Fibroblast growth factor-2(23) binds directly to the survival of motoneuron protein and is associated with small nuclear RNAs

The Biochemical Journal
Peter ClausClaudia Grothe

Abstract

The SMN (survival of motoneuron) protein is mutated in patients with the neurodegenerative disease spinal muscular atrophy. We have shown previously that a high-molecular-mass isoform of FGF (fibroblast growth factor) 2 (FGF-2(23)) is in a complex with SMN [Claus, Doring, Gringel, Muller-Ostermeyer, Fuhlrott, Kraft and Grothe (2003) J. Biol. Chem. 278, 479-485]. FGF-2 is a neurotrophic factor for motoneurons, and is known not only as a classical extracellular growth factor, but also as a nuclear protein. In the present study, we demonstrate that SMN binds to the arginine-rich N-terminus of FGF-2(23). In turn, FGF-2(23) interacts with amino acid residues 1-90 of the human SMN protein. This sequence displays nucleic-acid-binding capacity and overlaps partially with known binding sites for Gemin2/SIP1 (SMN-interacting protein 1) and p53. Finally, as a functional consequence of FGF-2(23) binding to SMN, FGF-2(23) is in a complex with the small nuclear RNAs U2 and U4. Since SMN functions as an assembly factor for snRNPs (small nuclear ribonucleoprotein particles), these results suggest binding of FGF-2(23) to snRNPs.

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Citations

Oct 14, 2008·Cellular and Molecular Life Sciences : CMLS·K ChlebovaP Krejci
Jul 9, 2009·Nature Reviews. Neuroscience·Arthur H M Burghes, Christine E Beattie
Jul 21, 2009·Proceedings of the National Academy of Sciences of the United States of America·Alexander-Francisco BrunsPeter Claus
Jun 13, 2013·Proceedings of the National Academy of Sciences of the United States of America·Anindya SenSpyros Artavanis-Tsakonas
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Dec 21, 2013·PloS One·Benjamin FörthmannPeter Claus
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Jan 22, 2013·Cellular and Molecular Life Sciences : CMLS·Benjamin FörthmannPeter Claus
Jan 2, 2015·Cellular and Molecular Life Sciences : CMLS·Benjamin FörthmannPeter Claus
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