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  • Title: Cargo binding and regulatory sites in the tail of fungal conventional kinesin.
    Author: Seiler S, Kirchner J, Horn C, Kallipolitou A, Woehlke G, Schliwa M.
    Journal: Nat Cell Biol; 2000 Jun; 2(6):333-8. PubMed ID: 10854323.
    Abstract:
    Here, using a quantitative in vivo assay, we map three regions in the carboxy terminus of conventional kinesin that are involved in cargo association, folding and regulation, respectively. Using C-terminal and internal deletions, point mutations, localization studies, and an engineered 'minimal' kinesin, we identify five heptads of a coiled-coil domain in the kinesin tail that are necessary and sufficient for cargo association. Mutational analysis and in vitro ATPase assays highlight a conserved motif in the globular tail that is involved in regulation of the motor domain; a region preceding this motif participates in folding. Although these sites are spatially and functionally distinct, they probably cooperate during activation of the motor for cargo transport.
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