Hy. He et al., HSP70 and heat shock factor 1 cooperate to repress Ras-induced transcriptional activation of the c-fos gene, CELL STR CH, 5(5), 2000, pp. 406-411
Heat shock protein 70 (HSP70) is a molecular chaperone involved in protein
folding and resistance to the deleterious effects of stress. Here we show t
hat HSP70 suppresses transcription of c-fos, an early response gene that is
a key component of the ubiquitous AP-1 transcription factor complex. HSP70
repressed Ras-induced c-fos transcription only in the presence of function
al heat shock factor1 (HSF1). This suggests that HSP70 functions as a corep
ressor with HSF1 to inhibit c-fos gene transcription. Therefore, besides it
s known function in the stress response, HSP70 also has the property of a c
orepressor and combines with HSF1 to antagonize Fos expression and may thus
impact multiple aspects of cell regulation.