Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR23902572_1.fastq.gz | Fastqsanger.gz | |||
| SRR23902572_2.fastq.gz | Fastqsanger.gz | |||
| SRR23902573_1.fastq.gz | Fastqsanger.gz | |||
| SRR23902573_2.fastq.gz | Fastqsanger.gz | |||
| SRR23902574_1.fastq.gz | Fastqsanger.gz |
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Project description:This 121-node Boolean regulatory network model that synthesizes mechanosensitive signaling that links anchorage and matrix stiffness to proliferation and migration, and cell density to contact inhibition. It can reproduce anchorage dependence and anoikis, detachment-induced cytokinesis errors, the effect of matrix stiffness on proliferation, and contact inhibition of proliferation and migration by two mechanisms that converge on the YAP transcription factor. In addition, this model offers testable predictions related to cell cycle-dependent sensitivity to anoikis, the molecular requirements for abolishing contact inhibition, substrate stiffness-dependent expression of the catalytic subunit of PI3K, heterogeneity of migratory and non-migratory phenotypes in sub-confluent monolayers, and linked inhibition but semi-independent induction of proliferation versus migration as a function of cell density and mitogenic stimulation.
The model is an extended version of the growth signaling, cell cycle and apoptosis model published in Sizek et al, PLoS Comp. Biol. 15(3): e1006402, 2019.
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Project description:Reiterer2013 - pseudophosphatase STYX role in
ERK signalling
This model is described in the article:
Pseudophosphatase STYX
modulates cell-fate decisions and cell migration by
spatiotemporal regulation of ERK1/2.
Reiterer V, Fey D, Kolch W,
Kholodenko BN, Farhan H.
Proc. Natl. Acad. Sci. U.S.A. 2013 Jul;
110(31): E2934-43
Abstract:
Serine/threonine/tyrosine-interacting protein (STYX) is a
catalytically inactive member of the dual-specificity
phosphatases (DUSPs) family. Whereas the role of DUSPs in
cellular signaling is well explored, the function of STYX is
still unknown. Here, we identify STYX as a spatial regulator of
ERK signaling. We used predictive-model simulation to test
several hypotheses for possible modes of STYX action. We show
that STYX localizes to the nucleus, competes with nuclear DUSP4
for binding to ERK, and acts as a nuclear anchor that regulates
ERK nuclear export. Depletion of STYX increases ERK activity in
both cytosol and nucleus. Importantly, depletion of STYX causes
an ERK-dependent fragmentation of the Golgi apparatus and
inhibits Golgi polarization and directional cell migration.
Finally, we show that overexpression of STYX reduces ERK1/2
activation, thereby blocking PC12 cell differentiation.
Overall, our results identify STYX as an important regulator of
ERK1/2 signaling critical for cell migration and PC12 cell
differentiation.
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2024-09-02 | BIOMD0000000557 | BioModels