Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 22, Issue 22, Pages 4279-4287Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E11-02-0112
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Funding
- Deutsche Forschungsgemeinschaft [SFB 863]
- Friedrich-Baur-Stiftung
- Elite Network of Bavaria
- Center for Integrated Protein Science
- TUM Institute of Advanced Study
- German Excellence Initiative
- German Research Society (DFG) [SFB863 Teilprojekt A9]
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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, Forster 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.
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