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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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Characterization of human septin interactions

Kirstin Sandrock1 / Ingrid Bartsch1 / Susanne Bläser1 / Anja Busse1 / Eileen Busse1 / 1

1Department of Pediatrics and Adolescent Medicine, University Medical Center Freiburg, D-79106 Freiburg, Germany

Corresponding author

Citation Information: Biological Chemistry. Volume 392, Issue 8-9, Pages 751–761, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2011.081, August 2011

Publication History:


Septins constitute a group of GTP binding proteins that assemble into homo- and hetero-oligomeric complexes and filaments. These higher order septin structures are thought to function like scaffolds and/or diffusion barriers serving as spatial localizers for many proteins with key roles in cell polarity and cell cycle progression. In this study, we extensively characterized septin interaction partners using yeast two-hybrid and three-hybrid systems in addition to precipitation analyses in platelets. As a result, we identified human hetero-trimeric septin complexes on a large scale, which had been only postulated in the past. In addition, we illustrated roles of SEPT9 that might contribute to hetero-trimeric septin complex formation. SEPT9 can substitute for septins of the SEPT2 group and partially for SEPT7. Mutagenic analyses revealed that mutation of a potential phosphorylation site in SEPT7 (Y318) regulates the interaction with other septins. We identified several septin-septin interactions in platelets suggesting a regulatory role of diverse septin complexes in platelet function.

Keywords: GTP binding domain; hetero-trimeric complex; phosphorylation; platelets; yeast three-hybrid system

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