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© Research
Publication : The EMBO journal

Stress-activated protein kinases are negatively regulated by cell density

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The EMBO journal - 01 Oct 1998

Lallemand D, Ham J, Garbay S, Bakiri L, Traincard F, Jeannequin O, Pfarr CM, Yaniv M

Link to Pubmed [PMID] – 9755162

EMBO J. 1998 Oct;17(19):5615-26

Stimulation by UV irradiation, TNFalpha, as well as PDGF or EGF activates the JNK/SAPK signalling pathway in mouse fibroblasts. This results in the phosphorylation of the N-terminal domain of c-Jun, increasing its transactivation potency. Using an antibody that specifically recognizes c-Jun phosphorylated at Ser63, we show that culture confluency drastically inhibited c-Jun N-terminal phosphorylation due to the inhibition of the JNK/SAPK pathway. Transfection experiments demonstrate that the inhibition occurs at the same level as, or upstream of, the small G-proteins cdc42 and Rac1. In contrast, the classical MAPK pathway was insensitive to confluency. The inhibition of JNK/SAPK activation depended on the integrity of the actin microfilament network. These results were confirmed and extended in monolayer wounding experiments. After PDGF, EGF or UV stimulation, c-Jun was predominantly phosphorylated in cells bordering the wound, which are the cells that move to occupy the wounded area. Thus, modulation of the stress-dependent signal cascade by confluency will restrict c-Jun N-terminal phosphorylation in response to mitogenic or chemotactic agents to cells that border a wounded area.

http://www.ncbi.nlm.nih.gov/pubmed/9755162