Current Signal Transduction Therapy - Volume 5, Issue 1, 2010

The journal Current Signal Transduction Therapy will start its 5th year in 2010 and in the past four years it has covered a very broad spectrum of the signaling- related molecular pathomechanisms and the existing and potential therapeutic possibilities. The journal has been very well received by the scientific community as it has generated an impact in three years and it is acknowledged and cited in many scientific publications Read More

It appears to be now fairly well accepted in the field of signal transduction that the monosaccharide N-acetylglucosamine (O-GlcNAc) added posttranslationally through a β-O-glycosidic linkage to serine and threonine residues in cytosolic and nuclear proteins has important regulatory roles. Since its first description in 1984 until today this highly dynamic sugar has been shown to be attached to about thousand proteins. Read More

Modification of cytosolic, nuclear, and mitochondrial proteins on serine and threonine residues by Nacetylglucosamine (O-GlcNAc) provides a mechanism by which glucose flux rates in the cell can feed back to regulate the function and synthesis of proteins involved in metabolism and growth. The hexosamine biosynthesis pathway (HBP) provides the substrate for this modification, UDP-GlcNAc. Production of UDP-GlcNA Read More

O-linked a-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation. Cells have developed complex regulatory systems in order to regulate gene expression appropriately in response to environmental and intracellular cues. Control of eukaryotic ge Read More

GlcNAcylation is a dynamic cytoplasmic and nuclear post-translational sugar modification of serine/threonine residues. The addition and removal of O-GlcNAc are regulated by O-GlcNAc Transferase and O-GlcNAcase, respectively. Over ∼1000 proteins have been identified to be GlcNAcylated with over 240 mapped sites. O-GlcNAc is involved in critical cellular functions, such as cell-cycle regulation, apoptosis, stress responses, Read More

The posttranslational modification of proteins by a single O-linked N-acetylglucosamine (O-GlcNAc) is an intracellular biochemical reaction which is ubiquitous in eukaryotic cells. Two enzymes regulate the process: O-linked Nacetylglucosaminyltransferase (OGT), which attaches O-GlcNAc to serine/threonine residues of proteins, and a a-Nacetylglucosaminidase (O-GlcNAcase), that removes the O-GlcNAc group. The serine or Read More

The post-translational modification of serine and threonine residues of nuclear and cytoplasmic proteins by the O-linked attachment of the monosaccharide ß-N-acetyl-glucosamine (O-GlcNAc) is a highly dynamic and ubiquitous protein modification that plays a critical role in regulating numerous biological processes. Much of our understanding of the mechanisms underlying the role of O-GlcNAc on cellular function has Read More

Caenorhabditis elegans is perhaps the best-understood metazoan in terms of cell fate, neural connectivity, nutrient sensing, and longevity. The study of this genetically amenable model has greatly accelerated progress in understanding human aging-associated diseases, such as diabetes and neurodegeneration. The nutrient-responsive cycling of OGlcNAc on key intracellular targets may play a key, yet unappreciated, role Read More

The post-translational modification of nucleocytoplasmic proteins with O-linked 2-acetamido-2-deoxy-Dglucopyranose (O-GlcNAc) is a topic of considerable interest and attracts a great deal of research effort. O-GlcNAcylation is a dynamic process which can occur multiple times over the lifetime of a protein, sometimes in a reciprocal relationship with phosphorylation. Several hundred proteins, which are involved in a dive Read More