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Pyruvate dehydrogenase (PDH) is a mitochondrial multienzyme complex that catalyzes the oxidative decarboxylation of pyruvate and is one of the major enzymes responsible for the regulation of homeostasis of carbohydrate fuels in mammals. The enzymatic activity is regulated by a phosphorylation/dephosphorylation cycle. Phosphorylation of PDH by a specific pyruvate dehydrogenase kinase (PDK) results in inactivation. Multiple alternatively spliced transcript variants have been found for this gene.

The protein encoded by this gene is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation, and development. MAPK11 is most closely related to p38 MAP kinase, both of which can be activated by proinflammatory cytokines and environmental stress. This kinase is activated through its phosphorylation by MAP kinase kinases

This gene product belongs to the histone deacetylase family. Histone deacetylases act via the formation of large multiprotein complexes, and are responsible for the deacetylation of lysine residues at the N-terminal regions of core histones (H2A, H2B, H3 and H4). This protein forms transcriptional repressor complexes by associating with many different proteins, including YY1, a mammalian zinc-finger transcription factor. Thus, it plays an important role in transcriptional regulation, cell cyc

Vascular endothelial growth factors (VEGFs) are a family of closely related growth factors having a conserved pattern of eight cysteine esidues and sharing common VEGF receptors. VEGFs stimulate the proliferation of endothelial cells, induce angiogenesis, and increase vascular permeability in both large and small vessels. The mitogenic activity of VEGFs appears to be mediated by specific VEGF receptors. VEGF Receptor 3 is one of the five receptor tyrosine kinases (RTKs) (VEGF Receptor 1/Flt1

The serine/threonine kinase PRAK is activated in response to cellular stress and proinflammatory cytokines, through its phosphorylation by MAP kinases including MAPK1/ERK, MAPK14/p38 alpha, and MAPK11/p38 beta. PRAK has been reported to have a putative tumor suppressor function by mediating senescence upon activation by p38 in response to oncogenic ras. It is thought that phosphorylation of p53 by PRAK following activation of p38 MAPK by ras plays an important role in ras induced senescence ａ

The serine/threonine kinase PRAK is activated in response to cellular stress and proinflammatory cytokines, through its phosphorylation by MAP kinases including MAPK1/ERK, MAPK14/p38 alpha, and MAPK11/p38 beta. PRAK has been reported to have a putative tumor suppressor function by mediating senescence upon activation by p38 in response to oncogenic ras. It is thought that phosphorylation of p53 by PRAK following activation of p38 MAPK by ras plays an important role in ras induced senescence ａ