RT info:eu-repo/semantics/article
T1 Effect of mutation of cytoplasmic receptor domain and of genistein on transport of acidic fibroblast growth factor into cells
A1 Muñoz Martínez, Raquel
A1 Klingenberg, Olav
A1 Wiedlocha, Antoni
A1 Rapak, Andrzej
A1 Falnes, Pål
A1 Olsnes, Sjur
K1 Receptor mutant
K1 Receptor mutante
K1 Genistein
K1 Genisteína
K1 Farnesylation
K1 Farnesilación
AB Acidic fibroblast growth factor (aFGF) binds to specific transmembrane receptors and is partly transported to a nuclear location. To study this transport we made a kinase-negative mutant of FGF receptor 4 as well as one where the major part of the cytoplasmic receptor domain was deleted, and expressed them in U2OSDr1 cells that lack functional FGF receptors. All receptors mediated endocytic uptake of aFGF. Translocation of the growth factor across cellular membranes was assayed using aFGF with a C-terminal CAAX-motif, which signals addition of a farnesyl group onto the protein once in the cytosol. CAAX-tagged aFGF was farnesylated when incubated with cells containing wild-type or kinase-negative receptors. It was not farnesylated in cells expressing the deleted receptor, or when the incubation was in the presence of genistein. aFGF incubated with cells transfected with wild-type or kinase-negative receptors, but not with the deleted receptor, was partly recovered from the nuclear fraction in the absence, but not in the presence of genistein. The data indicate that the cytoplasmic receptor domain, but not the active kinase, is required for transport of the growth factor into cells, and that genistein inhibits the process.
PB Springer Nature
SN 1476-5594
YR 1997
FD 1997
LK http://uvadoc.uva.es/handle/10324/41034
UL http://uvadoc.uva.es/handle/10324/41034
LA eng
NO Oncogene, 1997, vol. 15, n. 5. p. 525-536
NO Producción Científica
DS UVaDOC
RD 12-jul-2024