ArticleCurrent biology : CB2026
Bicaudal D acts as a sensor to enable dynein-kinesin co-dependence.
Article in Current biology : CB, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Cellular cargoes bind both the minus-end-directed motor dynein and the plus-end-directed motor kinesin, enabling bidirectional motion along microtubules. The molecular mechanism to explain why knocking down one motor abolishes motion in both directions, called the "paradox of co-dependence," remains enigmatic. Here, we use a model system consisting of dynein/dynactin and kinesin bound to the activating adaptor BicD to investigate this phenomenon. We demonstrate that run lengths are significantly increased when a full-length motor and a tail construct of the opposing motor are simultaneously bound to the same BicD, caused by an enhanced recruitment of two active motors to the complex. Notably, a registry-shifted point mutant of BicD (BicD
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