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Role of the ATFa/JNK2 complex in Jun activation
F De Graeve1, A Bahr, K T Sabapathy
1Institut de Génétique et de Biologie Moléculaire et Cellulaire, INSERM/CNRS/ULP, Illkirch, CU de Strasbourg, France.
Oncogene
|June 22, 1999
Summary
ATFa proteins are versatile transcription factors. Specific threonine residues and a metal-binding domain are crucial for ATFa
Area of Science:
- Molecular Biology
- Transcription Factor Research
- Cell Signaling
Background:
- ATFa proteins belong to the CREB/ATF family of transcription factors.
- Previous work showed ATFa interacts with adenovirus E1a and heterodimerizes with Jun/Fos proteins.
- ATFa's N-terminal domain binds Jun N-terminal kinase-2 (JNK2).
Purpose of the Study:
- To identify sequence requirements in the ATFa N-terminal activation domain.
- To investigate the role of specific threonine residues (Thr51, Thr53) and the metal-binding domain in transcriptional activation.
- To elucidate the interaction between ATFa, JNK2, and JunD.
Main Methods:
- Analysis of ATFa protein sequence requirements.
- In vivo studies of kinase activity and protein-protein interactions.
- Investigation of JNK2-mediated phosphorylation of ATFa partners.
Main Results:
- Specific threonine residues (Thr51, Thr53) and the metal-binding domain are essential for ATFa's transcriptional activation.
- The ATFa N-terminal domain acts as a docking site for JNK2, not a direct substrate.
- JunD is phosphorylated by JNK2 via the ATFa-JNK2 complex.
Conclusions:
- The study defines critical residues for ATFa transcriptional function.
- ATFa's role in JNK2-mediated signaling is clarified, highlighting its function as a scaffold.
- Findings provide insights into the regulation of transcription factors by kinase-docking mechanisms.