A role for polyproline motifs in the spinal muscular atrophy protein SMN - Profilins bind to and colocalize with SMN in nuclear gems

Giesemann T, Rathke-Hartlieb S, Rothkegel M, Bartsch JW, Buchmeier S, Jockusch BM, Jockusch H (1999)
JOURNAL OF BIOLOGICAL CHEMISTRY 274(53): 37908-37914.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Abstract / Bemerkung
Spinal muscular atrophy (SMA) is an autosomal, recessive disorder characterized by the loss of a-motoneurons in the spinal cord followed by atrophy of skeletal muscles. SMA-determining candidate genes, SMN1 and SMN2, have been identified on human chromosome 5q. The corresponding SMN protein is expressed ubiquitously. It is coded by seven exons and contains conspicuous proline-rich motifs in its COOH-terminal third (exons 4, 5, and 6). Such motifs are known to bind to profilins (PFNs), small proteins engaged in the control of actin dynamics. We tested whether profilins interact with SMN via its polyproline stretches. Using the yeast two-hybrid system we show that profilins bind to SMN and that this binding depends on its proline-rich motifs, These results were confirmed by coimmunoprecipitation and by in vitro binding studies. Two PFN isoforms, I and II, are known, of which II is characteristic for central nervous system tissue. me show by in situ hybridization that both PFNs are highly expressed in mouse spinal cord and that PFN II is expressed predominantly in neurons. In motoneurons, the primary target of neurodegeneration in SMA, profilins are highly concentrated and colocalize with SMN in the cytoplasm of the cell body and in nuclear gems. Likewise, SMN and PFN I colocalize in gems of HeLa cells. Although SMN interacts with both profilin isoforms, binding of PFN II was stronger than of PFN I in all assays employed. Because the SMN genes are expressed ubiquitously, our findings suggest that the interaction of PFN II with SMN may be involved in neuron-specific effects of SMN mutations.
Erscheinungsjahr
1999
Zeitschriftentitel
JOURNAL OF BIOLOGICAL CHEMISTRY
Band
274
Ausgabe
53
Seite(n)
37908-37914
ISSN
0021-9258
Page URI
https://pub.uni-bielefeld.de/record/1620928

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Giesemann T, Rathke-Hartlieb S, Rothkegel M, et al. A role for polyproline motifs in the spinal muscular atrophy protein SMN - Profilins bind to and colocalize with SMN in nuclear gems. JOURNAL OF BIOLOGICAL CHEMISTRY. 1999;274(53):37908-37914.
Giesemann, T., Rathke-Hartlieb, S., Rothkegel, M., Bartsch, J. W., Buchmeier, S., Jockusch, B. M., & Jockusch, H. (1999). A role for polyproline motifs in the spinal muscular atrophy protein SMN - Profilins bind to and colocalize with SMN in nuclear gems. JOURNAL OF BIOLOGICAL CHEMISTRY, 274(53), 37908-37914. doi:10.1074/jbc.274.53.37908
Giesemann, T., Rathke-Hartlieb, S., Rothkegel, M., Bartsch, J. W., Buchmeier, S., Jockusch, B. M., and Jockusch, H. (1999). A role for polyproline motifs in the spinal muscular atrophy protein SMN - Profilins bind to and colocalize with SMN in nuclear gems. JOURNAL OF BIOLOGICAL CHEMISTRY 274, 37908-37914.
Giesemann, T., et al., 1999. A role for polyproline motifs in the spinal muscular atrophy protein SMN - Profilins bind to and colocalize with SMN in nuclear gems. JOURNAL OF BIOLOGICAL CHEMISTRY, 274(53), p 37908-37914.
T. Giesemann, et al., “A role for polyproline motifs in the spinal muscular atrophy protein SMN - Profilins bind to and colocalize with SMN in nuclear gems”, JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 274, 1999, pp. 37908-37914.
Giesemann, T., Rathke-Hartlieb, S., Rothkegel, M., Bartsch, J.W., Buchmeier, S., Jockusch, B.M., Jockusch, H.: A role for polyproline motifs in the spinal muscular atrophy protein SMN - Profilins bind to and colocalize with SMN in nuclear gems. JOURNAL OF BIOLOGICAL CHEMISTRY. 274, 37908-37914 (1999).
Giesemann, T, Rathke-Hartlieb, S, Rothkegel, M, Bartsch, JW, Buchmeier, S, Jockusch, BM, and Jockusch, Harald. “A role for polyproline motifs in the spinal muscular atrophy protein SMN - Profilins bind to and colocalize with SMN in nuclear gems”. JOURNAL OF BIOLOGICAL CHEMISTRY 274.53 (1999): 37908-37914.

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