Cytoplasmic dynein, the 1.2 MDa motor driving minus-end-directed motility, has been
reported to move processively along microtubules, but its mechanism of motility remains
poorly understood. Here, using S. cerevisiae to produce recombinant dynein with a …

▪ Abstract The existence and function of actin in the nucleus has been hotly debated for forty
years. Recently, β-actin was found to be a component of mammalian SWI/SNF-like BAF
chromatin remodeling complexes and still more recently other SWI/SNF-related chromatin …

Cytoplasmic dynein is a minus-end-directed microtubule motor whose mechanism of
movement remains poorly understood. Here, we use optical tweezers to examine the force-
dependent stepping behavior of yeast cytoplasmic dynein. We find that dynein primarily …

The myosin family of actin-based molecular motors consists of 15 known classes that are
structurally distinct based on comparisons of the primary structure of the motor domains of
the known myosin heavy chain genes [1^ 3]. Information regarding the function and/or …

Cytoplasmic dynein and kinesin-1 are microtubule-based motors with opposite polarity that
transport a wide variety of cargo in eukaryotic cells. Many cellular cargos demonstrate
bidirectional movement due to the presence of ensembles of dynein and kinesin, but are …

Dynein at the cortex contributes to microtubule-based positioning processes such as spindle
positioning during embryonic cell division and centrosome positioning during fibroblast
migration. To investigate how cortical dynein interacts with microtubule ends to generate …

Processivity, the ability of single molecules to move continuously along a track, is a
fundamental requirement of cargo-transporting molecular motors. Here, we investigate how
cytoplasmic dynein, a homodimeric, microtubule-based motor, achieves processive motion …

The lissencephaly protein Lis1 has been reported to regulate the mechanical behavior of
cytoplasmic dynein, the primary minus-end-directed microtubule motor. However, the
regulatory mechanism remains poorly understood. Here, we address this issue using …

The microtubule-binding domain (MTBD) of dynein is separated from the AAA (A TPase with
a ny other a ctivity) core of the motor by an∼ 15-nm stalk that is predicted to consist of an
antiparallel coiled coil. However, the structure of this coiled coil and the mechanism it uses …

The motor properties of the two yeast class V myosins, Myo2p and Myo4p, were examined
using in vitro motility assays. Both myosins are active motors with maximum velocities of 4.5
μm/s for Myo2p and 1.1 μm/s for Myo4p. Myo2p motility is Ca 2+ insensitive. Both myosins …