Nonessential Sites Improve Phosphorylation Switch
نویسندگان
چکیده
منابع مشابه
Nonessential sites improve phosphorylation switch.
Multisite phosphorylation is a common form of posttranslational protein regulation which has been used to increase the switchlike behavior of the protein response to increasing kinase concentrations. In this letter, we show that the switchlike response of multisite phosphoproteins is strongly enhanced by nonessential phosphorylation sites, a mechanism that is robust to parameter changes and eas...
متن کاملEvolution of Human Phosphorylation Sites
Phosphorylation of proteins plays key roles in many intracellular signal pathways [3]. Gain or loss of phosphorylation sites of proteins during evolution may result in changes in signal transduction pathways. For example, FOXP2, a gene involved in speech and language, was reported to gain a potential target site for phosphorylation in humans after the human-chimpanzee divergence [2]. Here, we r...
متن کاملTyrosine Phosphorylation as a Conformational Switch
Lalit Deshmukh, Nahum Meller, Nathan Alder , Tatiana Byzova, and Olga Vinogradova From the Departments of Pharmaceutical Sciences, School of Pharmacy and Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut 06269, the Department of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195, and the Laboratory of Chemical Physics, NI...
متن کاملA phosphorylation-acetylation switch regulates STAT1 signaling.
Cytokines such as interferons (IFNs) activate signal transducers and activators of transcription (STATs) via phosphorylation. Histone deacetylases (HDACs) and the histone acetyltransferase (HAT) CBP dynamically regulate STAT1 acetylation. Here we show that acetylation of STAT1 counteracts IFN-induced STAT1 phosphorylation, nuclear translocation, DNA binding, and target gene expression. Biochemi...
متن کاملPhosphorylation: a molecular switch in opioid tolerance.
Protein phosphorylation is a key posttranslational modification mechanism controlling the conformation and activity of many proteins. Increasing evidence has implicated an essential role of phosphorylation by several major protein kinases in promoting and maintaining opioid tolerance. We review some of the most recent studies on protein kinase C (PKC), cyclic AMP dependent protein kinase A (PKA...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2010
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2010.07.030