Ligand‐induced transphosphorylation between different FGF receptors

Ligand‐induced transphosphorylation between different FGF receptors

Recent evidence shows that different fibroblast growth factors (FGF) bind with similar high affinities to two FGF receptors (FGFR) called flg and bek. In order to explore the mechanism of FGFR tyrosine autophosphorylation, we have generated cell lines which co‐express a kinase‐negative mutant of FGF...

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Bibliographic Details
Published in:The EMBO journal Vol. 10; no. 10; pp. 2849 - 2854
Main Authors: Bellot, F., Crumley, G., Kaplow, J.M., Schlessinger, J., Jaye, M., Dionne, C.A.
Format: Journal Article
Language:English
Published: London Nature Publishing Group 01-10-1991
Subjects:
autophosphorylation
Base Sequence
bek protein
Biological and medical sciences
Blotting, Western
Cell receptors
Cell structures and functions
comparison
Cross Reactions
Electrophoresis, Polyacrylamide Gel
fibroblast growth factor
Fibroblast Growth Factors - metabolism
Filaggrin Proteins
flg protein
Fundamental and applied biological sciences. Psychology
Genetic Vectors
Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors
Humans
Hygromycin B - metabolism
Ligands
Molecular and cellular biology
Molecular Sequence Data
Phosphorylation
Precipitin Tests
receptors
Receptors, Cell Surface - metabolism
Receptors, Fibroblast Growth Factor
Transfection
Tyrosine - metabolism
Tyrosine
Fibroblast growth factor
Phosphorylation
Radiolabelling
Enzyme
Rodentia
3T3-Cell line
Signal transduction
Vertebrata
Membrane receptor
Mammalia
Binding capacity
Mouse
Polypeptide
Scatchard plot
Protein-tyrosine kinase
Growth factor
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Summary:Recent evidence shows that different fibroblast growth factors (FGF) bind with similar high affinities to two FGF receptors (FGFR) called flg and bek. In order to explore the mechanism of FGFR tyrosine autophosphorylation, we have generated cell lines which co‐express a kinase‐negative mutant of FGFR and an active form of FGFR. The following transfected NIH 3T3 cells were generated: (i) cells which express a shorter truncated form of bek (two Ig domains) together with a kinase‐negative mutant of full length bek (bek K517A), (ii) cells which express wild‐type bek together with kinase‐negative flg (flg K514A) and (iii) cells co‐expressing wild‐type flg together with bek K517A. Immunoprecipitations with either bek‐or flg‐specific antisera followed by immunoblotting indicated that the double transfectants express the desired receptor species. The addition of acidic FGF (aFGF) to the various cell lines followed by immunoprecipitation with anti‐FGFR antibodies and immunoblotting with anti‐phosphotyrosine specific antibodies indicated that aFGF induces tyrosine phosphorylation of the kinase‐negative FGFR mutants. These results show that tyrosine autophosphorylation of the kinase‐negative FGFR is mediated by a transphosphorylation mechanism and that both homologous (bek‐‐‐‐bek) and heterologous (bek‐‐‐‐flg and flg‐‐‐‐bek) transphosphorylation occurs in living cells. Recent evidence shows that tyrosine autophosphorylation of receptors with tyrosine kinase activities is essential for mediating interactions with signaling molecules. Therefore, heterologous transphosphorylation could amplify the response of cells to various forms of FGFs and their cognate receptors.
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ISSN:0261-4189
1460-2075
DOI:10.1002/j.1460-2075.1991.tb07834.x