title: How kinesin-2 forms a stalk.
abstract: The heterotrimeric structure of kinesin-2 makes it a unique member of the kinesin superfamily; however, molecular details of the oligomer formation are largely unknown. Here we demonstrate that heterodimerization of the two distinct motor domains KLP11 and KLP20 of Caenorhabditis elegans kinesin-2 requires a dimerization seed of merely two heptads at the C terminus of the stalk. This heterodimeric seed is sufficient to promote dimerization along the entire length of the stalk, as shown by circular dichroism spectroscopy, Förster resonance energy transfer analysis, and electron microscopy. In addition to explaining the formation of the kinesin-2 stalk, the seed sequence identified here bears great potential for generating specific heterodimerization in other protein biochemical applications.
authors.affiliation: Center for Integrated Protein Science Munich and Institute for Cell Biology, Ludwig-Maximilians-Universität, D-80336 Munich, Germany.
authors.forename: Marija
authors.initials: M
authors.lastname: Vukajlovic
authors.forename: Hendrik
authors.initials: H
authors.lastname: Dietz
authors.forename: Manfred
authors.initials: M
authors.lastname: Schliwa
authors.forename: Zeynep
authors.initials: Z
authors.lastname: Ökten
mesh_terms: D000818:Animals; D017173:Caenorhabditis elegans; D029742:Caenorhabditis elegans Proteins / Q000737:chemistry* / Q000378:metabolism*; D016547:Kinesins / Q000737:chemistry* / Q000378:metabolism*; D055503:Protein Multimerization
chemical_list: D029742:Caenorhabditis elegans Proteins; C093002:OSM-3 protein, C elegans; C074152:kinesin-II; D016547:Kinesins