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Science 28 September 1990:
Vol. 249. no. 4976, pp. 1567 - 1570
DOI: 10.1126/science.1699274
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Articles

Science, Vol 249, Issue 4976, 1567-1570
Copyright © 1990 by American Association for the Advancement of Science

articles

Recovery of mitogenic activity of a growth factor mutant with a nuclear translocation sequence

T Imamura, K Engleka, X Zhan, Y Tokita, R Forough, D Roeder, A Jackson, JA Maier, T Hla, and T Maciag

Laboratory of Molecular Biology, Jerome H. Holland Laboratory for the Biomedical Sciences, American Red Cross, Rockville, MD 20855.

Heparin-binding growth factor-1 (HBGF-1) is an angiogenic polypeptide mitogen for mesoderm- and neuroectoderm-derived cells in vitro and remains biologically active after truncation of the amino-terminal domain (HBGF-1 alpha) of the HBGF-1 beta precursor. Polymerase chain reaction mutagenesis and prokaryotic expression systems were used to prepare a mutant of HBGF-1 alpha lacking a putative nuclear translocation sequence (amino acid residues 21 to 27; HBGF-1U). Although HBGF-1U retains its ability to bind to heparin, HBGF-1U fails to induce DNA synthesis and cell proliferation at concentrations sufficient to induce intracellular receptor-mediated tyrosine phosphorylation and c-fos expression. Attachment of the nuclear translocation sequence from yeast histone 2B at the amino terminus of HBGF-1U yields a chimeric polypeptide (HBGF-1U2) with mitogenic activity in vitro and indicates that nuclear translocation is important for this biological response.


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Role of the Nuclear Localization Sequence in Fibroblast Growth Factor-1-stimulated Mitogenic Pathways.
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The Neurotrophic Activity of Fibroblast Growth Factor 1 (FGF1) Depends on Endogenous FGF1 Expression and Is Independent of the Mitogen-activated Protein Kinase Cascade Pathway.
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Insulin-induced egr-1 Expression in Chinese Hamster Ovary Cells Is Insulin Receptor and Insulin Receptor Substrate-1 Phosphorylation-independent.
S. Harada, R. M. Smith, J. A. Smith, N. Shah, D.-Q. Hu, and L. Jarett (1995)
J. Biol. Chem. 270, 26632-26638
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Analysis of Putative Heparin-binding Domains of Fibroblast Growth Factor-1.
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J. Biol. Chem. 270, 17457-17467
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Inhibition of Nuclear Translocation of Transcription Factor NF-[IMAGE]B by a Synthetic Peptide Containing a Cell Membrane-permeable Motif and Nuclear Localization Sequence.
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E. Mesri, M Ono, R. Kreitman, M Klagsbrun, and I Pastan (1994)
J. Cell Sci. 107, 2599-2608
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Heparan sulfate proteoglycan and FGF receptor target basic FGF to different intracellular destinations.
J Reiland and A. Rapraeger (1993)
J. Cell Sci. 105, 1085-1093
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Characterization of the nuclear translocation of acidic fibroblast growth factor.
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Autocrine Secretion--10 Years Later.
M. B. Sporn and A. B. Roberts (1992)
Ann Intern Med 117, 408-414
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Hypotensive activity of fibroblast growth factor.
P Cuevas, F Carceller, S Ortega, M Zazo, I Nieto, and G Gimenez-Gallego (1991)
Science 254, 1208-1210
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Requirement of nuclear prolactin for interleukin-2--stimulated proliferation of T lymphocytes.
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Three-dimensional structures of acidic and basic fibroblast growth factors.
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   Abstract »    Full Text »    PDF »


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