Erratum
Benjamin E. Deverman 1,2,3, Brian L. Cook 1,2,3, Scott R. Manson 1,2,3, Robert A. Niederhoff 1,2,3, Ellen M. Langer 1,2,3, Ivana Rosová 1,2,3, Laura A. Kulans 1,2,3, Xiaoyun Fu 2,4, Justin S. Weinberg 2,4, Jay W. Heinecke 2,4, Kevin A. Roth 3,5, and Steven J. Weintraub 1,2,3
In Deverman et al. (Cell 111, 51–62), we concluded that deamidation inactivates Bcl-xL. This conclusion was based partly on results obtained using Bcl-xL constructs in which asparagines 52 and 66 were replaced with aspartates to mimic deamidation. We reported that these constructs lacked the antiapoptotic and BIM-binding function of native Bcl-xL (Figure 4). However, during the course of subsequent studies, we discovered a previously undetected mutation in these constructs. When this secondary mutation was corrected and the resulting constructs were assessed as in Figure 4, we found that their antiapoptotic activity was similar to that of wild-type Bcl-xL and their BIM-binding activity was restored.
However, we stand by our conclusion that deamidation results in the loss of cellular Bcl-xL activity. This is evidenced by our finding that replacement of asparagines 52 and 66 in Bcl-xL with alanines [Bcl-xL(N52A/N66A)] to block deamidation increases the antiapoptotic activity of Bcl-xL, which is stated as “data not shown” in our manuscript (second paragraph from the bottom of the right-hand column on page 55). Thus, all of the other conclusions in the manuscript remain supported. We are currently pursuing studies to determine the precise mechanism by which deamidation results in the loss of cellular Bcl-xL activity.
