DKK3 (dickkopf related protein 3) is a member of the dickkopf-related family consisting of DKK1 , DKK2 , DKK3 and DKK4. It is a secreted protein , and also known as REIC (Reduced Expansion in Immortalized Cells). The DKK3 protein is proposed to function as a secreted tumor suppressor since it is downregulated in a number of cancer cells and prostate cancer tissue and may be a promising candidate molecule for therapeutic interference. DKK3 protein is also a negative regulator of beta-catenin and its downregulation contribute to an activation of the beta-catenin signaling pathway.
Dickkopf-related protein 3 (DKK3) belongs to the DKK protein family including Dkk-1, 2, 3 and -4. DKK3 is a 350 amino acid secreted glycoprotein which is comprised of an N-terminal signal peptide and 2 conserved cysteine-rich domains that are separated by a 12 amino acid linker region. Dkk-3 also have one prokineticin domain. DKK3 is involved in embryonic development through its inhibition of the WNT signaling pathway. The Dkk family also includes Soggy, which is homologous to Dkk-3 but not to the other family members. Soggy has not been shown to inhibit Wnt signaling, and its role in the pathway is unclear.
This gene encodes a protein that is a member of the dickkopf family. The secreted protein contains two cysteine rich regions and is involved in embryonic development through its interactions with the Wnt signaling pathway. Activity of this protein is modulated by binding to the Wnt co-receptor and the co-factor kremen 2.
Disks large homolog 4(DLG4) is a cell membrane protein and it is a member of the membrane-associated guanylate kinase (MAGUK) family. The protein contains 1 guanylate kinase-like domain,3 PDZ (DHR) domains and 1 SH3 domain. With PSD-93 it is recruited into the same NMDA receptor and potassium channel clusters. These two MAGUK proteins may interact at postsynaptic sites to form a multimeric scaffold for the clustering of receptors, ion channels, and associated signaling proteins. DLG4 is the best studied member of the MAGUK-family of PDZ domain-containing proteins. Like all MAGUK-family proteins, its basic structure includes three PDZ domains, an SH3 domain, and a guanylate kinase-like domain (GK) connected by disordered linker regions. It is almost exclusively located in the post synaptic density of neurons, and is involved in anchoring synaptic proteins. Its direct and indirect binding partners include neuroligin, NMDA receptors, AMPA receptors, and potassium channels.
Delta-like protein 1 (DLL1) is a type I transmembrane protein that belongs to the Delta/Serrate/Lag2 (DSL) family of Notch ligands. Mature human DLL1 consists of a 528 amino acid (aa) extracellular domain (ECD) with one DSL domain and eight EGF-like repeats, a 23 aa transmembrane segment, and a 155 aa cytoplasmic domain. Within the ECD, human DLL1 shares 91% aa sequence identity with mouse and rat DLL1. The residual membranebound portion of DLL1 can be cleave by presenilin-dependent γ-secretase, enabling the cytoplasmic domain to migrate to the nucleus. DLL1 localizes to adherens junctions on neuronal processes through its association with the scaffolding protein MAGI1. DLL1 is widely expressed, and it plays an important role in embryonic somite formation, cochlear hair cell differentiation, plus B and T lymphocyte differentiation. The upregulation of DLL1 in arterial endothelial cells following injury or angiogenic stimulation is central to postnatal arteriogenesis. DLL1 is also overexpressed in cervical carcinoma and glioma and contributes to tumor progression.
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