Structural insight into filament formation by mammalian septins

Minhajuddin Sirajuddin, Marian Farkasovsky, Florian Hauer, Dorothee Kühlmann, Ian G. Macara, Michael Weyand, Holger Stark and Alfred Wittinghofer ()
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Minhajuddin Sirajuddin: Max-Planck-Institut für molekulare Physiologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany
Marian Farkasovsky: Max-Planck-Institut für molekulare Physiologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany
Florian Hauer: Max-Planck-Institut für Biophysikaische Chemie, Am Fassberg 11, 37077 Goettingen, Germany
Dorothee Kühlmann: Max-Planck-Institut für molekulare Physiologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany
Ian G. Macara: Center for Cell Signaling, University of Virginia School of Medicine, Charlottesville, Virginia 22908-0577, USA
Michael Weyand: Max-Planck-Institut für molekulare Physiologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany
Holger Stark: Max-Planck-Institut für Biophysikaische Chemie, Am Fassberg 11, 37077 Goettingen, Germany
Alfred Wittinghofer: Max-Planck-Institut für molekulare Physiologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany

Nature, 2007, vol. 449, issue 7160, 311-315

Abstract: Abstract Septins are GTP-binding proteins that assemble into homo- and hetero-oligomers and filaments. Although they have key roles in various cellular processes, little is known concerning the structure of septin subunits or the organization and polarity of septin complexes. Here we present the structures of the human SEPT2 G domain and the heterotrimeric human SEPT2–SEPT6–SEPT7 complex. The structures reveal a universal bipolar polymer building block, composed of an extended G domain, which forms oligomers and filaments by conserved interactions between adjacent nucleotide-binding sites and/or the amino- and carboxy-terminal extensions. Unexpectedly, X-ray crystallography and electron microscopy showed that the predicted coiled coils are not involved in or required for complex and/or filament formation. The asymmetrical heterotrimers associate head-to-head to form a hexameric unit that is nonpolarized along the filament axis but is rotationally asymmetrical. The architecture of septin filaments differs fundamentally from that of other cytoskeletal structures.

Date: 2007
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DOI: 10.1038/nature06052

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