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Cited by 309

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BAD Ser-155 Phosphorylation Regulates BAD/Bcl-XL Interaction and Cell Survival

Open access
Tan, Yi, Demeter, Matthew R., Ruan, Hong, Comb, Michael J.·2000·Journal of Biological Chemistry

Abstract

The BH3 domain of BAD mediates its death-promoting activities via heterodimerization to the Bcl-XL family of death regulators. Growth and survival factors inhibit the death-promoting activity of BAD by stimulating phosphorylation at multiple sites including Ser-112 and Ser-136. Phosphorylation at these sites promotes binding of BAD to 14-3-3 proteins, sequestering BAD away from the mitochondrial membrane where it dimerizes with Bcl-XL to exert its killing effects. We report here that the phosphorylation of BAD at Ser-155 within the BH3 domain is a second phosphorylation-dependent mechanism that inhibits the death-promoting activity of BAD. Protein kinase A, RSK1, and survival factor signaling stimulate phosphorylation of BAD at Ser-155, blocking the binding of BAD to Bcl-XL. RSK1 phosphorylates BAD at both Ser-112 and Ser-155 and rescues BAD-mediated cell death in a manner dependent upon phosphorylation at both sites.

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Metadata

Authors
Tan, Y., Demeter, M. R., Ruan, H., & Comb, M. J.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2000-08
Volume
275
Issue
33
Pages
25865-25869
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2007486260
Cited by
309
References
1
FWCI
6.87
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: BAD Ser-155 Phosphorylation Regulates BAD/Bcl-XL Interaction and Cell Survival. https://app.cochat.ai/papers/10.1074/jbc.m004199200
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Tan, Y., Demeter, M. R., Ruan, H., & Comb, M. J. (2000). BAD Ser-155 Phosphorylation Regulates BAD/Bcl-XL Interaction and Cell Survival. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m004199200

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