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Gene Review: 

Pdlim7  -  PDZ and LIM domain 7

Mus musculus

 
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Disease relevance of Pdlim7

  • Another form of LMP (D1LMP), deleted for the amino terminus and first four putative transmembrane domains of LMP, was recently shown to be expressed late in Epstein-Barr virus replication [1].
 

High impact information on Pdlim7

  • These observations suggest that the LMP complex may be responsible for generating peptides from cytoplasmic antigen during antigen processing [2].
  • The class II region of the major histocompatibility complex (MHC) contains genes encoding at least two subunits of a large, intracellular protein complex (the low molecular mass polypeptide, or LMP, complex) [2].
  • Analyses of transcript sizes, tissue distribution, sequence, and genetic mapping data suggest that none of these genes code for LMP antigens [3].
  • We conclude that LIM domains of Enigma recognize tyrosine-containing motifs with specificity residing in both the LIM domains and in the target structures [4].
  • Although the association with Enigma required Tyr-586 of Ret/ptc2, the interaction was phosphorylation-independent [5].
 

Biological context of Pdlim7

  • For two determinants, the kinetics of presentation are shown to be similar for LMP-expressing and -nonexpressing cells [6].
  • In many cases, the lack of antigen presentation can be attributed to the downregulation of genes needed for antigen processing, such as the transporters associated with antigen processing (TAP) 1, and the proteasomal component, low molecular weight proteins (LMP) 2 [7].
  • The BNLF-1 protein (also termed LMP) is a membrane protein, and its predicted amino acid sequence indicates that the protein has six membrane-spanning segments in addition to a short amino-terminal (approximately 25 amino acids) and a long carboxyl-terminal (approximately 200 amino acids) cytoplasmic domain [8].
  • In both cell types, loss of contact inhibition and anchorage independence are acutely evident after LMP expression [1].
  • It showed a more drastic shift towards an LCL-like phenotype than the other convertants as reflected by high HLA class-I and EBV-encoded latent membrane protein (LMP) expression [9].
 

Anatomical context of Pdlim7

  • Similar alteration in actin cytoskeleton organisation was observed in cells expressing both Enigma and APS with a mutation in the NPTY motif [10].
  • Cloned cytotoxic and non-cytotoxic lymphocytes in mouse and man: their reactivities and a large cell surface membrane protein (LMP) differentiation marker system [11].
  • Molecular relationships between large membrane proteins (LMP) expressed on T and B lymphocytes [12].
  • Clones prepared from day 5 mixed lymphocyte cultures (MLC) were examined for the expression of large (170,000- to 200,000-dalton) membrane proteins (LMP), found on bulk cultures of resting and allogeneically activated T lymphocytes [12].
  • LMP activity and D1LMP inactivity in inducing anchorage-independent growth are not restricted to Rat-1 cells, but are also evident in BALB/c 3T3 cells [1].
 

Associations of Pdlim7 with chemical compounds

  • Interaction of two random peptide libraries with glutathione S-transferase-LIM3 of Enigma indicated specific binding to Gly-Pro-Hyd-Gly-Pro-Hyd-Tyr-Ala corresponding to the major endocytic code of InsR [4].
 

Other interactions of Pdlim7

  • This interaction required the NPTY motif of APS and the LIM domains of Enigma [10].
 

Analytical, diagnostic and therapeutic context of Pdlim7

  • We developed an improved method for the dye-exclusion microcytotoxicity test by introducing low melting point agarose (LMP-Aga) into the assay medium [13].

References

  1. The truncated form of the Epstein-Barr virus latent-infection membrane protein expressed in virus replication does not transform rodent fibroblasts. Wang, D., Liebowitz, D., Kieff, E. J. Virol. (1988)
  2. Homology of proteasome subunits to a major histocompatibility complex-linked LMP gene. Martinez, C.K., Monaco, J.J. Nature (1991)
  3. A cluster of transcribed sequences between the Pb and Ob genes of the murine major histocompatibility complex. Cho, S., Attaya, M., Brown, M.G., Monaco, J.J. Proc. Natl. Acad. Sci. U.S.A. (1991)
  4. Specificity of LIM domain interactions with receptor tyrosine kinases. Wu, R., Durick, K., Songyang, Z., Cantley, L.C., Taylor, S.S., Gill, G.N. J. Biol. Chem. (1996)
  5. Mitogenic signaling by Ret/ptc2 requires association with enigma via a LIM domain. Durick, K., Wu, R.Y., Gill, G.N., Taylor, S.S. J. Biol. Chem. (1996)
  6. MHC-encoded proteasome subunits LMP2 and LMP7 are not required for efficient antigen presentation. Yewdell, J., Lapham, C., Bacik, I., Spies, T., Bennink, J. J. Immunol. (1994)
  7. The mutation in the ATP-binding region of JAK1, identified in human uterine leiomyosarcomas, results in defective interferon-gamma inducibility of TAP1 and LMP2. Hayashi, T., Kobayashi, Y., Kohsaka, S., Sano, K. Oncogene (2006)
  8. The multiple membrane-spanning segments of the BNLF-1 oncogene from Epstein-Barr virus are required for transformation. Baichwal, V.R., Sugden, B. Oncogene (1989)
  9. Reversion of tumorigenicity and decreased agarose clonability after EBV conversion of an IgH/myc translocation-carrying BL line. Torsteinsdóttir, S., Andersson, M.L., Avila-Cariño, J., Ehlin-Henriksson, B., Masucci, M.G., Klein, G., Klein, E. Int. J. Cancer (1989)
  10. The interaction between the adaptor protein APS and Enigma is involved in actin organisation. Barrès, R., Gonzalez, T., Le Marchand-Brustel, Y., Tanti, J.F. Exp. Cell Res. (2005)
  11. Cloned cytotoxic and non-cytotoxic lymphocytes in mouse and man: their reactivities and a large cell surface membrane protein (LMP) differentiation marker system. Bach, F.H., Alter, B.J., Widmer, M.B., Segall, M., Dunlap, B. Immunol. Rev. (1981)
  12. Molecular relationships between large membrane proteins (LMP) expressed on T and B lymphocytes. Dunlap, B., Mixter, P.F., Koller, B., Watson, A., Widmer, M.B., Bach, F.H. J. Immunol. (1980)
  13. Further improvement of dye-exclusion microcytotoxicity assay by introducing low melting point agarose into the medium. Kubota, E., Ishikawa, H., Saito, K. J. Immunol. Methods (1983)
 
 
 
 
 
 
 
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