Difference between revisions of "Part:BBa K3582301"
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Basigin is a major signalling receptor for cyclophilin A (and cyclophilin B, a related molecule) which when secreted exhibits chemotactic activity for neutrophils, eosinophils and T cells[5][6]
 
Basigin is a major signalling receptor for cyclophilin A (and cyclophilin B, a related molecule) which when secreted exhibits chemotactic activity for neutrophils, eosinophils and T cells[5][6]
  
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[[Image:1 BBa K3582301.png|300px|thumb|center|Figure 1.Structure of the interacting domain of Basigin Protein.]]
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[[Image:1 BBa K3582301.png|400px|thumb|center|Figure 1.Structure of the interacting domain of Basigin Protein.]]
  
  

Revision as of 15:44, 26 October 2020


Basigin protein

Basigin (BSG) is a member of the Ig superfamily and is important in numerous physiological and pathological phenomena. It is a highly glycosylated transmembrane protein and can recognize molecules both in the same membrane (cis-recognition) as well as those located extracellularly[1].

Basigin is known to bind to MonoCarboxylate Transporter(MCTs) which catalyse the transport of substituted short-chain fatty acids across the plasma membrane[2]. Basigin acts as a chaperone, important for the membrane translocation of MCTs. By associating with MCTs, Basigin plays an important role in energy metabolism. The tight association between Basigin and MCTs is consistent with the high level of expression of BSG in metabolically active cells, such as tumour cells and activated lymphocytes[3]

CD98, CD43, MCT4 and galectin-3 are important proteins that mediate binding between Basigin and integrins. BSG directly binds to CD98, which can covalently bind to amino acid transporters and hence can associate with integrins. Therefore, BSG can interact with integrins through CD98[4]

Basigin is a major signalling receptor for cyclophilin A (and cyclophilin B, a related molecule) which when secreted exhibits chemotactic activity for neutrophils, eosinophils and T cells[5][6]

File:1 BBa K3582301.png
Figure 1.Structure of the interacting domain of Basigin Protein.


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 67
    Illegal NgoMIV site found at 730
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 358
    Illegal SapI.rc site found at 330
    Illegal SapI.rc site found at 747

References

  • [1]Muramatsu, T. (2015). Basigin (CD147), a multifunctional transmembrane glycoprotein with various binding partners. Journal of Biochemistry, 159(5), 481–490. https://doi.org/10.1093/jb/mvv127
  • [2]Halestrap, A. P. (2011). The monocarboxylate transporter family-Structure and functional characterization. IUBMB Life, 64(1), 1–9. https://doi.org/10.1002/iub.573
  • [3]Kirk, P., Wilson, M. C., Heddle, C., Brown, M. H., Barclay, A. N., & Halestrap, A. P. (2000). CD147 is tightly associated with lactate transporters MCT1 and MCT4 and facilitates their cell surface expression. The EMBO Journal, 19(15), 3896–3904. https://doi.org/10.1093/emboj/19.15.3896
  • [4]Xu, D., & Hemler, M. E. (2005). Metabolic Activation-related CD147-CD98 Complex. Molecular & Cellular Proteomics, 4(8), 1061–1071. https://doi.org/10.1074/mcp.m400207-mcp200
  • [5]Yurchenko, V., Constant, S., Eisenmesser, E., & Bukrinsky, M. (2010). Cyclophilin-CD147 interactions: a new target for anti-inflammatory therapeutics. Clinical & Experimental Immunology, 160(3), 305–317. https://doi.org/10.1111/j.1365-2249.2010.04115.x
  • [6]Yurchenko, V., Zybarth, G., O’Connor, M., Dai, W. W., Franchin, G., Hao, T., Guo, H., Hung, H.-C., Toole, B., Gallay, P., Sherry, B., & Bukrinsky, M. (2002). Active Site Residues of Cyclophilin A Are Crucial for Its Signaling Activity via CD147. Journal of Biological Chemistry, 277(25), 22959–22965. https://doi.org/10.1074/jbc.m201593200