Lymphotoxin beta receptor

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LTBR
Lymphotoxin b receptor.png
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesLTBR, CD18, D12S370, LT-BETA-R, TNF-R-III, TNFCR, TNFR-RP, TNFR2-RP, TNFR3, TNFRSF3, lymphotoxin beta receptor
External IDsOMIM: 600979 MGI: 104875 HomoloGene: 1753 GeneCards: LTBR
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for LTBR
Genomic location for LTBR
Band12p13.31Start6,375,045 bp[1]
End6,391,571 bp[1]
RNA expression pattern
PBB GE LTBR 203005 at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001270987
NM_002342

NM_010736

RefSeq (protein)

NP_001257916
NP_002333

NP_034866

Location (UCSC)Chr 12: 6.38 – 6.39 MbChr 6: 125.31 – 125.31 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Lymphotoxin beta receptor (LTBR), also known as tumor necrosis factor receptor superfamily member 3 (TNFRSF3), is a cell surface receptor for lymphotoxin involved in apoptosis and cytokine release.[5][6][7] It is a member of the tumor necrosis factor receptor superfamily.

Function[edit]

The protein encoded by this gene is a member of the tumor necrosis factor (TNF) family of receptors. It is expressed on the surface of most cell types, including cells of epithelial and myeloid lineages, but not on T and B lymphocytes. The protein specifically binds the lymphotoxin membrane form (a complex of lymphotoxin-alpha and lymphtoxin-beta). The encoded protein and its ligand play a role in the development and organization of lymphoid tissue and transformed cells. Activation of the encoded protein can trigger apoptosis.[5]

Not only does the LTBR help trigger apoptosis, it can lead to the release of the cytokine interleukin 8. Overexpression of LTBR in HEK293 cells increases IL-8 promoter activity and leads to IL-8 release. LTBR is also essential for development and organization of the secondary lymphoid organs and chemokine release.[8]

Structure[edit]

The Ramachandran plots show that 64.6% of all residues were in a favored region. This structure was found using X-ray diffraction. The resolution is 3.50 angstroms. The alpha and beta angles are 90 degrees while the gamma angle is 120 degrees.[9]

Interactions[edit]

Lymphotoxin beta receptor has been shown to interact with Diablo homolog[10] and TRAF3.[11][12][13]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000111321 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000030339 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: LTBR lymphotoxin beta receptor (TNFR superfamily, member 3)".
  6. ^ Baens M, Chaffanet M, Cassiman JJ, van den Berghe H, Marynen P (April 1993). "Construction and evaluation of a hncDNA library of human 12p transcribed sequences derived from a somatic cell hybrid". Genomics. 16 (1): 214–8. doi:10.1006/geno.1993.1161. PMID 8486360.
  7. ^ Crowe PD, VanArsdale TL, Walter BN, Ware CF, Hession C, Ehrenfels B, Browning JL, Din WS, Goodwin RG, Smith CA (April 1994). "A lymphotoxin-beta-specific receptor". Science. 264 (5159): 707–10. Bibcode:1994Sci...264..707C. doi:10.1126/science.8171323. PMID 8171323.
  8. ^ Chang YH, Hsieh SL, Chen MC, Lin WW (August 2002). "Lymphotoxin beta receptor induces interleukin 8 gene expression via NF-kappaB and AP-1 activation". Exp. Cell Res. 278 (2): 166–74. doi:10.1006/excr.2002.5573. PMID 12169272.
  9. ^ "MolProbity Ramachandran analysis" (PDF).
  10. ^ Kuai, Jun; Nickbarg Elliott; Wooters Joe; Qiu Yongchang; Wang Jack; Lin Lih-Ling (Apr 2003). "Endogenous association of TRAF2, TRAF3, cIAP1, and Smac with lymphotoxin beta receptor reveals a novel mechanism of apoptosis". J. Biol. Chem. United States. 278 (16): 14363–9. doi:10.1074/jbc.M208672200. ISSN 0021-9258. PMID 12571250.
  11. ^ VanArsdale, T L; VanArsdale S L; Force W R; Walter B N; Mosialos G; Kieff E; Reed J C; Ware C F (Mar 1997). "Lymphotoxin-beta receptor signaling complex: role of tumor necrosis factor receptor-associated factor 3 recruitment in cell death and activation of nuclear factor kappaB". Proc. Natl. Acad. Sci. U.S.A. UNITED STATES. 94 (6): 2460–5. Bibcode:1997PNAS...94.2460V. doi:10.1073/pnas.94.6.2460. ISSN 0027-8424. PMC 20110. PMID 9122217.
  12. ^ Wu, M Y; Wang P Y; Han S H; Hsieh S L (Apr 1999). "The cytoplasmic domain of the lymphotoxin-beta receptor mediates cell death in HeLa cells". J. Biol. Chem. UNITED STATES. 274 (17): 11868–73. doi:10.1074/jbc.274.17.11868. ISSN 0021-9258. PMID 10207006.
  13. ^ Marsters, S A; Ayres T M; Skubatch M; Gray C L; Rothe M; Ashkenazi A (May 1997). "Herpesvirus entry mediator, a member of the tumor necrosis factor receptor (TNFR) family, interacts with members of the TNFR-associated factor family and activates the transcription factors NF-kappaB and AP-1". J. Biol. Chem. UNITED STATES. 272 (22): 14029–32. doi:10.1074/jbc.272.22.14029. ISSN 0021-9258. PMID 9162022.

Further reading[edit]

External links[edit]