BAD Ser128 is not phosphorylated by c-Jun NH2- terminal kinase for promoting apoptosis

Jiyan Zhang, Jing Liu, Chenfei Yu, Anning Lin*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

17 Scopus citations


The phosphorylation and regulation of the proapoptotic Bcl-2 family protein BAD by c-Jun NH2-terminal kinase (JNK) is controversial. JNK can suppress interleukin-3 withdrawal-induced apoptosis via phosphorylation of BAD at Thr201. However, it has also been reported that JNK promotes apoptosis through phosphorylation of BAD at Ser128. Here, we report that JNK is not a BAD Ser128 kinase. JNK phosphorylates murine BAD (mBAD), but not human BAD (hBAD), in which Ser91 is equivalent to Ser128 in mBAD. In contrast, Cdc2, which phosphorylates Ser 128, phosphorylates both mBAD and hBAD. Replacement of Ser 128 by alanine has no effects on BAD phosphorylation by JNK in vitro and in vivo. Two-dimensional phosphopeptide mapping in combination with phosphoamino acid analysis reveals that JNK does not phosphorylate BAD at Ser128. Elimination of Ser128 phosphorylation has no effects on the proapoptotic activity of BAD in apoptosis induced by UV via JNK or growth factor withdrawal. Thus, our results show that Ser128 is not phosphorylated by JNK for promoting cell death.

Original languageEnglish (US)
Pages (from-to)8372-8378
Number of pages7
JournalCancer Research
Issue number18
StatePublished - Sep 15 2005

ASJC Scopus subject areas

  • Oncology
  • Cancer Research


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