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Strong negative feedback from Erk to Raf confers robustness to MAPK signalling.


ABSTRACT: Protein levels within signal transduction pathways vary strongly from cell to cell. Here, we analysed how signalling pathways can still process information quantitatively despite strong heterogeneity in protein levels. We systematically perturbed the protein levels of Erk, the terminal kinase in the MAPK signalling pathway in a panel of human cell lines. We found that the steady-state phosphorylation of Erk is very robust against perturbations of Erk protein level. Although a multitude of mechanisms exist that may provide robustness against fluctuating protein levels, we found that one single feedback from Erk to Raf-1 accounts for the observed robustness. Surprisingly, robustness is provided through a fast post-translational mechanism although variation of Erk levels occurs on a timescale of days.

SUBMITTER: Fritsche-Guenther R 

PROVIDER: S-EPMC3130559 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature

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Strong negative feedback from Erk to Raf confers robustness to MAPK signalling.

Fritsche-Guenther Raphaela R   Witzel Franziska F   Sieber Anja A   Herr Ricarda R   Schmidt Nadine N   Braun Sandra S   Brummer Tilman T   Sers Christine C   Blüthgen Nils N  

Molecular systems biology 20110501


Protein levels within signal transduction pathways vary strongly from cell to cell. Here, we analysed how signalling pathways can still process information quantitatively despite strong heterogeneity in protein levels. We systematically perturbed the protein levels of Erk, the terminal kinase in the MAPK signalling pathway in a panel of human cell lines. We found that the steady-state phosphorylation of Erk is very robust against perturbations of Erk protein level. Although a multitude of mechan  ...[more]

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