The BioGRID | PUBLICATION VIEW

	Biochem. Biophys. Res. Commun. Nov (1998); 252(2):524-8
Intracellular association of FGF-2 with the ribosomal protein L6/TAXREB107.
Shen B, Arese M, Gualandris A, Rifkin DB
Department of Cell Biology, Kaplan Cancer Center, and the Raymond and Beverly Sackler Foundation Laboratory, New York University Medical Center, New York, New York, 10016, USA. shenb01@mcrcr6.med.nyu.edu
Abstract: By using the yeast two-hybrid system, we identified the ribosomal protein L6/TAXREB107 as an intracellular partner for FGF-2. L6/TAXREB107 also mediates the DNA binding of the HTLV-1 transactivator Tax. In vitro binding experiments indicated that both the high-molecular-weight forms (HMW) and the 18-kDa form of FGF-2 bind to L6/TAXREB107. Deletion analysis suggested that L6/TAXREB107 has two binding sites for HMW FGF-2 and one binding site for 18-kDa FGF-2, implying that the unique N-terminal extension of the HMW FGF-2 is one of the binding domains for L6/TAXREB107. Transfection assays showed that high expression of either HMW or 18 kDa FGF-2 stimulates Tax-mediated transactivation in NIH 3T3 cells. This result suggests a possible role of FGF-2 in Tax-mediated HTLV-1 transformation as well as FGF-2 binding to ribosomes and/or their precursors.
[PUBMED: 9826564]