ULBP1: Difference between revisions
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{{ | '''UL16 binding protein 1''' ('''ULBP1''') is a cell surface [[glycoprotein]] encoded by ''ULBP1'' gene located on the chromosome 6.<ref name="pmid11239445">{{cite journal | vauthors = Cosman D, Müllberg J, Sutherland CL, Chin W, Armitage R, Fanslow W, Kubin M, Chalupny NJ | title = ULBPs, novel MHC class I-related molecules, bind to CMV glycoprotein UL16 and stimulate NK cytotoxicity through the NKG2D receptor | journal = Immunity | volume = 14 | issue = 2 | pages = 123–33 | date = Feb 2001 | pmid = 11239445 | pmc = | doi = 10.1016/S1074-7613(01)00095-4 }}</ref><ref name="pmid11827464">{{cite journal | vauthors = Radosavljevic M, Cuillerier B, Wilson MJ, Clément O, Wicker S, Gilfillan S, Beck S, Trowsdale J, Bahram S | title = A cluster of ten novel MHC class I related genes on human chromosome 6q24.2-q25.3 | journal = Genomics | volume = 79 | issue = 1 | pages = 114–23 | date = Jan 2002 | pmid = 11827464 | pmc = | doi = 10.1006/geno.2001.6673 }}</ref> ULBP1 is related to [[MHC class I]] molecules, but its gene maps outside the MHC locus.<ref name="pmid11239445" /><ref name="pmid11827464" /> The domain structure of ULBP1 differs significantly from those of conventional [[MHC class I]] molecules. It does not contain the α3 domain and the transmembrane segment. ULBP1 is thus composed of only the α1α2 domain which is linked to the cell membrane by the [[Glycophosphatidylinositol|GPI anchor]].<ref name="pmid11239445" /><ref name="pmid11827464" /> It functions as a [[Induced-self antigen|stress-induced]] ligand for [[NKG2D]] receptor.<ref name="pmid11239445" /> ULBP1 is, for example, upregulated during [[Human cytomegalovirus|HCMV]] infection.<ref name=":0">{{cite journal | vauthors = Rölle A, Mousavi-Jazi M, Eriksson M, Odeberg J, Söderberg-Nauclér C, Cosman D, Kärre K, Cerboni C | title = Effects of human cytomegalovirus infection on ligands for the activating NKG2D receptor of NK cells: up-regulation of UL16-binding protein (ULBP)1 and ULBP2 is counteracted by the viral UL16 protein | language = en | journal = Journal of Immunology | volume = 171 | issue = 2 | pages = 902–8 | date = Jul 2003 | pmid = 12847260 | doi = 10.4049/jimmunol.171.2.902 | url = http://www.jimmunol.org/content/171/2/902 }}</ref> Binding of HCMV-encoded UL16 glycoprotein to ULBP1 interferes with cell surface localization of ULBP1; this represents another mechanism by which HCMV-infected cells might escape the immune system.<ref name=":0" /> | ||
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== References == | |||
{{reflist}} | |||
== Further reading == | |||
==Further reading== | |||
{{refbegin | 2}} | {{refbegin | 2}} | ||
* {{cite journal | vauthors = Cerwenka A, Lanier LL | title = NKG2D ligands: unconventional MHC class I-like molecules exploited by viruses and cancer | journal = Tissue Antigens | volume = 61 | issue = 5 | pages = 335–43 | date = May 2003 | pmid = 12753652 | doi = 10.1034/j.1399-0039.2003.00070.x }} | |||
* {{cite journal | vauthors = Steinle A, Li P, Morris DL, Groh V, Lanier LL, Strong RK, Spies T | title = Interactions of human NKG2D with its ligands MICA, MICB, and homologs of the mouse RAE-1 protein family | journal = Immunogenetics | volume = 53 | issue = 4 | pages = 279–87 | year = 2001 | pmid = 11491531 | doi = 10.1007/s002510100325 }} | |||
