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Tapasin

 
Wikipedia: Tapasin
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TAP binding protein (tapasin)
Identifiers
Symbols TAPBP; NGS17; TAPA; TPN; TPSN
External IDs OMIM601962 MGI1201689 HomoloGene2401 GeneCards: TAPBP Gene
RNA expression pattern
PBB GE TAPBP 210294 at tn.png
PBB GE TAPBP 208829 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 6892 21356
Ensembl ENSG00000112493 ENSMUSG00000024308
UniProt O15533 Q3TCU5
RefSeq (mRNA) NM_003190 NM_001025313
RefSeq (protein) NP_003181 NP_001020484
Location (UCSC) Chr 6:
33.38 - 33.39 Mb
Chr 17:
33.53 - 33.54 Mb
PubMed search [1] [2]

TAP-associated glycoprotein also known as tapasin or TAPBP is a protein[1] [2] that, in humans, is encoded by the TAPBP gene.[3]

Contents

Function

This gene encodes a transmembrane glycoprotein that mediates interaction between newly-assembled major histocompatibility complex (MHC) class I molecules and the transporter associated with antigen processing (TAP), which is required for the transport of antigenic peptides across the endoplasmic reticulum membrane. This interaction facilitates optimal peptide loading on the MHC class I molecule. Up to four complexes of MHC class I and tapasin may be bound to a single TAP molecule. Tapasin contains a C-terminal double-lysine motif (KKKAE) known to maintain membrane proteins in the endoplasmic reticulum. In humans, the tapasin gene lies within the major histocompatibility complex on chromosome 6. Alternative splicing results in three transcript variants encoding different isoforms.[3]

Tapasin is a MHC class I antigen-processing molecule present in the lumen of the endoplasmic reticulum. It plays an important role in the maturation of MHC class I molecules in the ER lumen. Tapasin is one component of the peptide-loading complex, and can be found associated with MHC class I molecules after the MHC class I heavy chain has associated with Beta2 microglobulin. The peptide-loading complex consists of TAP, tapasin, MHC class I, calreticulin, and ERp57. Tapasin recruits MHC class I molecules to the TAP peptide transporter, and also enhances loading of MHC class I with high-affinity peptides. Following loading of MHC class I with a high-affinity ligand, the interaction between tapasin and MHC class I disappears.[4]

Interactions

Tapasin has been shown to interact with TAP1[5][6] and HLA-A.[6]

See also

References

  1. ^ Sadasivan B, Lehner PJ, Ortmann B, Spies T, Cresswell P (August 1996). "Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP". Immunity 5 (2): 103–14. PMID 8769474. 
  2. ^ Li, S., Sjogren, H.O., Hellman, U., Pettersson, R.F. & Wang, P. (May 1997). Cloning and functional characterization of a subunit of the transporter associated with antigen processing.. PMID 9238042. 
  3. ^ a b "Entrez Gene: TAPBP TAP binding protein (tapasin)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6892. 
  4. ^ Zhang Y, Williams DB (2006). "Assembly of MHC class I molecules within the endoplasmic reticulum". Immunol. Res. 35 (1-2): 151–62. doi:10.1385/IR:35:1:151. PMID 17003517. 
  5. ^ Raghuraman, Gayatri; Lapinski Philip Edward, Raghavan Malini (Nov. 2002). "Tapasin interacts with the membrane-spanning domains of both TAP subunits and enhances the structural stability of TAP1 x TAP2 Complexes". J. Biol. Chem. (United States) 277 (44): 41786–94. doi:10.1074/jbc.M207128200. ISSN 0021-9258. PMID 12213826. 
  6. ^ a b Paulsson, Kajsa M; Kleijmeer Monique J, Griffith Janice, Jevon Marc, Chen Shangwu, Anderson Per O, Sjogren Hans-Olov, Li Suling, Wang Ping (May. 2002). "Association of tapasin and COPI provides a mechanism for the retrograde transport of major histocompatibility complex (MHC) class I molecules from the Golgi complex to the endoplasmic reticulum". J. Biol. Chem. (United States) 277 (21): 18266–71. doi:10.1074/jbc.M201388200. ISSN 0021-9258. PMID 11884415. 

