CAMLG

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Calcium modulating ligand
Identifiers
Symbols CAMLG ; CAML; MGC163197
External IDs Template:OMIM5 Template:MGI HomoloGene1323
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Calcium modulating ligand, also known as CAMLG, is a human gene.[1]

The immunosuppressant drug cyclosporin A blocks a calcium-dependent signal from the T-cell receptor (TCR) that normally leads to T-cell activation. When bound to cyclophilin B, cyclosporin A binds and inactivates the key signaling intermediate calcineurin. The protein encoded by this gene functions similarly to cyclosporin A, binding to cyclophilin B and acting downstream of the TCR and upstream of calcineurin by causing an influx of calcium. This integral membrane protein appears to be a new participant in the calcium signal transduction pathway, implicating cyclophilin B in calcium signaling, even in the absence of cyclosporin.[1]

References

  1. 1.0 1.1 "Entrez Gene: CAMLG calcium modulating ligand".

Further reading

  • Bram RJ, Crabtree GR (1994). "Calcium signalling in T cells stimulated by a cyclophilin B-binding protein". Nature. 371 (6495): 355–8. doi:10.1038/371355a0. PMID 7522304.
  • Bram RJ, Valentine V, Shapiro DN; et al. (1997). "The gene for calcium-modulating cyclophilin ligand (CAMLG) is located on human chromosome 5q23 and a syntenic region of mouse chromosome 13". Genomics. 31 (2): 257–60. doi:10.1006/geno.1996.0044. PMID 8824814.
  • von Bülow GU, Bram RJ (1997). "NF-AT activation induced by a CAML-interacting member of the tumor necrosis factor receptor superfamily". Science. 278 (5335): 138–41. PMID 9311921.
  • Holloway MP, Bram RJ (1998). "Co-localization of calcium-modulating cyclophilin ligand with intracellular calcium pools". J. Biol. Chem. 273 (26): 16346–50. PMID 9632697.
  • Tovey SC, Bootman MD, Lipp P; et al. (2000). "Calcium-modulating cyclophilin ligand desensitizes hormone-evoked calcium release". Biochem. Biophys. Res. Commun. 276 (1): 97–100. doi:10.1006/bbrc.2000.3442. PMID 11006089.
  • Larramendy ML, Niini T, Elonen E; et al. (2003). "Overexpression of translocation-associated fusion genes of FGFRI, MYC, NPMI, and DEK, but absence of the translocations in acute myeloid leukemia. A microarray analysis". Haematologica. 87 (6): 569–77. PMID 12031912.
  • Feng P, Park J, Lee BS; et al. (2002). "Kaposi's sarcoma-associated herpesvirus mitochondrial K7 protein targets a cellular calcium-modulating cyclophilin ligand to modulate intracellular calcium concentration and inhibit apoptosis". J. Virol. 76 (22): 11491–504. PMID 12388711.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Tran DD, Russell HR, Sutor SL; et al. (2003). "CAML is required for efficient EGF receptor recycling". Dev. Cell. 5 (2): 245–56. PMID 12919676.
  • Kumar R, Lutz W, Frank E, Im HJ (2004). "Immediate early gene X-1 interacts with proteins that modulate apoptosis". Biochem. Biophys. Res. Commun. 323 (4): 1293–8. doi:10.1016/j.bbrc.2004.09.006. PMID 15451437.
  • Guo S, Lopez-Ilasaca M, Dzau VJ (2005). "Identification of calcium-modulating cyclophilin ligand (CAML) as transducer of angiotensin II-mediated nuclear factor of activated T cells (NFAT) activation". J. Biol. Chem. 280 (13): 12536–41. doi:10.1074/jbc.M500296200. PMID 15668245.
  • Nagano J, Kitamura K, Hujer KM; et al. (2006). "Fibrocystin interacts with CAML, a protein involved in Ca2+ signaling". Biochem. Biophys. Res. Commun. 338 (2): 880–9. doi:10.1016/j.bbrc.2005.10.022. PMID 16243292.

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