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Phosphorylation status modulates Bcl‐2 function during glucocorticoid‐induced apoptosis in T lymphocytes
Author(s) -
Huang SeTe J.,
Cidlowski John A.
Publication year - 2002
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fj.01-0852com
Subject(s) - apoptosis , phosphorylation , programmed cell death , serine , dna fragmentation , glucocorticoid , biology , mutant , microbiology and biotechnology , transfection , kinase , cell culture , biochemistry , gene , immunology , genetics
Glucocorticoids are known to induce apoptosis in lymphoid cells, and Bcl‐2 overexpression can block the apoptosis‐inducing action of glucocorticoids. Since phosphorylation of Bcl‐2 is implicated in regulating Bcl‐2 function, we considered the role of Bcl‐2 phosphorylation in protecting lymphoid cells from glucocorticoidinduced cell death. Five stably transfected cell lines of WEHI 7.1 cells expressing either wild‐type Bcl‐2 or alanine mutants of Bcl‐2 at amino acids threonine 56, serine 70, threonine 74, or serine 87 were created. Expression of the mutant Bcl‐2 proteins was documented by flow cytometry and Western blot analysis. Mutation of Bcl‐2 on T56 and S87 eliminated the ability of Bcl‐2 to inhibit glucocorticoid‐induced cell shrinkage, mitochondrial depolarization, DNA fragmentation, and cell death. Mutation of T74 only partially impaired the ability of Bcl‐2 to block glucocorticoid‐induced apoptosis whereas mutation of S70 in Bcl‐2 did not alter its ability to block glucocorticoidinduced apoptosis.—Huang, S.‐T. J., Cidlowski, J. A. Phosphorylation status modulates Bcl‐2 function during glucocorticoid‐induced apoptosis in T lymphocytes. FASEB J. 16, 825–832 (2002)