Kazrin, a protein widely expressed in vertebrates whose depletion causes defects in cell adhesion and migration, is recruited to early endosomes and promotes dynein/dynactin-dependent traffic of endocytosed cargo to the recycling endosomes.

Actr10, a dynactin pointed end protein, is essential for mitochondrial interaction with the dynein-dynactin retrograde motor and subsequent transport.

Dynactin acts as an anti-catastrophe factor that extends microtubule growth; posteriorly elucidating a new essential step in oskar mRNA localisation and providing a novel mechanism by which motor-dependent transport can amplify the polarity of MT networks.

Computational modeling of a dynamin-constricted membrane neck can rank proposed shape changes of the helical scaffold in terms of their fission aptitude and elucidate the associated pathways.

A new approach using combination of electron microscopy (EM) and high-speed atomic force microscopy (HS-AFM) clearly demonstrates dynamics of dynamin-amphiphysin complexes during membrane constriction and fission suggesting a novel 'clusterase' model of the dynamin-mediated membrane fission.

The recycling of transmitter vesicles at synapses shows calcium-dependent regulation that depends on the phosphorylation status of an enzyme called dynamin.

At mitosis, NuMA recruits dynein-dynactin to microtubule minus-ends, enabling robust microtubule clustering and the emergence of spindle poles.

The BAR protein endophilin spaces out turns of the dynamin helix, blocking its active conformational change and membrane fission.

Uncoupling of dynamin polymerization and GTPase activity can be induced with dynamin, which allows in vivo visualization of its activity at endocytic pits.

A single amino acid residue is critical for cardiolipin interaction specificity and nuclear membrane recruitment of a dynamin-related protein.