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Biochem Biophys Res Commun. 1998 Nov 18;252(2):524-8.

Intracellular association of FGF-2 with the ribosomal protein L6/TAXREB107.

Author information

  • 1Department 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.

Copyright 1998 Academic Press.

PMID:
9826564
[PubMed - indexed for MEDLINE]
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