*{{cite journal | * {{cite journal | vauthors = Sutherland CL, Chalupny NJ, Schooley K, VandenBos T, Kubin M, Cosman D | title = UL16-binding proteins, novel MHC class I-related proteins, bind to NKG2D and activate multiple signaling pathways in primary NK cells | journal = Journal of Immunology | volume = 168 | issue = 2 | pages = 671–9 | date = Jan 2002 | pmid = 11777960 | doi = 10.4049/jimmunol.168.2.671 }} | ||
* {{cite journal | vauthors = Dunn C, Chalupny NJ, Sutherland CL, Dosch S, Sivakumar PV, Johnson DC, Cosman D | title = Human cytomegalovirus glycoprotein UL16 causes intracellular sequestration of NKG2D ligands, protecting against natural killer cell cytotoxicity | journal = The Journal of Experimental Medicine | volume = 197 | issue = 11 | pages = 1427–39 | date = Jun 2003 | pmid = 12782710 | pmc = 2193902 | doi = 10.1084/jem.20022059 }} | |||
*{{cite journal | * {{cite journal | vauthors = Rölle A, Mousavi-Jazi M, Eriksson M, Odeberg J, Söderberg-Nauclér C, Cosman D, Kärre K, Cerboni C | title = Effects of human cytomegalovirus infection on ligands for the activating NKG2D receptor of NK cells: up-regulation of UL16-binding protein (ULBP)1 and ULBP2 is counteracted by the viral UL16 protein | journal = Journal of Immunology | volume = 171 | issue = 2 | pages = 902–8 | date = Jul 2003 | pmid = 12847260 | doi = 10.4049/jimmunol.171.2.902 }} | ||
*{{cite journal | * {{cite journal | vauthors = Eleme K, Taner SB, Onfelt B, Collinson LM, McCann FE, Chalupny NJ, Cosman D, Hopkins C, Magee AI, Davis DM | title = Cell surface organization of stress-inducible proteins ULBP and MICA that stimulate human NK cells and T cells via NKG2D | journal = The Journal of Experimental Medicine | volume = 199 | issue = 7 | pages = 1005–10 | date = Apr 2004 | pmid = 15051759 | pmc = 2211882 | doi = 10.1084/jem.20032194 }} | ||
* {{cite journal | vauthors = Bacon L, Eagle RA, Meyer M, Easom N, Young NT, Trowsdale J | title = Two human ULBP/RAET1 molecules with transmembrane regions are ligands for NKG2D | journal = Journal of Immunology | volume = 173 | issue = 2 | pages = 1078–84 | date = Jul 2004 | pmid = 15240696 | doi = 10.4049/jimmunol.173.2.1078 }} | |||
* {{cite journal | vauthors = López-Soto A, Quiñones-Lombraña A, López-Arbesú R, López-Larrea C, González S | title = Transcriptional regulation of ULBP1, a human ligand of the NKG2D receptor | journal = The Journal of Biological Chemistry | volume = 281 | issue = 41 | pages = 30419–30 | date = Oct 2006 | pmid = 16901903 | doi = 10.1074/jbc.M604868200 }} | |||
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UL16 binding protein 1 (ULBP1) is a cell surface glycoprotein encoded by ULBP1 gene located on the chromosome 6.[1][2] ULBP1 is related to MHC class I molecules, but its gene maps outside the MHC locus.[1][2] The domain structure of ULBP1 differs significantly from those of conventional MHC class I molecules. It does not contain the α3 domain and the transmembrane segment. ULBP1 is thus composed of only the α1α2 domain which is linked to the cell membrane by the GPI anchor.[1][2] It functions as a stress-induced ligand for NKG2D receptor.[1] ULBP1 is, for example, upregulated during HCMV infection.[3] Binding of HCMV-encoded UL16 glycoprotein to ULBP1 interferes with cell surface localization of ULBP1; this represents another mechanism by which HCMV-infected cells might escape the immune system.[3]
References
- ↑ 1.0 1.1 1.2 1.3 Cosman D, Müllberg J, Sutherland CL, Chin W, Armitage R, Fanslow W, Kubin M, Chalupny NJ (Feb 2001). "ULBPs, novel MHC class I-related molecules, bind to CMV glycoprotein UL16 and stimulate NK cytotoxicity through the NKG2D receptor". Immunity. 14 (2): 123–33. doi:10.1016/S1074-7613(01)00095-4. PMID 11239445.
