Fibroblast growth factor-1 interacts with the glucose-regulated protein GRP75/mortalin

Fibroblast growth factor-1 (FGF-1), which lacks a signal peptide and is intracellularly localized as a result of endogenous expression or endocytosis, is thought to be involved in regulating cell growth and differentiation. In the study reported here, we purified proteins that bind intracellular FGF...

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Bibliographic Details
Published in:Biochemical journal 1999-10, Vol.343 Pt 2 (2), p.461-466
Main Authors: Mizukoshi, E, Suzuki, M, Loupatov, A, Uruno, T, Hayashi, H, Misono, T, Kaul, S C, Wadhwa, R, Imamura, T
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Binding Sites
Carrier Proteins
Cell Line
Chromatography, Affinity
Fibroblast Growth Factor 1
Fibroblast Growth Factor 2 - genetics
Fibroblast Growth Factor 2 - metabolism
HSP70 Heat-Shock Proteins - chemistry
HSP70 Heat-Shock Proteins - genetics
HSP70 Heat-Shock Proteins - metabolism
Humans
Immunohistochemistry
Membrane Proteins - chemistry
Membrane Proteins - genetics
Membrane Proteins - metabolism
Mice
Mitochondrial Proteins
Molecular Weight
Precipitin Tests
Protein Binding
Rats
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - metabolism
Sequence Analysis, Protein
Two-Hybrid System Techniques
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Summary:Fibroblast growth factor-1 (FGF-1), which lacks a signal peptide and is intracellularly localized as a result of endogenous expression or endocytosis, is thought to be involved in regulating cell growth and differentiation. In the study reported here, we purified proteins that bind intracellular FGF-1. Affinity adsorption was used to purify FGF-1-binding proteins from rat L6 cells expressing FGF-1. One of the isolated proteins was identified as the glucose-regulated protein GRP75/mortalin/PBP-74/mthsp70, a member of the hsp70 family of heat-shock proteins known to be involved in regulating glucose responses, antigen processing and cell mortality. The interaction of FGF-1 and GRP75/mortalin in vivo was confirmed by co-immunoprecipitation, immunohistochemical co-localization in Rat-1 fibroblasts and by using the yeast two-hybrid system. Moreover, a binding assay in vitro with the use of recombinant FGF-1 and mortalin demonstrated a direct physical interaction between the two proteins. These results reveal that GRP75/mortalin is an intracellular FGF-1-binding protein in cells and suggest that GRP75/mortalin is involved in the trafficking of and/or signalling by FGF-1.
ISSN:0264-6021
1470-8728
DOI:10.1042/0264-6021:3430461