Tapasin

TAP binding protein (tapasin), also known as TAPBP, is encoded for by a human gene.cite web | title = Entrez Gene: TAPBP TAP binding protein (tapasin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6892| accessdate = ]

PBB_Summary
section_title =
summary_text = This gene encodes a transmembrane glycoprotein which 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 is essential for optimal peptide loading on the MHC class I molecule. Up to four complexes of MHC class I and this protein may be bound to a single TAP molecule. This protein contains a C-terminal double-lysine motif (KKKAE) known to maintain membrane proteins in the endoplasmic reticulum. This gene lies within the major histocompatibility complex on chromosome 6. Alternative splicing results in three transcript variants encoding different isoforms.cite web | title = Entrez Gene: TAPBP TAP binding protein (tapasin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6892| accessdate = ]

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. This protein 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 the Beta₂ microglobulin. 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.cite journal | author = Zhang Y, Williams DB | title = Assembly of MHC class I molecules within the endoplasmic reticulum | journal = Immunol. Res. | volume = 35 | issue = 1-2 | pages = 151–62 | year = 2006 | pmid = 17003517 | doi = 10.1385/IR:35:1:151 | issn = ]

ee also

* Transporter associated with antigen processing ("TAP")

References

Further reading

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

External links

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