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Survival factor-induced extracellular signal-regulated kinase phosphorylates BIM, inhibiting its association with BAX and proapoptotic activity
Open accessAbstract
The “BH3-only” proapoptotic BCL-2 family members initiate the intrinsic apoptotic pathway. A small interfering RNA knockdown of BIM confirms this BH3-only member is important for the cytokine-mediated homeostasis of hematopoietic cells. We show here that the phosphorylation status of BIM controls its proapoptotic activity. IL-3, a hematopoietic survival factor, induces extracellular signal-regulated kinase/mitogen-activated protein kinase-mediated phosphorylation of BIM on three serine sites (S55, S65, and S100). After IL-3 withdrawal, only nonphosphorylated BIM interacts with the multidomain proapoptotic effector BAX. Phosphorylation of BIM on exposure of cells to IL-3 dramatically reduces the BIM/BAX interaction. A nonphosphorylatable BIM molecule (S55A, S65A, and S100A) demonstrates enhanced interaction with BAX and enhanced proapoptotic activity. Thus, ERK/mitogen-activated protein kinase-dependent phosphorylation of BIM in response to survival factor regulates BIM/BAX interaction and the pro-death activity of BIM.
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Metadata
- Authors
- Harada, H., Quearry, B., Ruiz-Vela, A., & Korsmeyer, S. J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2004-10-14
- Volume
- 101
- Issue
- 43
- Pages
- 15313-15317
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2121796473
- Cited by
- 287
- References
- 3
- FWCI
- 9.84
- Type
- journal article
- Language
- en
- Open access
- green
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