GNE
GNE is a bifunctional cytosolic enzyme that combines UDP-N-acetylglucosamine 2-epimerase and N-acetylmannosamine kinase activities and initiates the biosynthesis of N-acetylneuraminic acid, a precursor of sialic acids. It is also known as Uae1 and IBM2. Browse Assay Genie's current range of GNE research reagents below, or read on for the biology behind the target.
GNE (glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase) is a bifunctional enzyme with both UDP-N-acetylglucosamine 2-epimerase and N-acetylmannosamine kinase activities. It serves as the initiator of the biosynthetic pathway leading to N-acetylneuraminic acid (NeuAc), a critical precursor in the synthesis of sialic acids. By catalysing this pivotal, rate-limiting step, GNE plays a central role in governing the regulation of cell surface sialylation, and UniProt also annotates a role in embryonic angiogenesis.
Sialic acids are negatively charged sugars found on the cell surface as terminal components of glycoconjugates. They mediate important functions in cell adhesion, signal transduction and cellular recognition. Differential sialylation of cell surface molecules has also been implicated in the tumorigenicity and metastatic behaviour of malignant cells, which makes the control of this pathway relevant to cancer biology. The GNE protein is found in the cytosol, and the C-terminal section belongs to the ROK (NagC/XylR) family. The GNE gene belongs to the HGNC group of carbohydrate kinases, and orthologues are recorded in mouse and rat as Gne.
Mutations in the GNE gene are associated with sialuria, autosomal recessive inclusion body myopathy and Nonaka myopathy. Alternative splicing produces transcript variants that encode different isoforms. Previous names include UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase, and the symbols Uae1 and IBM2 appear in older literature.
GNE catalyses the rate-limiting step in the pathway producing N-acetylneuraminic acid, making it a key point for studying how sialic acid supply is controlled.
As a regulator of cell surface sialylation, GNE is relevant to work on adhesion, signal transduction and cellular recognition mediated by sialylated glycoconjugates.
Mutations in GNE are associated with autosomal recessive inclusion body myopathy and Nonaka myopathy, so the protein is studied in myopathy models.
Differential sialylation of cell surface molecules is implicated in tumorigenicity and metastatic behaviour, linking GNE-dependent pathways to malignant cell biology.
GNE is a bifunctional enzyme with UDP-N-acetylglucosamine 2-epimerase and N-acetylmannosamine kinase activities. It initiates the pathway leading to N-acetylneuraminic acid, a sialic acid precursor, and through this rate-limiting step regulates cell surface sialylation. Sialic acids contribute to cell adhesion, signal transduction and cellular recognition.
The HGNC full name is glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase. Aliases and previous symbols include Uae1 and IBM2, and an earlier name was UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase. Alternative splicing of the gene gives transcript variants encoding different isoforms.
Mutations in the GNE gene are associated with sialuria, autosomal recessive inclusion body myopathy and Nonaka myopathy. Orthologues exist in mouse and rat, both named Gne. Check the datasheet of any product for its validated reactivity.
Other sialic acid pathway enzymes, sialyltransferases and carbohydrate kinases with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9Y223; product specifications from Assay Genie datasheets.