Cell-Cycle Dependent Tyrosine Phosphorylation on Mortalin Regulates Its Interaction with Fibroblast Growth Factor-1

We previously reported that endogenously expressed, intracellularly localized fibroblast growth factor (FGF)-1 interacts with mortalin. Here we report that FGF-1 added to the culture medium of quiescent BALB/c3T3 cells is taken up by the cells and interacts with mortalin in the cells in a regulated...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2001-02, Vol.280 (4), p.1203-1209
Main Authors: Mizukoshi, Eiichi, Suzuki, Masashi, Misono, Tomoko, Loupatov, Alexei, Munekata, Eisuke, Kaul, Sunil C., Wadhwa, Renu, Imamura, Toru
Format: Article
Language:English
Subjects:
3T3 Cells
Animals
Carrier Proteins
Cell Cycle
Cell Line
DNA - metabolism
Electrophoresis, Polyacrylamide Gel
FGF
fibroblast growth factor
Fibroblast Growth Factor 1 - metabolism
Fibroblast Growth Factor 1 - pharmacokinetics
GRP75
HSP70 Heat-Shock Proteins - metabolism
Immunoblotting
interaction
internalization
Mice
Mice, Inbred BALB C
Microscopy, Fluorescence
mortalin
Phosphorylation
Precipitin Tests
Protein Binding
Time Factors
Tyrosine - metabolism
tyrosine phosphorylation
Vanadates - pharmacology
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Summary:We previously reported that endogenously expressed, intracellularly localized fibroblast growth factor (FGF)-1 interacts with mortalin. Here we report that FGF-1 added to the culture medium of quiescent BALB/c3T3 cells is taken up by the cells and interacts with mortalin in the cells in a regulated manner. Although both the internalized FGF-1 and mortalin were present at high levels throughout the FGF-1-initiated cell cycle, their interaction became apparent only in late G1 phase. Interestingly, mortalin was preferentially tyrosine phosphorylated at the same time, and when its normally weak phosphorylation in early G1 phase was augmented by treating the cells with vanadate, a strong interaction between mortalin and FGF-1 was established. Conversely, when phosphorylated mortalin was treated with tyrosine phosphatase, its interaction with FGF-1 was abrogated. These results indicate that FGF-1 taken up by cells preferentially interacts with mortalin in late G1 phase of the cell cycle, and that tyrosine phosphorylation of mortalin regulates this interaction.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.2001.4225