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Published online January 2, 2007
doi:10.1083/jcb.200611082
The Journal of Cell Biology, Vol. 176, No. 1, 7-9
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Hackney
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 Jump-starting kinesin

David D. Hackney

Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA 15213

Correspondence to David D. Hackney: ddh{at}andrew.cmu.edu


Abstract
When it is not actively transporting cargo, conventional Kinesin-1 is present in the cytoplasm in a folded conformation that cannot interact effectively with microtubules (MTs). Two important and largely unexplored aspects of kinesin regulation are how it is converted to an active species when bound to cargo and the related issue of how kinesin discriminates among its many potential cargo molecules. Blasius et al. (see p. 11 of this issue) report that either binding of the cargo linker c-Jun N-terminal kinase–interacting protein 1 (JIP1) to the light chains (LCs) or binding of fasciculation and elongation protein {zeta}1 (FEZ1) to the heavy chains (HCs) is insufficient for activation but that activation occurs when both are present simultaneously. A related paper by Cai et al. (see p. 51 of this issue) provides structural insight into the conformation of the folded state in the cell obtained by fluorescence resonance energy transfer analysis.


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