Journal
PROTEOMICS
Volume 6, Issue 1, Pages 123-130Publisher
WILEY
DOI: 10.1002/pmic.200500068
Keywords
interaction; orphan receptor; phosphorylation; p300; CBP-associated factor
Funding
- NIDA NIH HHS [DA 11190, DA 11806, K02 DA 13926, P50 DA011806] Funding Source: Medline
- NIDDK NIH HHS [DK 60521, DK 54733] Funding Source: Medline
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [R01DK054733, R01DK060521] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE ON DRUG ABUSE [P50DA011806, K02DA013926, R01DA011190] Funding Source: NIH RePORTER
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In a previous report we demonstrated protein kinase C (PKC)-mediated phosphorylation of the ligand-binding domain (LBD) of orphan nuclear receptor TR2. In this report, we provide the evidence of PKC-mediated phosphorylation of the DNA-binding domain (DBD) of TR2. Two PKC target sites were predicted within the DBD, at Ser-170 and Ser-185, but only Ser-185 was confirmed by MS. Phosphorylation of DBD facilitated DNA binding of the TR2 receptor and its recruiting of coactivator p300/CBP-associated factor (P/CAF). Ser-185 was required for DNA binding, whereas both Ser-170 and Ser-185 were necessary for receptor interaction with P/CAF. The P/CAF-interacting domain of TR2 was located in its DBD. Adouble mutant (Ser-170 and Ser-185) of TR2 significantly lowered the activation of its target gene RAR beta 2. This study provides the first evidence for ligand-independent activation of TR2 orphan receptor through PTM at the DBD, which enhanced its DNA-binding ability and interaction with coactivator P/CAF.
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