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Article

Novel role for JNK as a stress-activated Bcl2 kinase.

The Journal of biological chemistry - 29 Jun 2001

Deng X, Xiao L, Lang W, Gao F, Ruvolo P, May W S

Abstract excerpt

Interleukin (IL)-3-induced Bcl2 phosphorylation at Ser(70) may be required for its full and potent antiapoptotic activity. However, in the absence of IL-3, increased expression of Bcl2 can also prolong cell survival. To determine how Bcl2 may be functionally phosphorylated following IL-3 withdrawal, a stress-activated Bcl2 kinase (SAK) was sought. Results indicate that anisomycin, a potent activator of the stress...

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Identifiers

PMID: 11323415
DOI: 10.1074/jbc.M100279200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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