Further reading

  • Turnquist HR, Vargas SE, Schenk EL, et al. (2002). "The interface between tapasin and MHC class I: identification of amino acid residues in both proteins that influence their interaction.". Immunol. Res. 25 (3): 261–9. doi:10.1385/IR:25:3:261. PMID 12018464. 
  • Momburg F, Tan P (2002). "Tapasin-the keystone of the loading complex optimizing peptide binding by MHC class I molecules in the endoplasmic reticulum.". Mol. Immunol. 39 (3-4): 217–33. doi:10.1016/S0161-5890(02)00103-7. PMID 12200052. 
  • Dissemond J, Kothen T, Mörs J, et al. (2004). "Downregulation of tapasin expression in progressive human malignant melanoma.". Arch. Dermatol. Res. 295 (2): 43–9. doi:10.1007/s00403-003-0393-8. PMID 12682852. 
  • Paulsson K, Wang P (2003). "Chaperones and folding of MHC class I molecules in the endoplasmic reticulum.". Biochim. Biophys. Acta 1641 (1): 1–12. doi:10.1016/S0167-4889(03)00048-X. PMID 12788224. 
  • Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction.". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474. 
  • Sadasivan B, Lehner PJ, Ortmann B, et al. (1996). "Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP.". Immunity 5 (2): 103–14. doi:10.1016/S1074-7613(00)80487-2. PMID 8769474. 
  • Lewis JW, Neisig A, Neefjes J, Elliott T (1997). "Point mutations in the alpha 2 domain of HLA-A2.1 define a functionally relevant interaction with TAP.". Curr. Biol. 6 (7): 873–83. doi:10.1016/S0960-9822(02)00611-5. PMID 8805302. 
  • Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353–8. PMID 9110174. 
  • Li S, Sjögren HO, Hellman U, et al. (1997). "Cloning and functional characterization of a subunit of the transporter associated with antigen processing.". Proc. Natl. Acad. Sci. U.S.A. 94 (16): 8708–13. doi:10.1073/pnas.94.16.8708. PMID 9238042. 
  • Ortmann B, Copeman J, Lehner PJ, et al. (1997). "A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes.". Science 277 (5330): 1306–9. doi:10.1126/science.277.5330.1306. PMID 9271576. 
  • Herberg JA, Sgouros J, Jones T, et al. (1998). "Genomic analysis of the Tapasin gene, located close to the TAP loci in the MHC.". Eur. J. Immunol. 28 (2): 459–67. doi:10.1002/(SICI)1521-4141(199802)28:02<459::AID-IMMU459>3.0.CO;2-Z. PMID 9521053. 
  • Lindquist JA, Jensen ON, Mann M, Hämmerling GJ (1998). "ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly.". Embo J. 17 (8): 2186–95. doi:10.1093/emboj/17.8.2186. PMID 9545232. 
  • Herberg JA, Beck S, Trowsdale J (1998). "TAPASIN, DAXX, RGL2, HKE2 and four new genes (BING 1, 3 to 5) form a dense cluster at the centromeric end of the MHC.". J. Mol. Biol. 277 (4): 839–57. doi:10.1006/jmbi.1998.1637. PMID 9545376. 
  • Furukawa H, Kashiwase K, Yabe T, et al. (1999). "Polymorphism of TAPASIN and its linkage disequilibria with HLA class II genes in the Japanese population.". Tissue Antigens 52 (3): 279–81. doi:10.1111/j.1399-0039.1998.tb03044.x. PMID 9802609. 
  • El Ouakfaoui S, Heitz D, Paquin R, Beaulieu AD (1999). "Granulocyte-macrophage colony-stimulating factor modulates tapasin expression in human neutrophils.". J. Leukoc. Biol. 65 (2): 205–10. PMID 10088603. 
  • Bangia N, Lehner PJ, Hughes EA, et al. (1999). "The N-terminal region of tapasin is required to stabilize the MHC class I loading complex.". Eur. J. Immunol. 29 (6): 1858–70. doi:10.1002/(SICI)1521-4141(199906)29:06<1858::AID-IMMU1858>3.0.CO;2-C. PMID 10382748. 
  • Knittler MR, Alberts P, Deverson EV, Howard JC (2000). "Nucleotide binding by TAP mediates association with peptide and release of assembled MHC class I molecules.". Curr. Biol. 9 (18): 999–1008. doi:10.1016/S0960-9822(99)80448-5. PMID 10508608. 
  • Li S, Paulsson KM, Chen S, et al. (2000). "Tapasin is required for efficient peptide binding to transporter associated with antigen processing.". J. Biol. Chem. 275 (3): 1581–6. doi:10.1074/jbc.275.3.1581. PMID 10636848. 
  • Tan P, Kropshofer H, Mandelboim O, et al. (2002). "Recruitment of MHC class I molecules by tapasin into the transporter associated with antigen processing-associated complex is essential for optimal peptide loading.". J. Immunol. 168 (4): 1950–60. PMID 11823531. 
  • Mayer WE, Klein J (2002). "Is tapasin a modified Mhc class I molecule?". Immunogenetics 53 (9): 719–23. doi:10.1007/s00251-001-0403-y. PMID 11862402. 

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