Pubmed-entry ::= {
  pmid 17911602,
  medent {
    em std {
      year 2007,
      month 10,
      day 3
    },
    cit {
      title {
        name "Regulation of Ca2+ signaling in mast cells by
 tyrosine-phosphorylated and unphosphorylated non-T cell activation linker."
      },
      authors {
        names ml {
          "Draberova L",
          "Shaik GM",
          "Volna P",
          "Heneberg P",
          "Tumova M",
          "Lebduska P",
          "Korb J",
          "Draber P"
        },
        affil str "Department of Signal Transduction, Academy of Sciences of
 the Czech Republic, Prague, Czech Republic."
      },
      from journal {
        title {
          iso-jta "J. Immunol.",
          ml-jta "J Immunol",
          issn "0022-1767",
          name "Journal of immunology (Baltimore, Md. : 1950)"
        },
        imp {
          date std {
            year 2007,
            month 10,
            day 15
          },
          volume "179",
          issue "8",
          pages "5169-5180",
          language "eng",
          pubstatus ppublish,
          history {
            {
              pubstatus pubmed,
              date std {
                year 2007,
                month 10,
                day 4,
                hour 9,
                minute 0
              }
            },
            {
              pubstatus medline,
              date std {
                year 2007,
                month 12,
                day 6,
                hour 9,
                minute 0
              }
            },
            {
              pubstatus other,
              date std {
                year 2007,
                month 10,
                day 4,
                hour 9,
                minute 0
              }
            }
          }
        }
      },
      ids {
        pii "179/8/5169",
        pubmed 17911602
      }
    },
    abstract "Engagement of the FcepsilonRI in mast cells and basophils leads
 to a rapid tyrosine phosphorylation of the transmembrane adaptors LAT (linker
 for activation of T cells) and NTAL (non-T cell activation linker, also
 called LAB or LAT2). NTAL regulates activation of mast cells by a mechanism,
 which is incompletely understood. Here we report properties of rat basophilic
 leukemia cells with enhanced or reduced NTAL expression. Overexpression of
 NTAL led to changes in cell morphology, enhanced formation of actin filaments
 and inhibition of the FcepsilonRI-induced tyrosine phosphorylation of the
 FcepsilonRI subunits, Syk kinase and LAT and all downstream activation
 events, including calcium and secretory responses. In contrast, reduced
 expression of NTAL had little effect on early FcepsilonRI-induced signaling
 events but inhibited calcium mobilization and secretory response. Calcium
 response was also repressed in Ag-activated cells defective in Grb2, a major
 target of phosphorylated NTAL. Unexpectedly, in cells stimulated with
 thapsigargin, an inhibitor of the endoplasmic reticulum Ca(2+) ATPase, the
 amount of cellular NTAL directly correlated with the uptake of extracellular
 calcium even though no enhanced tyrosine phosphorylation of NTAL was
 observed. The combined data indicate that NTAL regulates FcepsilonRI-mediated
 signaling at multiple steps and by different mechanisms. At early stages NTAL
 interferes with tyrosine phosphorylation of several substrates and formation
 of signaling assemblies, whereas at later stages it regulates the activity of
 store-operated calcium channels through a distinct mechanism independent of
 enhanced NTAL tyrosine phosphorylation.",
    mesh {
      {
        term "Adaptor Proteins, Signal Transducing",
        qual {
          {
            mp TRUE,
            subh "metabolism"
          }
        }
      },
      {
        term "Amino Acid Sequence"
      },
      {
        term "Amino Acid Transport System y+",
        qual {
          {
            mp TRUE,
            subh "physiology"
          }
        }
      },
      {
        term "Animals"
      },
      {
        term "Antigens, CD98 Light Chains",
        qual {
          {
            mp TRUE,
            subh "physiology"
          }
        }
      },
      {
        term "Calcium",
        qual {
          {
            subh "metabolism"
          }
        }
      },
      {
        term "Calcium Signaling",
        qual {
          {
            mp TRUE,
            subh "immunology"
          }
        }
      },
      {
        term "Cell Line, Tumor"
      },
      {
        term "Intracellular Fluid",
        qual {
          {
            subh "metabolism"
          }
        }
      },
      {
        term "Mast Cells",
        qual {
          {
            mp TRUE,
            subh "immunology"
          },
          {
            mp TRUE,
            subh "metabolism"
          }
        }
      },
      {
        term "Molecular Sequence Data"
      },
      {
        term "Phosphorylation"
      },
      {
        term "Rats"
      },
      {
        term "Receptors, IgE",
        qual {
          {
            subh "physiology"
          }
        }
      },
      {
        term "Tyrosine",
        qual {
          {
            mp TRUE,
            subh "metabolism"
          }
        }
      }
    },
    substance {
      {
        type nameonly,
        name "Adaptor Proteins, Signal Transducing"
      },
      {
        type nameonly,
        name "Amino Acid Transport System y+"
      },
      {
        type nameonly,
        name "Antigens, CD98 Light Chains"
      },
      {
        type nameonly,
        name "LAT2 protein, human"
      },
      {
        type nameonly,
        name "Receptors, IgE"
      },
      {
        type nameonly,
        name "Slc7a8 protein, rat"
      },
      {
        type cas,
        cit "55520-40-6",
        name "Tyrosine"
      },
      {
        type cas,
        cit "7440-70-2",
        name "Calcium"
      }
    },
    pmid 17911602,
    pub-type {
      "Comparative Study",
      "Journal Article",
      "Research Support, Non-U.S. Gov't"
    },
    status medline
  }
}

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