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Merck
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Cofilin-1 Is a Mechanosensitive Regulator of Transcription.

Frontiers in cell and developmental biology (2020-09-10)
Catarina Domingues, A Margarida Geraldo, Sandra Isabel Anjo, André Matos, Cláudio Almeida, Inês Caramelo, José A Lopes-da-Silva, Artur Paiva, João Carvalho, Ricardo Pires das Neves, Bruno Manadas, Mário Grãos
摘要

The mechanical properties of the extracellular environment are interrogated by cells and integrated through mechanotransduction. Many cellular processes depend on actomyosin-dependent contractility, which is influenced by the microenvironment's stiffness. Here, we explored the influence of substrate stiffness on the proteome of proliferating undifferentiated human umbilical cord-matrix mesenchymal stem/stromal cells. The relative abundance of several proteins changed significantly by expanding cells on soft (∼3 kPa) or stiff substrates (GPa). Many such proteins are associated with the regulation of the actin cytoskeleton, a major player of mechanotransduction and cell physiology in response to mechanical cues. Specifically, Cofilin-1 levels were elevated in cells cultured on soft comparing with stiff substrates. Furthermore, Cofilin-1 was de-phosphorylated (active) and present in the nuclei of cells kept on soft substrates, in contrast with phosphorylated (inactive) and widespread distribution in cells on stiff. Soft substrates promoted Cofilin-1-dependent increased RNA transcription and faster RNA polymerase II-mediated transcription elongation. Cofilin-1 is part of a novel mechanism linking mechanotransduction and transcription.

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Sigma-Aldrich
Blebbistatin, Racemic, InSolution, ≥97%, 50 mM in 90% DMSO, reversible inhibitor of nonmuscle myosin II
Sigma-Aldrich
LIM Kinase Inhibitor I, LIMKi 3, The LIM Kinase Inhibitor I, LIMKi 3 controls the biological activity of LIM Kinase. This small molecule/inhibitor is primarily used for Phosphorylation & Dephosphorylation applications.