Articles tagged with Protein Phosphorylation
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The study reveals that CBL-CIPK complex senses specific Ca2+ signals, phosphorylates ZIP12, and initiates its partial degradation to fine-tune the plant's response to Zn deficiency environments. This negative feedback mechanism effectively regulates zinc homeostasis and maintains efficient resource utilization.
Researchers from the University of Gothenburg have made a breakthrough in understanding the role of protein tau in Alzheimer's disease. By identifying specific amino acid modifications that occur before thread-like fibrils form, scientists hope to develop complementary drugs to combat the disease.
A study reveals that protein kinase A promotes wakefulness, while protein phosphatase 1 and calcineurin promote sleep in mammals. The balance between sleep and wakefulness is regulated by multiple enzymes, including PKA, PP1, and calcineurin.
Scientists at Purdue University have identified new molecular markers for neurodegenerative diseases by analyzing protein behavior with age. The study sheds light on how phosphorylation causes protein aggregation, a hallmark of these diseases.
Researchers have developed a new protocol to exclusively access and quantify proteins carried by extracellular vesicles in the blood. This breakthrough may lead to early diagnosis of Parkinson's disease and other brain disorders, providing treatment opportunities before symptoms appear.
Researchers from Chinese Academy of Sciences have provided mechanistic insights into the activation of SLAC1, a key anion channel involved in plant guard cell signaling. Phosphorylation of SLAC1 facilitates anion efflux, leading to membrane depolarization and stomatal closure.
A new study found that combining histone deacetylase inhibitors, poly (ADP ribose) polymerase inhibitors, and decitabine resulted in synergistic cytotoxicity in all cell lines tested. This combination impaired DNA repair pathways and altered epigenetic regulation of gene expression.
Researchers at La Jolla Institute for Immunology have developed a new, rapid method to study phosphorylation and other post-translational modifications in immune cells. This method sheds light on signaling pathways that trigger T cell activation and reveals how phosphate groups direct specific gene expression responses.
Scientists at Nagoya University have discovered a novel regulatory mechanism controlling plant stomatal opening in response to red and blue light. Phosphorylation of Thr881 activates the plasma membrane proton pump, facilitating stomatal opening and enhancing photosynthetic activity.
Researchers identified a key chromatin modifier-centered pathway for grain size regulation in rice, showing that HHC4 and bZIP23 interact and enhance grain size. Phosphorylation of HHC4 by TGW3 triggers negative influences on the pathway, leading to increased rice yield.
Researchers discovered phosphorylated α-synuclein is involved in normal neuronal communication processes in a healthy brain. The protein's structure changes promote interactions with other proteins, regulating activity and synaptic function.
Researchers discovered NSMF protein's role in alleviating DNA replication stress by displacing weakly bound RPA proteins and promoting phosphorylation. This mechanism accelerates relief of replication stress, offering a new direction for treating various diseases, including cancer and age-related conditions.
A comprehensive study reveals that genetics and diet significantly influence insulin signaling in skeletal muscle. The research identified thousands of novel phosphosites associated with insulin regulation and provided a unique tool for assessing phosphorylation in insulin reactions.
Research identifies key molecular signatures and pathways contributing to skeletal muscle strength loss in females with estrogen deficiency. The study found parallel patterns of inhibition and activation across various signaling pathways, including AMPK and calcium signaling.
Researchers from Rice University and Princeton University have developed a new technology that allows for the live monitoring of signaling protein networks in living cells. The 'live reporter' system uses unobtrusive proteins to tag specific proteins, which can activate fluorescent markers when they become phosphorylated.
Scientists have used high-speed atomic force microscopy to observe the structural dynamics of CaMKII protein, shedding light on its role in modulating neural connections. The study reveals that the protein's structure changes in response to calcium and calmodulin binding, leading to a form of molecular memory.
Researchers have identified a gene network underlying rice grain size regulation, revealing a phosphorylation-driven auxin signaling pathway. The study found that OsTIR1–OsIAA10–OsARF4 plays a crucial role in controlling rice grain size and weight.
Researchers from Osaka University have identified a system known as the GET pathway as crucial for regulating the numbers of energy-producing mitochondria. The study found that disruption of the GET pathway leads to reduced mitophagy, a process responsible for removing defective or excess mitochondria.
Researchers discovered a point mutation in the fruit fly Drosophila melanogaster that leads to a temperature-dependent lengthening of circadian clock periods. The mutation affects the nuclear export signal of the PERIOD protein, resulting in its retention in the cell nucleus at higher temperatures.
Researchers found that CaMKII β promotes sleep onset and inhibits awakening, with its phosphorylation state controlling the transition from wakefulness to sleep. The study provides clues for ideal sleep control methods, aiming to maintain sleep duration.
