Dario Alessi FRSE FRS (born in France, 1967) is a biochemist, Director of the Medical Research Council Protein Phosphorylation and Ubiquitylation Unit (MRC PPU) and Professor of Signal Transduction, at University of Dundee.
Phosphorylation is a key reversible modification that regulates protein function, subcellular localization, complex formation, degradation of proteins and therefore cell signalling networks.
Recently, EThcD has been developed combining electron-transfer and higher-energy collision dissociation.
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Compared to the usual fragmentation methods, EThcD scheme provides more informative MS/MS spectra for unambiguous phosphosite localization.
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Phosphorylation of the cytosolic components of NADPH oxidase, a large membrane-bound, multi-protein enzyme present in phagocytic cells, plays an important role in the regulation of protein-protein interactions in the enzyme.
Deletion of the C-terminus of CNP or phosphorylation abolish the catalytic activity of microtubule formation.
These two succinylpurines are the dephosphorylated derivatives of SAICA ribotide (SAICAR) and adenylosuccinate (S-AMP), the two substrates of adenylosuccinate lyase (ASL), which catalyzes an important reaction in the de novo pathway of purine biosynthesis.
Upon phosphorylation, formation of an R-SMAD complex in conjunction with common-partner Smad (co-Smad) occurs where it migrates to the nucleus.
E-cadherin binding to p120ctn may activate SRC leading to activation of Rac1 which results in phosphorylation of LIMK1 and LIMK2 to deactivate cofilin causing G-actin polymerization.
After translocation, CagA localises to the inner surface of the cell membrane and undergoes tyrosine phosphorylation by Src family kinases (e.g. Fyn and Lyn).
CST maintains a curated, web-based bioinformatics resource known as PhosphoSitePlus, which details protein phosphorylation in human, mouse and rat.
Phosphorylation is a key regulatory role in centrosome maturation and it is thought that Polo-like kinases (Plks) and Aurora kinases are responsible for this phosphorylation.
This activity facilitates phosphorylation of important downstream kinetochore targets (such as tension-sensing 3F3/2 phospho-epitope) of Plk1, which is important for recruitment of spindle assembly checkpoint proteins such as Mad1 and proper kinetochore-microtubule attachment.
Glucokinase, an enzyme that facilitates the phosphorylation of glucose into glucose 6-phosphate.
Dissipation of the proton gradient is coupled to the phosphorylation of ADP through membrane-bound ATPases.
Tau-phosphorylation is decreased and cholinergic function enhanced.
This phosphorylation results in higher ATPase activity and the assembly of myosin II filaments.
Once they are phosphorylated, they work as antimetabolites by being similar enough to nucleotides to be incorporated into growing DNA strands; but they act as chain terminators and stop viral DNA Polymerase.
Upon ligand binding the Tyk2 protein associated with IFNAR1 is phosphorylated which in turn phosphorylates Jak1 associated with IFNAR2.
Phosphorylation of serine and threonine residues is conserved during MHC class I and MHC class II antigen processing.
Protein phosphatase-1 (PP1) participates in the regulation of a wide variety of cellular functions by reversible protein phosphorylation.
Activation of PARs also led to an increase in tyrosine phosphorylation of ZAP-70 and SLP-76, two key proteins in T cell receptor (TCR) signalling.
Kinases are turned on or off by phosphorylation (sometimes by the kinase itself - cis-phosphorylation/autophosphorylation), by binding of activator proteins or inhibitor proteins, or small molecules, or by controlling their location in the cell relative to their substrates.
Increased β-adrenergic stimulation reduces the association between SERCA and PLB by the phosphorylation of PLB by PKA.
After the RNase cleavage of the last six nucleotides, the next step is phosphorylation of the 5'-end via Kinase.
The university’s College of Life Sciences located on Hawkhill incorporates the Wellcome Trust Biocentre, Sir James W. Black Centre, MRC Protein Phosphorylation Unit and Cancer Research UK Centre laboratories.