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Kinases are enzymes that catalyze the addition of a phosphate group (PO43−) to substrates, usually proteins. The phosphate generally comes from adenosine triphosphate (ATP). Kinases and phosphatases, which remove phosphate groups, are involved in nearly all signal transduction processes, often with cascades of phosphorylation events.
Real-time biosensors have been developed for visualizing kinase activity dynamics, but they are confronted with many challenges. Here, the authors develop a light-gated KINACT integrator for post hoc analysis of transient kinase activity and signalling manipulation.
Cryo-electron microscopy and biochemical analysis reveal the activation mechanism of protein arginine kinase McsB by its activator McsA for protein quality control under stress in Gram-positive bacteria.
The inhibitor of kB kinase (IKK) is a central regulator of NF-kB signalling. Here the authors identify a motif conserved in substrates of canonical and alternative NF-kB pathways which mediates docking to catalytic IKK dimers: they show that phosphorylation of the conserved tyrosine suppresses the docking interaction.
Histidine kinases (HK) are the main component of a wide-spread signal transduction system in bacteria that are essential for cell viability, however, the details of HK autophosphorylation remain poorly understood. Here, the authors utilize a multi-scale simulation approach to investigate the mechanism of activation and autophosphorylation process, revealing the rate determining step and reaction free energy of the process.
Ferroptosis, a cell death mechanism induced by lipid peroxidation, is pivotal in tumor suppression. A recent study shows that tumor repopulating cells evade ferroptosis and develop resistance to therapy via subverting a lipid metabolism enzyme.
Understanding the role of pyrophosphorylation requires specific analytical strategies to discriminate it from protein phosphorylation. A custom workflow reveals that nucleolar protein pyrophosphorylation in human cells regulates the transcription of ribosomal DNA.
Reprogramming intercellular mechanotransduction and signaling pathways is still challenging. A recent advance uses a plug-and-play DNA nanodevice to allow non-mechanosensitive receptor tyrosine kinase (RTK) to transmit force-induced cellular signals.
Cells use various metabolic pathways to synthesize the building blocks for growth and proliferation. To ensure balanced growth, these biosynthetic processes must be tightly coordinated. We describe a molecular machinery that senses the cellular capacity to make lipids to regulate other biosynthetic processes — such as protein synthesis — accordingly.