Researchers at Tokyo Institute of Technology have developed a novel method for detecting protein phosphorylation using phosphate's electrical signature. The technique boasts 95% accuracy and 91% specificity, offering new avenues for clinical diagnosis and pharmaceutical applications.
A recent study published in Life Metabolism found that impaired phosphorylation of SERCA2a plays a bidirectional role in myocardial insulin resistance, dysregulation of calcium homeostasis, and the early stages of DCM. This mechanism involves the regulation of protein stability and insulin receptor maturation.
Researchers at Kyoto University have discovered a phosphorylation pathway that regulates meiotic double-strand break activity, ensuring genome stability. Enzymes ATR kinase and PP4 phosphatase work together to maintain a balance of DNA breaks, allowing for successful meiosis.
A novel inhibitor has been discovered that stalls a critical enzyme inside tumour cells, locking them in place and preventing invasion into healthy tissue. The findings hold promise for the development of metastasis-blocking agents.
Scientists have identified over 100 phosphorylation sites with regulatory potential on RNA-binding proteins, including RBM20, which plays a crucial role in titin synthesis and heart muscle diseases. These findings provide insight into the post-transcriptional regulation of gene expression.
The newly developed KANPHOS database provides comprehensive information on kinase-associated protein phosphorylation, facilitating research into neural signaling pathways. The database contains information on phosphoproteins, phosphorylation sites, and participant kinases, allowing for searches based on various parameters.
A new pathway has been discovered to explain how excessive alcohol consumption damages the liver, specifically through mitochondrial dysfunction. By targeting an enzyme called MATα1, researchers believe they can develop a new treatment for people suffering from alcohol-associated liver disease.
Researchers have discovered a new mechanism for regulating organelle contacts, essential for producing specific lipids in nerve cells. The study reveals that phosphorylation of a protein at the peroxisomes can block interaction with the endoplasmic reticulum.
Researchers discover that sudden cardiac episodes are caused by a combination of genetic mutations and chemical modifications in heart cells. The study uses new technology to manipulate the protein, demonstrating that phosphorylation can affect its function, particularly when paired with mutations.
A comprehensive molecular map of lung squamous cell carcinoma has identified potential new drug targets, including the gene NSD3, and highlighted immune regulation pathways that could help cancer evade immunotherapies. The study's findings have also revealed metabolic dysregulation and crosstalk between different cellular processes.
Researchers applied proteogenomics to identify precise diagnostics for known treatment targets, new tumor susceptibilities, and mechanisms involved in breast cancer treatment resistance. The study provides insights into the metabolic vulnerabilities of ER+ and ER- breast cancers and suggests potential targets for diagnosis and treatment.
Researchers at the University of South Carolina have identified a biological trigger that promotes quicker nerve regeneration. The discovery highlights the importance of protein phosphorylation and Casein kinase 2-alpha (CK2α) in breaking down stress granules, allowing nerves to regrow faster.
Researchers at KBRI found a new molecular mechanism that can inhibit neuronal degeneration by TDP-43, which is a major cause of dementia and Lou Gehrig's disease. The discovery reveals a potential therapeutic strategy to remove abnormal protein accumulation in neurons of patients with dementia.
A team led by Professor Claire Eyers has made a major breakthrough in cell signalling research, revealing a diverse and complex phenomenon of protein modification. The study found that approximately one-third of unique 'non-canonical' phosphorylation sites exist in addition to the well-studied serine, threonine and tyrosine residues.
Researchers at Waseda University have found that inhibiting the phosphorylation of CRMP2, a microtubule-binding protein, suppresses degeneration and promotes regeneration of nerve fibers in the optic nerve after injury. This breakthrough could lead to the development of novel treatments for patients with optic neuropathies such as glau...
Researchers identified associations between functional changes in certain brain cell types with Alzheimer's-related accumulation of phosphorylated tau protein. The study also showed that machine learning can be used to classify patients into different stages of disease pathogenesis based on gene expression patterns.
A Japanese team of researchers found that early changes to synapse gene regulation, including the phosphorylation of SRRM2 protein, can lead to Alzheimer's disease. This discovery offers new insights into the pathology of AD and may suggest possibilities for gene therapies using virus vectors.
Researchers at Japan's University of Tsukuba found that phosphoproteins accumulate when mice are awake and dissipate during sleep. The study identified 80 proteins, dubbed the Sleep-Need-Index-PhosphoProteins (SNIPPs), which change their phosphorylation state along with sleep need.
A research project that began with an interest in bipolar disorder drugs has led to a better understanding of leukemia. The study found that the protein GSK-3 affects RNA splicing, which is linked to acute myeloid leukemia. This discovery could also explain why lithium causes increased white blood cell count.
