Motor protein function articles from across Nature Portfolio

Mutational analysis of the flagellar export apparatus protein FlhA suggests that the conserved GYXLI motif of FlhA, together with the cytoplasmic ATPase complex, strictly regulate the order of flagellar protein export.

This study presents an image processing-based stage height control and optical trap dithering technique to detect protein-protein interactions. It was used to show that the MT binding rate for KIF5B has a strong spatial and motor length dependence.

Inspired by biology, great progress has been made in creating artificial molecular motors. Here the authors report the synthesis and characterization of the Lawnmower, an autonomous, protein-based artificial molecular motor and show their design is capable of track-guided motion.

Here, the authors elucidate how sequential activities of opposite-polarity microtubule motors are coordinated on a cargo, by showing how the Tm1 protein inhibits kinesin-1 during delivery of oskar RNA into the Drosophila oocyte by dynein.

Myosin transduces chemical energy into mechanical work, but the mechanism remains unclear. In this work, the authors show that force-generation precedes product release and that a mutation in the active site alters the load dependence of product release.

Prestin, a motor protein, plays a major role in sound amplification. Using molecular dynamics simulations, the authors show that prestin causes membrane deformation patterns thereby achieving a particular lipid-mediated alignment in the membrane.

An experimental study of living cells suggests that single myosin molecules are capable of generating unusually large forces. The observation is supported by a theoretical model — and demonstrates the complexity of in vivo force generation.

Cytoplasmic dyneins transport cellular components from the periphery toward the center of the cell. By moving cargoes along microtubules, dyneins ensure proper cell division, regulate exchange of materials between organelles, and contribute to the internal organization of eukaryotic cells. Two recent studies show that, upon dimerization, cytoplasmic dyneins intrinsically adopt an autoinhibited configuration that can be relieved by other factors to precisely control motor activity and regulate dynein-based transport.

A curious peak in the distribution describing stochastic switching in bacterial motility had researchers confounded. But a careful study performed under varying mechanical conditions has now revealed that the breaking of detailed balance is to blame.

A nanopore used for sequencing gives a detailed view of how motor proteins behave on DNA.

The detailed mechanism by which the molecular motors kinesin and myosin travel along their respective protein tracks as they generate force during motile processes is still poorly understood. In a recent breakthrough, a crystal structure of kinesin in complex with tubulin illuminates the atomic-level details of a motor-track interaction, answering many questions yet leaving a number of mysteries unresolved.