A non-enzymatic p21 protein inhibitor of stress-activated protein kinases

J. Shim, H. Lee, J. Park, H. Kim, E. J. Choi

Research output: Contribution to journalArticle

239 Citations (Scopus)

Abstract

The stress-activated protein kinases (SAPKs), which are identical to the c-Jun amino-terminal kinases (JNKs), are activated in response to a variety of cellular stresses, including DNA damage, heat shock or tumour-necrosis factor-α. SAPK, a subfamily of the mitogen-activated protein (MAP) kinases, is a major protein kinase that phosphorylates c-Jun and other transcription factors. SAPK phosphorylation of transcription factors is important in stress-activated signalling cascades. Here we report that the protein p21(WAF1/CIP1/Sd11), a DNA-damage-inducible cell-cycle inhibitor, acts as an inhibitor of the SAPK group of mammalian MAP kinases. This highlights a new biochemical activity of p21, which may provide the first evidence for a non- enzymatic inhibitory protein for SAPK. We suggest that p21, by inhibiting SAPK, may participate in regulating signalling cascades that are activated by cellular stresses such as DNA damage.

Original languageEnglish
Pages (from-to)804-807
Number of pages4
JournalNature
Volume381
Issue number6585
DOIs
Publication statusPublished - 1996

ASJC Scopus subject areas

  • General

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