A new study on mice sheds light on the role of protein modification in heart failure, suggesting new strategies for personalizing treatment by examining phosphorylation. Researchers found that abnormal addition of phosphate to a specific heart muscle protein may damage the heart's pumping ability.
Researchers stopped FUS protein clumping using phosphorylation, a natural cellular process that increases protein charge and repels aggregation. The findings could have positive implications for treating ALS and dementia.
Researchers found that a small fraction of phosphosites remain conserved across species, while new sites are rapidly evolved. This suggests that changes in protein regulation can quickly generate diversity in response to environmental conditions.
A new University of Toronto study reveals widespread differences in protein biochemistry between healthy and diseased hearts, shedding light on the molecular causes behind dilated cardiomyopathy. The researchers mapped changes in protein signalling pathways, uncovering hundreds of signalling pathways that go off course in DCM hearts.
Scientists at Gladstone Institutes discovered that phosphorylation of the huntingtin protein prevents loss of critical brain cells and protected against behavioral symptoms in a mouse model of Huntington's disease. The study suggests a potential therapeutic target for treating the devastating neurodegenerative disorder.
Researchers used integrated 'omics' approaches to analyze changes in proteins across different organs in young and old rats. They found that aging affects organs in strikingly different ways, with specific protein patterns related to the organ's unique cellular properties or function. The study suggests that aging is an organ-specific ...
Researchers found that CpdR binds to the ClpXP protease, priming it for engagement with substrates, allowing for broad recognition of multiple pathways. This mechanism enables cells to control multiple pathways with a single regulator, facilitating rapid response to stress.
The study found that Fam20C phosphorylates more than 100 different secreted proteins, directing numerous cellular processes. This discovery has significant implications for understanding cancer cell metastasis and developing new therapeutic targets.
Researchers at Dartmouth's Geisel School of Medicine have identified a determinant of the circadian clock's period, suggesting that protein structure plays a crucial role in determining clock speed. This finding may lead to new treatments for sleep disorders and other health problems tied to circadian rhythms.
Researchers find that protein phosphorylation slows down Parkinson's disease, contradicting the assumption that it triggers toxic aggregates. The study suggests a new approach for therapeutic development.
Australian scientists mapped insulin action in cells with precise detail, providing a comprehensive blueprint for understanding diabetes. The breakthrough study catalogued 37,248 phosphorylation sites on 5,705 proteins, revealing 15% that changed in response to insulin.
A new protein called Lem4 has been discovered to direct a crucial step in cell division by preventing the addition of phosphate tags to BAF while promoting their removal. This process is essential for cellular growth and division, and its regulation may be key to understanding various cellular processes.
Scientists have assembled a massive catalogue of protein data using a new method, providing unprecedented insight into protein phosphorylation. This understanding brings researchers closer to unraveling the mechanisms of disease.
Scientists develop technique to monitor protein phosphorylation in single living cells, revealing chemical changes over time. The method uses Fourier-transform infrared spectromicroscopy to analyze infrared radiation from a synchrotron light source without damaging cells.
Scientists at EMBL discovered that bacteria like Mycoplasma pneumoniae tune proteins to perform multiple tasks, leveraging post-translational modifications. This strategy may be an ancient evolutionary tactic shared with complex cells.
Scientists have elevated little-studied cellular mechanism sulfenylation to potential drug target by showing its importance in cell signaling and cancer. A new chemical probe allowed detection of minute differences in sulfenylation rates, revealing a key role for hydrogen peroxide in activating epidermal growth factor receptor.
Researchers at RIKEN Brain Science Institute discovered a key mechanism for degrading ubiquitinated protein aggregates in brain cells. This process is mediated by the phosphorylation of p62, which triggers selective autophagy and degradation of protein aggregates.
Researchers developed a technique to isolate specific cancer proteins using a synthetic nanopolymer. The polymer-based metal-ion affinity capture (PolyMAC) method isolated phosphorylated proteins, which are highly associated with cancer, from a sea of other proteins. This breakthrough may aid in the development of new cancer drugs.
Researchers at Brown University have identified how protein phosphatase 1 (PP1) regulates substrate proteins by binding to specific sites, increasing specificity and reducing errors. This discovery sheds light on the enzyme's critical role in various diseases, including cancer and Parkinson's disease.
Researchers have made new inroads into understanding the regulatory circuitry of the biological clock that synchronizes daily activities. Two studies published in Cell and Molecular Cell provide a complete view of the regulation of circadian clocks across a day, revealing the role of phosphorylation and temperature compensation.
Scientists have developed a new approach to survey phosphorylation in cells, revealing a previously uncharacterized protein that plays a crucial role in cancer cell invasion. The study identified ninety phosphorylation events regulated by oncogenic B-Raf and found that one target, MINERVA/FAM129B, is involved in melanoma progression.