
Health Dictionary
Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.
KLRC4
Introduction
NKG2-F type II integral membrane protein is a protein that in humans is encoded by the KLRC4 gene.[1][2]
Natural killer (NK) cells are lymphocytes that can mediate lysis of certain tumor cells and virus-infected cells without previous activation. They can also regulate specific humoral and cell-mediated immunity. NK cells preferentially express several calcium-dependent (C-type) lectins, which have been implicated in the regulation of NK cell function. KLRC4 is a member of the NKG2 group which are expressed primarily in natural killer (NK) cells and encodes a family of transmembrane proteins characterized by a type II membrane orientation (extracellular C terminus) and the presence of a C-type lectin domain. The NKG2 gene family is located within the NK complex, a region that contains several C-type lectin genes preferentially expressed on NK cells. The 3′ end of the KLRC4 transcript includes the first non-coding exon found at the 5′ end of the adjacent D12S2489E gene transcript.[2]
References
References
- ↑ Plougastel B, Trowsdale J (Aug 1998). “Sequence analysis of a 62-kb region overlapping the human KLRC cluster of genes”. Genomics. 49 (2): 193–9. doi:10.1006/geno.1997.5197. PMID 9598306.
- ↑ 2.0 2.1 “Entrez Gene: KLRC4 killer cell lectin-like receptor subfamily C, member 4”.
Further reading
Further reading
- Vivier E, Tomasello E, Paul P (2002). “Lymphocyte activation via NKG2D: towards a new paradigm in immune recognition?”. Curr. Opin. Immunol. 14 (3): 306–11. doi:10.1016/S0952-7915(02)00337-0. PMID 11973127.
- Houchins JP, Yabe T, McSherry C, Bach FH (1991). “DNA sequence analysis of NKG2, a family of related cDNA clones encoding type II integral membrane proteins on human natural killer cells”. J. Exp. Med. 173 (4): 1017–20. doi:10.1084/jem.173.4.1017. PMC 2190798. PMID 2007850.
- Yabe T, McSherry C, Bach FH, et al. (1993). “A multigene family on human chromosome 12 encodes natural killer-cell lectins”. Immunogenetics. 37 (6): 455–60. doi:10.1007/BF00222470. PMID 8436421.
- Plougastel B, Trowsdale J (1998). “Cloning of NKG2-F, a new member of the NKG2 family of human natural killer cell receptor genes”. Eur. J. Immunol. 27 (11): 2835–9. doi:10.1002/eji.1830271114. PMID 9394807.
- Glienke J, Sobanov Y, Brostjan C, et al. (1998). “The genomic organization of NKG2C, E, F, and D receptor genes in the human natural killer gene complex”. Immunogenetics. 48 (3): 163–73. doi:10.1007/s002510050420. PMID 9683661.
- Bauer S, Groh V, Wu J, et al. (1999). “Activation of NK cells and T cells by NKG2D, a receptor for stress-inducible MICA”. Science. 285 (5428): 727–9. doi:10.1126/science.285.5428.727. PMID 10426993.
- Wu J, Song Y, Bakker AB, et al. (1999). “An activating immunoreceptor complex formed by NKG2D and DAP10”. Science. 285 (5428): 730–2. doi:10.1126/science.285.5428.730. PMID 10426994.
- Li P, Morris DL, Willcox BE, et al. (2001). “Complex structure of the activating immunoreceptor NKG2D and its MHC class I-like ligand MICA”. Nat. Immunol. 2 (5): 443–51. doi:10.1038/87757. PMID 11323699.
- O’Callaghan CA, Cerwenka A, Willcox BE, et al. (2001). “Molecular competition for NKG2D: H60 and RAE1 compete unequally for NKG2D with dominance of H60”. Immunity. 15 (2): 201–11. doi:10.1016/S1074-7613(01)00187-X. PMID 11520456.
- Girardi M, Oppenheim DE, Steele CR, et al. (2001). “Regulation of cutaneous malignancy by gammadelta T cells”. Science. 294 (5542): 605–9. doi:10.1126/science.1063916. PMID 11567106.
- Shum BP, Flodin LR, Muir DG, et al. (2002). “Conservation and variation in human and common chimpanzee CD94 and NKG2 genes”. J. Immunol. 168 (1): 240–52. doi:10.4049/jimmunol.168.1.240. PMID 11751968.
- Radaev S, Rostro B, Brooks AG, et al. (2002). “Conformational plasticity revealed by the cocrystal structure of NKG2D and its class I MHC-like ligand ULBP3”. Immunity. 15 (6): 1039–49. doi:10.1016/S1074-7613(01)00241-2. PMID 11754823.
- Sutherland CL, Chalupny NJ, Schooley K, et al. (2002). “UL16-binding proteins, novel MHC class I-related proteins, bind to NKG2D and activate multiple signaling pathways in primary NK cells”. J. Immunol. 168 (2): 671–9. doi:10.4049/jimmunol.168.2.671. PMID 11777960.
- Holmes MA, Li P, Petersdorf EW, Strong RK (2002). “Structural studies of allelic diversity of the MHC class I homolog MIC-B, a stress-inducible ligand for the activating immunoreceptor NKG2D”. J. Immunol. 169 (3): 1395–400. doi:10.4049/jimmunol.169.3.1395. PMID 12133964.
- Gilfillan S, Ho EL, Cella M, et al. (2002). “NKG2D recruits two distinct adapters to trigger NK cell activation and costimulation”. Nat. Immunol. 3 (12): 1150–5. doi:10.1038/ni857. PMID 12426564.
- Diefenbach A, Tomasello E, Lucas M, et al. (2002). “Selective associations with signaling proteins determine stimulatory versus costimulatory activity of NKG2D”. Nat. Immunol. 3 (12): 1142–9. doi:10.1038/ni858. PMID 12426565.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- McFarland BJ, Kortemme T, Yu SF, et al. (2004). “Symmetry recognizing asymmetry: analysis of the interactions between the C-type lectin-like immunoreceptor NKG2D and MHC class I-like ligands”. Structure. 11 (4): 411–22. doi:10.1016/S0969-2126(03)00047-9. PMID 12679019.
