this model for any parameter combination. But, as revealed by stability and bifurcation analysis, domain formation is reproduced after augmenting the model with combinations of two spatial interaction mechanisms: 1. attraction and 2. adhesion among active GTPases. These interactions can be mediated by effector proteins that bind active GTPases, and the model therefore predicts domains to disintegrate if effector binding is inhibited.


Original languageEnglish
Title of host publicationMathematical Modeling of Biological Systems
EditorsAndreas Deutsch, Lutz Brusch, Helen Byrne, Gerda de Vries, Hanspeter Herzel
Place of PublicationBoston
PublisherBirkhauser Boston
Number of pages14
VolumeVolume I
Publication statusPublished - 2006

Publication series

SeriesModeling and Simulation in Science, Engineering and Technology (MSSET)

External IDs

researchoutputwizard legacy.publication#10169
Scopus 85028025922
ORCID /0000-0003-0137-5106/work/142244195