- ↑ 2.0 2.1 2.2 Radosavljevic M, Cuillerier B, Wilson MJ, Clément O, Wicker S, Gilfillan S, Beck S, Trowsdale J, Bahram S (Jan 2002). "A cluster of ten novel MHC class I related genes on human chromosome 6q24.2-q25.3". Genomics. 79 (1): 114–23. doi:10.1006/geno.2001.6673. PMID 11827464.
- ↑ 3.0 3.1 Rölle A, Mousavi-Jazi M, Eriksson M, Odeberg J, Söderberg-Nauclér C, Cosman D, Kärre K, Cerboni C (Jul 2003). "Effects of human cytomegalovirus infection on ligands for the activating NKG2D receptor of NK cells: up-regulation of UL16-binding protein (ULBP)1 and ULBP2 is counteracted by the viral UL16 protein". Journal of Immunology. 171 (2): 902–8. doi:10.4049/jimmunol.171.2.902. PMID 12847260.
Further reading
- Cerwenka A, Lanier LL (May 2003). "NKG2D ligands: unconventional MHC class I-like molecules exploited by viruses and cancer". Tissue Antigens. 61 (5): 335–43. doi:10.1034/j.1399-0039.2003.00070.x. PMID 12753652.
- Steinle A, Li P, Morris DL, Groh V, Lanier LL, Strong RK, Spies T (2001). "Interactions of human NKG2D with its ligands MICA, MICB, and homologs of the mouse RAE-1 protein family". Immunogenetics. 53 (4): 279–87. doi:10.1007/s002510100325. PMID 11491531.
- Sutherland CL, Chalupny NJ, Schooley K, VandenBos T, Kubin M, Cosman D (Jan 2002). "UL16-binding proteins, novel MHC class I-related proteins, bind to NKG2D and activate multiple signaling pathways in primary NK cells". Journal of Immunology. 168 (2): 671–9. doi:10.4049/jimmunol.168.2.671. PMID 11777960.
- Dunn C, Chalupny NJ, Sutherland CL, Dosch S, Sivakumar PV, Johnson DC, Cosman D (Jun 2003). "Human cytomegalovirus glycoprotein UL16 causes intracellular sequestration of NKG2D ligands, protecting against natural killer cell cytotoxicity". The Journal of Experimental Medicine. 197 (11): 1427–39. doi:10.1084/jem.20022059. PMC 2193902. PMID 12782710.
- Rölle A, Mousavi-Jazi M, Eriksson M, Odeberg J, Söderberg-Nauclér C, Cosman D, Kärre K, Cerboni C (Jul 2003). "Effects of human cytomegalovirus infection on ligands for the activating NKG2D receptor of NK cells: up-regulation of UL16-binding protein (ULBP)1 and ULBP2 is counteracted by the viral UL16 protein". Journal of Immunology. 171 (2): 902–8. doi:10.4049/jimmunol.171.2.902. PMID 12847260.
- Eleme K, Taner SB, Onfelt B, Collinson LM, McCann FE, Chalupny NJ, Cosman D, Hopkins C, Magee AI, Davis DM (Apr 2004). "Cell surface organization of stress-inducible proteins ULBP and MICA that stimulate human NK cells and T cells via NKG2D". The Journal of Experimental Medicine. 199 (7): 1005–10. doi:10.1084/jem.20032194. PMC 2211882. PMID 15051759.
- Bacon L, Eagle RA, Meyer M, Easom N, Young NT, Trowsdale J (Jul 2004). "Two human ULBP/RAET1 molecules with transmembrane regions are ligands for NKG2D". Journal of Immunology. 173 (2): 1078–84. doi:10.4049/jimmunol.173.2.1078. PMID 15240696.
- López-Soto A, Quiñones-Lombraña A, López-Arbesú R, López-Larrea C, González S (Oct 2006). "Transcriptional regulation of ULBP1, a human ligand of the NKG2D receptor". The Journal of Biological Chemistry. 281 (41): 30419–30. doi:10.1074/jbc.M604868200. PMID 16901903.
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