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J Biol Chem, Vol. 275, Issue 2, 1176-1182, January 14, 2000

Phosphorylation Modulates the Function of the Vasoactive Intestinal Polypeptide Receptor Transcriptional Repressor Protein*

Lin PeiDagger

From the Division of Endocrinology and Metabolism, Cedars-Sinai Research Institute-UCLA School of Medicine, Los Angeles, California 90048

The transcriptional repressor for rat vasoactive intestinal polypeptide receptor 1 (VIPR-RP) is a recently isolated transcription factor. In this study, we have characterized the functional domains of VIPR-RP and the importance of phosphorylation on VIPR-RP function. Using various regions of VIPR-RP in gel mobility shift assays, we show that the amino acid sequences between positions 367 and 475 play an essential role for VIPR-RP DNA binding. Transient transfection of fusion constructs containing GAL4 DNA binding domain and different parts of VIPR-RP indicated that there are two separate transcriptional repression domains in VIPR-RP, located between amino acids 50 and 101 and between 469 and 527. We demonstrated that VIPR-RP is phosphorylated in vitro by casein kinase II on Ser-69/71 and Thr-110, and by cAMP-dependent kinase on Ser-245/361. Furthermore, by site-directed mutagenesis, we show that phosphorylation of the casein kinase II sites potentiates VIPR-RP transcriptional repression activity by enhancing its nuclear translocation, and that phosphorylation by cAMP-dependent kinase inhibits VIPR- RP transcriptional repression function without affecting its subcellular localization. These observations suggest that phosphorylation plays an important role in regulating VIPR-RP function.

* This work was supported by National Institutes of Health Grant DK-02346 and American Lung Association Grant RG-018-N.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Div. of Endocrinology and Metabolism, Cedars-Sinai Medical Center, 8700 Beverly Blvd., D3066, Los Angeles, CA 90048. Tel.: 310-423-7682; Fax: 815-352-6253; E-mail: pei@cshs.org.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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