Activating transcription factor 2.

ERIC LAU; PABLO LOPEZ BERGAMI; ZEEV RONAI

UCSD-Nature Molecule Pages

Nature Publishing Group

Año: 2010 p. 1 - 8

1476-4687

Activating transcription factor 2 (ATF2) is a basic leucine zipper-containing transcription factor and DNA damage response protein, member of the activating protein-1 (AP-1) transcription factor superfamily. Similar to its AP-1 family members, ATF2 is most often recognized for its role in mediating the activities of the stress-activated protein kinases Jun N-terminal kinases (JNK) and p38, as well as the mitogen-activated protein (MAP) kinase, extracellular signal-regulated kinase (ERK), whose phosphorylation of ATF2 is prerequisite for its transcriptional activities. Correspondingly, ATF2 is also implicated in a multitude of cellular processes, including apoptosis, proliferation and development. As a member of the AP-1 transcription factor family, ATF2 dimerizes with other bZIP proteins, following its phosphorylation by one of its above noted kinases. The nature of ATF2 transcriptional output largely depends on its dimerization partner, which varies depending on the cell/tissue type and stimuli. ATF2 protein contains two nuclear localization sequences and one nuclear export sequence, and, as expected, exhibits generally nuclear localization. However, ATF2 has also been observed to localize in the cytoplasmic compartment under various circumstances, suggesting potential cytoplasmic function that remains unknown. Although total loss of ATF2 results in postnatal lethality, conditional deletion of ATF2 results in numerous cellular and physiological defects. Notably, expression, localization and function of ATF2 are commonly deregulated in human diseases.