Vol. 203, No. 2, February 20, 2006. Pages 281–287.

Please note that an error appeared in the online early release version of this article. The final html, pdf, and print versions have been corrected. For reference, the correction appears below.

The authors regret that an acknowledgment was left out of the first sentence of the Mice section under Materials and methods. The sentence should have read: “TSAd (+/+) and (−/−) C57BL/6 mice were obtained from Dr. Jeff Bluestone (University of California, San Francisco, San Francisco, CA) and were bred in our laboratory (4).”

Also, Fig. 2 contained a labeling error. In panels A and B, all instances of “100” should have read “150.” The corrected figure and its legend appear below.

Figure 2.

Impaired LAT phosphorylation and interaction with PLCγ1 and Grb-2 in TSAd-deficient T cells. LN T cells from TSAd (+/+) and (−/−) mice were stimulated with optimal concentrations of CD3 and CD28 mAb for the indicated times (in min). (A) PLCγ1 activation was assessed by Western blotting of whole cell lysates using a phospho-specific antibody. (B) LAT was immunoprecipitated from lysates. Phosphorylation of immunoprecipitated LAT on Y136 and Y195 and coimmunoprecipitation of PLCγ1 and Grb-2 was detected by Western blotting using specific antibodies. (C) Activation of ZAP-70 was assessed by Western blotting of whole cell lysates using a phospho-specific antibody.

Figure 2.

Impaired LAT phosphorylation and interaction with PLCγ1 and Grb-2 in TSAd-deficient T cells. LN T cells from TSAd (+/+) and (−/−) mice were stimulated with optimal concentrations of CD3 and CD28 mAb for the indicated times (in min). (A) PLCγ1 activation was assessed by Western blotting of whole cell lysates using a phospho-specific antibody. (B) LAT was immunoprecipitated from lysates. Phosphorylation of immunoprecipitated LAT on Y136 and Y195 and coimmunoprecipitation of PLCγ1 and Grb-2 was detected by Western blotting using specific antibodies. (C) Activation of ZAP-70 was assessed by Western blotting of whole cell lysates using a phospho-specific antibody.

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