Free Access
Issue |
Med Sci (Paris)
Volume 22, Number 12, Décembre 2006
|
|
---|---|---|
Page(s) | 1081 - 1086 | |
Section | M/S revues | |
DOI | https://doi.org/10.1051/medsci/200622121081 | |
Published online | 15 December 2006 |
- Pawson T, Scott JD. Signaling through scaffold, anchoring, and adaptor proteins. Science 1997; 278 : 2075–80. [Google Scholar]
- Jordan MS, Singer AL, Koretzky GA. Adaptors as central mediators of signal transduction in immune cells. Nat Immunol 2003; 4 : 110–6. [Google Scholar]
- Ren R, Mayer BJ, Cicchetti P, Baltimore D. Identification of a ten-amino acid proline-rich SH3 binding site. Science 1993; 259 : 1157–61. [Google Scholar]
- Deckert M, Tartare-Deckert S, Hernandez J, et al. Adaptor function for the Syk kinases-interacting protein 3BP2 in IL-2 gene activation. Immunity 1998; 9 : 595–605. [Google Scholar]
- Bell SM, Shaw M, Jou YS, et al. Identification and characterization of the human homologue of SH3BP2, an SH3 binding domain protein within a common region of deletion at 4p16.3 involved in bladder cancer. Genomics 1997; 44 : 163–70. [Google Scholar]
- Foucault I, Le Bras S, Charvet C, et al. The adaptor protein 3BP2 associates with VAV guanine nucleotide exchange factors to regulate NFAT activation by the B-cell antigen receptor. Blood 2005; 105 : 1106–13. [Google Scholar]
- Maeno K, Sada K, Kyo S, et al. Adaptor protein 3BP2 is a potential ligand of Src homology 2 and 3 domains of Lyn protein-tyrosine kinase. J Biol Chem 2003; 278 : 24912–20. [Google Scholar]
- Songyang Z, Shoelson SE, McGlade J, et al. Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav. Mol Cell Biol 1994; 14 : 2777–85. [Google Scholar]
- Kendrick TS, Lipscombe RJ, Rausch O, et al. Contribution of the membrane-distal tyrosine in intracellular signaling by the granulocyte colony-stimulating factor receptor. J Biol Chem 2004; 279 : 326–40. [Google Scholar]
- Sada K, Miah SM, Maeno K, et al. Regulation of FcεRI-mediated degranulation by an adaptor protein 3BP2 in rat basophilic leukemia RBL-2H3 cells. Blood 2002; 100 : 2138–44. [Google Scholar]
- Jevremovic D, Billadeau DD, Schoon RA, et al. Regulation of NK cell-mediated cytotoxicity by the adaptor protein 3BP2. J Immunol 2001; 166 : 7219–28. [Google Scholar]
- Qu X, Kawauchi-Kamata K, Miah SM, et al. Tyrosine phosphorylation of adaptor protein 3BP2 induces T cell receptor-mediated activation of transcription factor. Biochemistry 2005; 44 : 3891–8. [Google Scholar]
- Foucault I, Liu YC, Bernard A, Deckert M. The chaperone protein 14-3-3 interacts with 3BP2/SH3BP2 and regulates its adapter function. J Biol Chem 2003; 278 : 7146–53. [Google Scholar]
- Miah SM, Hatani T, Qu X, et al. Point mutations of 3BP2 identified in human-inherited disease cherubism result in the loss of function. Genes Cells 2004; 9 : 993–1004. [Google Scholar]
- Turner M, Billadeau DD. VAV proteins as signal integrators for multi-subunit immune-recognition receptors. Nat Rev Immunol 2002; 2 : 476–86. [Google Scholar]
- Wu J, Motto DG, Koretzky GA, Weiss A. Vav and SLP-76 interact and functionally cooperate in IL-2 gene activation. Immunity 1996; 4 : 593–602. [Google Scholar]
- Zakaria S, Gomez TS, Savoy DN, et al. Differential regulation of TCR-mediated gene transcription by Vav family members. J Exp Med 2004; 199 : 429–34. [Google Scholar]
- Saborit-Villarroya I, Del Valle JM, Romero X, et al. The adaptor protein 3BP2 binds human CD244 and links this receptor to Vav signaling, ERK activation, and NK cell killing. J Immunol 2005; 175 : 4226–35. [Google Scholar]
- Zollino M, Di Stefano C, Zampino G, et al. Genotype-phenotype correlations and clinical diagnostic criteria in Wolf-Hirschhorn syndrome. Am J Med Genet 2000; 94 : 254–61. [Google Scholar]
- Ueki Y, Tiziani V, Santanna C, et al. Mutations in the gene encoding c-Abl-binding protein SH3BP2 cause cherubism. Nat Genet 2001; 28 : 125–6. [Google Scholar]
- Jones WA. Cherubism: A thumbnail sketch of its diagnosis and a conservative method of treatment. Oral Surg Oral Med Oral Pathol 1965; 20 : 648–53. [Google Scholar]
- Southgate J, Sarma U, Townend JV, et al. Study of the cell biology and biochemistry of cherubism. J Clin Pathol 1998; 51 : 831–7. [Google Scholar]
- Imai Y, Kanno K, Moriya T, et al. A missense mutation in the SH3BP2 gene on chromosome 4p16.3 found in a case of nonfamilial cherubism. Cleft Palate Craniofac J 2003; 40 : 632–8. [Google Scholar]
- Lo B, Faiyaz-Ul-Haque M, Kennedy S, et al. Novel mutation in the gene encoding c-Abl-binding protein SH3BP2 causes cherubism. Am J Med Genet 2003; 121A : 37–40. [Google Scholar]
- Takayanagi H. Mechanistic insight into osteoclast differentiation in osteoimmunology. J Mol Med 2005; 83 : 170–9. [Google Scholar]
- Li B, Boast S, de los Santos K, et al. Mice deficient in Abl are osteoporotic and have defects in osteoblast maturation. Nat Genet 2000; 24 : 304–8. [Google Scholar]
- Soriano P, Montgomery C, Geske R, Bradley A. Targeted disruption of the c-src proto-oncogene leads to osteopetrosis in mice. Cell 1991; 64 : 693–702. [Google Scholar]
- Mocsai A, Humphrey MB, Van Ziffle JA, et al. The immunomodulatory adapter proteins DAP12 and Fc receptor gamma-chain (FcRγ) regulate development of functional osteoclasts through the Syk tyrosine kinase. Proc Natl Acad Sci USA 2004; 101 : 6158–63. [Google Scholar]
- Faccio R, Teitelbaum SL, Fujikawa K, et al. Vav3 regulates osteoclast function and bone mass. Nat Med 2005; 11 : 284–90. [Google Scholar]
- Theill LE, Boyle WJ, Penninger JM. RANK-L and RANK: T cells, bone loss, and mammalian evolution. Annu Rev Immunol 2002; 20 : 795–823. [Google Scholar]
Current usage metrics show cumulative count of Article Views (full-text article views including HTML views, PDF and ePub downloads, according to the available data) and Abstracts Views on Vision4Press platform.
Data correspond to usage on the plateform after 2015. The current usage metrics is available 48-96 hours after online publication and is updated daily on week days.
Initial download of the metrics may take a while.