Cytoplasmic Protein NCK1 (NCK1) is a cytoplasmic protein that contains one SH2 domain and three SH3 domains. NCK1 is a member of the adapter family, which associates with tyrosine-phosphorylated growth factor receptors, such as KDR and PDGFRB, or their cellular substrates. NCK1 maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. NCK1 plays a role in the DNA damage response, but not in the detection of the damage by ATM/ATR. It is also involved in transducing signals from receptor tyrosine kinases to downstream signal recipients, such as ELK1-dependent transcriptional activation in response to activated Ras signaling.
NCKIPSD is localized exclusively in the cell nucleus. It plays a role in signal transduction, and may function in the maintenance of sarcomeres and in the assembly of myofibrils into sarcomeres. NCKIPSD also plays an important role in stress fiber formation. NCKIPSD gene is involved in therapy-related leukemia by a chromosomal translocation t(3;11)(p21;q23) that involves this gene and the myeloid/lymphoid leukemia gene. Alternative splicing occurs in this locus and two transcript variants encoding distinct isoforms have been identified. NCKIPSD is a SH3 domain protein. Fas ligand is a cytotoxic effector molecule of T and NK cells which is characterized by an intracellular N-terminal polyproline region that serves as a docking site for SH3 and WW domain proteins. Several previously described Fas ligand-interacting SH3 domain proteins turned out to be crucial for the regulation of storage, expression and function of the death factor. Recent observations, however, indicate that Fas ligand is also subject to posttranslational modifications including shedding and intramembrane proteolysis.
Natural cytotoxicity triggering receptor 1(NCR1) is a single-pass type I membrane protein .It contains 2 Ig-like (immunoglobulin-like) domains and belongs to the natural cytotoxicity receptor (NCR) family. The protein is a natural killer (NK) lymphocyte-activating receptor. It is involved in major aspects of NK immune function and shows a high degree of lineage specificity in blood and bone marrow.
Natural cytotoxicity triggering receptor 2 (NCR2), also known as Natural killer cell p44-related protein (NKp44), or CD336, is a member of the natural cytotoxicity receptor (NCR) family, which composed of one Ig-like extracellular domain, a transmembrane segment, and a cytoplasmic domain. It is a novel transmembrane glycoprotein belonging to the Immunoglobulin superfamily characterized by a single extracellular V-type domain. The cytoplasmic domain of NKp44 also contains a sequence that matches the immunoreceptor tyrosine-based inhibitory motif (ITIM) consensus. This Cytotoxicity-activating receptor that may contribute to the increased efficiency of activated natural killer (NK) cells to mediate tumor cell lysis. NKp44 is selectively expressed by IL-2-activated NK cells and may contribute to the increased efficiency of activated NK cells to mediate tumor cell lysis. Tumor cell recognition of the mutated NKp44 proteins was significantly reduced and correlated with their lower recognition of heparin.
Natural Cytotoxicity Triggering Receptor 3 (NCR3) along with NKp44 and NKp46 constitute a group of receptors termed “Natural Cytotoxicity Receptors”. They play a major role in triggering NK-mediated killing of most tumor cells lines. NKp30 is a type I transmembrane protein having a single extracellular V-like immunoglobulin domain. NKp30 is selectively expressed both in resting and activated human NK cells. In addition; NKp30 is also involved in NK-mediated induction of dendritic cell (DC) maturation. It has been demonstrated that NK cell activation signaling specifically induces lytic activity against several tumor cell types and synthesis of new NF-κB dependent proteins during the initiation of cytotoxicity.
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