GAPDH Protein, Mouse (His)

GAPDH protein showcases a dual functionality with both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, playing integral roles in glycolysis and nuclear functions, respectively. In glycolysis, it serves as a key enzyme catalyzing the initial step by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Beyond its metabolic role, GAPDH modulates the organization and assembly of the cytoskeleton and facilitates CHP1-dependent microtubule and membrane associations by stimulating the binding of CHP1 to microtubules (By similarity). It is also a component of the GAIT complex, which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. In innate immunity, GAPDH contributes to TNF-induced NF-kappa-B activation and type I interferon production by interacting with TRAF2 and TRAF3, respectively (By similarity). Furthermore, its involvement in nuclear events, including transcription, RNA transport, DNA replication, and apoptosis, is likely mediated by its nitrosylase activity, leading to cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2, and PRKDC (By similarity). The multifaceted functions of GAPDH underscore its versatile and critical roles in cellular processes.