The protein encoded by this gene is a critical subunit of N-methyl-D-aspartate receptors, members of the glutamate receptor channel superfamily which are heteromeric protein complexes with multiple subunits arranged to form a ligand-gated ion channel. These subunits play a key role in the plasticity of synapses, which is believed to underlie memory and learning. Cell-specific factors are thought to control expression of different isoforms, possibly contributing to the functional diversity of the subunits. Alternatively spliced transcript variants have been described.
This gene (NME1) was identified because of its reduced mRNA transcript levels in highly metastatic cells. Nucleoside diphosphate kinase (NDK) exists as a hexamer composed of 'A' (encoded by this gene) and 'B' (encoded by NME2) isoforms. Mutations in this gene have been identified in aggressive neuroblastomas. Two transcript variants encoding different isoforms have been found for this gene. Co-transcription of this gene and the neighboring downstream gene (NME2) generates naturally-occurring transcripts (NME1-NME1), which encodes a fusion protein comprised of sequence sharing identity with each individual gene product.
Members of the Myc/Max/Mad network function as transcriptional regulators with roles in various aspects of cell behavior, including proliferation, differentiation, and apoptosis. These proteins share a common basic-helix-loop-helix leucine zipper (bHLH-ZIP) motif required for dimerization and DNA-binding. Max was originally discovered based on its ability to associate with c-Myc and found to be required for the ability of Myc to bind DNA and activate transcription. Subsequently, Max has been viewed as a central component of the transcriptional network, forming homodimers as well as heterodimers with other members of the Myc and Mad families. The association between Max and either Myc or Mad can have opposing effects on transcriptional regulation and cell behavior. The Mad family consists of four related proteins; Mad1, Mad2 (Mxi1), Mad3, and Mad4, and the more distantly related members of the bHLH-ZIP family, Mnt and Mga. Like Myc, the Mad proteins are tightly regulated with short half-lives. In general, Mad family members interfere with Myc-mediated processes, such as proliferation, transformation, and prevention of apoptosis by inhibiting transcription.In humans the Myc family consists of 5 genes: c-Myc, N Myc, L-Myc, R-Myc, and B-Myc. While c-Myc is expressed in many proliferating cells, N-Myc expression is very restricted, with highest levels in during embryonic development and then in the adult during B-cell development. These expression patterns and results from targeted deletion of N-Myc suggest that N-Myc plays an important role in tissue development and differentiation. In addition, amplification or overexpression of N-Myc has been found in human neuroblastomas and is associated with rapid progression and poor prognosis.
This gene encodes a type I single transmembrane domain receptor, which is a subunit of cis-prenyltransferase, and serves as a specific receptor for the neural and cardiovascular regulator Nogo-B. The encoded protein is essential for dolichol synthesis and protein glycosylation. This gene is highly expressed in non-small cell lung carcinomas as well as estrogen receptor-alpha positive breast cancer cells where it promotes epithelial mesenchymal transition. This gene is associated with the poor prognosis of human hepatocellular carcinoma patients. Naturally occurring mutations in this gene cause a congenital disorder of glycosylation and are associated with epilepsy. A knockout of the orthologous gene in mice causes embryonic lethality before day 6.5. Pseudogenes of this gene have been defined on chromosomes 13 and X.
Non-muscle myosin is an actin-based motor protein essential to cell motility, cell division, migration, adhesion, and polarity. The holoenzyme consists of two identical heavy chains and two sets of light chains. The light chains (MLCs) regulate myosin II activity and stability. The heavy chains (NMHCs) are encoded by three genes, MYH9, MYH10, and MYH14, which generate three different non-muscle myosin II isoforms, IIa, IIb, and IIc, respectively.
β-catenin is a key downstream effector in the Wnt signaling pathway. It is implicated in two major biological processes in vertebrates: early embryonic development and tumorigenesis. CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β. GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41. Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines.Non-phospho (Active) β-Catenin (Ser33/37/Thr41) Rabbit mAb specifically recognizes β-catenin that is non-phosphorylated at Ser33, Ser33 or Thr41. Non-phospho β-Catenin (Ser33, Ser33 or Thr41) protein is useful as a readout of stabilized β-catenin protein, and therefore functionally active in cell-cell adhesion and mediating transcriptional activity via the canonical Wnt signaling pathway.
Inserisci la tua e-mail e seleziona le aree di interesse per ricevere le ultime novità, approfondimenti e promozioni.
Seleziona uno o più ambiti di interesse per ricevere comunicazioni più utili e mirate.
2025 TEMA Ricerca - All Rights Reserved.
