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Papers In Press, published online ahead of print April 18, 2002
Department of Biochemistry, Institute for Cancer Research, Oslo 0310
Corresponding Author: sjur.olsnes{at}labmed.uio.no
With the aim of identifying new intracellular binding partners for acidic fibroblast growth factor (aFGF), proteins from U2OS human osteosarcoma cells were adsorbed to immobilised aFGF. One of the adsorbed proteins is a member of the leucine-rich repeat protein family termed ribosome-binding protein p34 (p34). This protein has previously been localised to ER-membranes and is thought to span the membrane with the N-terminus on the cytosolic side. Confocal microscopy on cells transfected with myc-p34 confirmed the ER-localisation and Northern blotting determined p34 mRNA to be present in a multitude of different tissues. Cross-linking experiments indicated that the protein is present in the cell as a dimer. In vitro translated p34 was found to interact with MBP-aFGF through its cytosolic coiled coil domain. The interaction between aFGF and p34 was further characterised by surface plasmon resonance giving a KD of (1.4 ± 0.3)* 10-6 M. Even though p34 interacted with mitogenic aFGF, it bound poorly to the non-mitogenic aFGF(K132E) mutant, indicating a possible involvement of p34 in intracellular signalling by aFGF.
J. Biol. Chem, 10.1074/jbc.M112193200
Submitted on December 20, 2001
Revised on March 26, 2002
Accepted on April 18, 2002
Identification of ribosome-binding protein p34 as an intracellular protein that binds acidic fibroblast growth factor
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