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J. Biol. Chem., Vol. 276, Issue 22, 18925-18933, June 1, 2001
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From the In this study we demonstrate a direct interaction
between a cytosolic fibroblast growth factor family member and a sodium channel. A yeast two-hybrid screen for proteins that associate with the
cytoplasmic domains of the tetrodotoxin-resistant sodium channel
rNav1.9a (NaN) led to the identification of
fibroblast growth factor homologous factor 1B (FHF1B), a member of the
fibroblast growth factor family, as an interacting partner of
rNav1.9a. FHF1B selectively interacts with the C-terminal
region but not the other four intracellular segments of
rNav1.9a. FHF1B binds directly to the C-terminal
polypeptide of rNav1.9a both in vitro and in mammalian cell lines. The N-terminal 5-77 amino acid residues of FHF1B
are essential for binding to rNav1.9a. FHF1B did not interact with C termini of two other sodium channels
hNav1.7a (hNaNE) and rNav1.8a (SNS), which
share 50% similarity to the C-terminal polypeptide of
rNav1.9a. FHF1B is the first growth factor found to bind
specifically to a sodium channel. Although the functional significance
of this interaction is not clear, FHF1B may affect the
rNav1.9a channel directly or by recruiting other proteins
to the channel complex. Alternatively, it is possible that
rNav1.9a may help deliver this factor to the cell membrane, where it exerts its function.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF348446.
Fibroblast Growth Factor Homologous Factor 1B Binds to the C
Terminus of the Tetrodotoxin-resistant Sodium Channel
rNav1.9a (NaN)*
§¶
,§¶**, and§¶
Department of Neurology and
§ Paralyzed Veterans of America/Eastern Paralyzed Veterans
Association Neuroscience Research Center, Yale University School
of Medicine, New Haven, Connecticut 06510 and the ¶ Rehabilitation
Research Center, Veterans Affairs Medical Center,
West Haven, Connecticut 06516
*
This work was supported in part by grants from the National
Multiple Sclerosis Society and the Rehabilitation Research and Development Service and Medical Research Services, Department of
Veterans Affairs and by gifts from the Paralyzed Veterans of America
and Eastern Paralyzed Veterans Association.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by a Spinal Cord Research Fellowship from the
Eastern Paralyzed Veterans Association.
**
To whom correspondence should be addressed: PVA/EPVA Neuroscience
Research Center, Yale University School of Medicine, 127A, Bldg. 34, 950 Campbell Ave., West Haven, CT 06516. Tel.: 203-937-3802; Fax:
203-937-3801; E-mail: sulayman.dib-hajj@yale.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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