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Isolation and Characterization of Ret Finger Protein
Author(s) -
Tang Catherine,
Cheng Xiwen,
Kao HungYing
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a287-c
Subject(s) - corepressor , fusion protein , biology , zinc finger , microbiology and biotechnology , nuclear receptor , transcription factor , chemistry , genetics , gene , recombinant dna
The Ret finger protein (RFP) belongs to the tripartite motif family, which is characterized by a RING finger, a B‐Box, and a coiled‐coil domain (RBCC), also known as the B30.2‐like domain. RFP has been shown to promote apoptosis through a mechanism that is independent of mitochondrial events. RFP was also shown to bind to promyelocytic leukemia protein (PML), which is another member of the RBCC family and acts as a tumor suppressor by its ability to control apoptosis. The role of RFP in cell control, however, has not been well‐studied and remains unclear. We focus on the role of RFP in mediating transcriptional repression. Retinoid acid receptors have been shown to repress transcription in the absence of ligand. This repression is achieved by a corepressor complex recruited by corepressor SMRT (silencing mediator of retinoid and thyroid hormone receptor). Immunoprecipitation studies indicate protein‐protein interactions between RFP and GPS2 (G‐protein pathway suppressor 2), a subunit of SMRT. We have generated a GST‐fusion construct, GST‐RFP, which was also expressed and purified. The purified GST‐RFP fusion protein was sent to generate an antibody. Development of the RFP antibody can allow us to determine the specific interactions of RFP and its partners. Taken altogether, we suggest that RFP is involved in the SMRT‐recruited corepressor complex by associating directly with GPS2.