Cytoplasmic dynein is a motor protein complex involved in microtubule-based cargo movement. Previous biochemical evidence suggests that dynein light chain subunits also exist outside the dynein complex. Here we show that the dynein light chain rp3 is present in both the cytoplasm and the nucleus. Nuclear rp3 binds to and assembles with the transcription factor SATB1 at nuclear matrix-associated...

Cytoplasmic dynein is a microtubule motor involved in cargo transport, nuclear migration and cell division. Despite structural conservation of the dynein motor domain from yeast to higher eukaryotes, the extensively studied S. cerevisiae dynein behaves distinctly from mammalian dyneins, which produce far less force and travel over shorter distances. However, isolated reports of yeast-like force...

Chromosome movement during meiosis is crucial for homologous pairing and meiotic recombination. During meiotic prophase in fission yeast, rapid nuclear migration is dependent on cytoplasmic dynein, which is anchored to the cell cortex and pulls microtubules, thereby driving nuclear migration. However, the precise mechanisms underlying dynein localization and activation remain unclear. Here, we ...

The working mechanism of the eukaryotic flagellar axoneme remains one of nature's most enduring puzzles. The basic mechanical operation of the axoneme is now a story that is fairly complete; however, the mechanism for coordinating the action of the dynein motor proteins to produce beating is still controversial. Although a full grasp of the dynein switching mechanism remains elusive, recent exp...

Cytoplasmic dynein is a ubiquitously expressed microtubule motor involved in vesicle transport, mitosis, nuclear migration, and spindle orientation. In the filamentous fungus Aspergillus nidulans, inactivation of cytoplasmic dynein, although not lethal, severely impairs nuclear migration. The role of dynein in mitosis and vesicle transport in this organism is unclear. To investigate the complet...

Sequence comparisons and structural analyses show that the dynein heavy chain motor subunit is related to the AAA family of chaperone-like ATPases. The core structure of the dynein motor unit derives from the assembly of six AAA domains into a hexameric ring. In dynein, the first four AAA domains contain consensus nucleotide triphosphate-binding motifs, or P-loops. The recent structural models ...

BACKGROUND Cytoplasmic dynein complex is a large multi-subunit microtubule (MT)-associated molecular motor involved in various cellular functions including organelle positioning, vesicle transport and cell division. However, regulatory mechanism of the cell-cycle dependent distribution of dynein has not fully been understood. METHODOLOGY/PRINCIPAL FINDINGS Here we report live-cell imaging of ...

Two microtubule-stimulated ATPases, cytoplasmic dynein, and kinesin, are believed to be responsible for the intracellular movement of membrane-bound organelles in opposite directions along microtubules. An unresolved component of this model is the mechanism by which cells regulate these two motors to direct various membrane-bound organelles to their proper locations. To determine if phosphoryla...

The cytoplasmic dynein-1 (dynein) motor plays a central role in microtubule organisation and cargo transport. These functions are spatially regulated by association of dynein and its accessory complex dynactin with dynamic microtubule plus ends. Here, we elucidate in vitro the roles of dynactin, end-binding protein-1 (EB1) and Lissencephaly-1 (LIS1) in the interaction of end tracking and minus ...

Cytoplasmic dynein purified by nucleotide dependent microtubule affinity has significant minus end-directed vesicle motor activity that decreases with each further purification step. Highly purified dynein causes membrane vesicles to bind but not move on microtubules. We exploited these observations to develop an assay for factors that, in combination with dynein, would permit minus end-directe...