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Dynein motion switches from diffusive to directed upon cortical anchoring.

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TLDR
It is observed that dyneins on the microtubule move either in a diffusive or directed manner, with the switch from diffusion to directed movement occurring upon binding of dynein to cortical anchors.
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This article is published in Cell.The article was published on 2013-06-20 and is currently open access. It has received 89 citations till now. The article focuses on the topics: Cytoplasmic Dyneins & Dynactin.

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Journal ArticleDOI

Functions and mechanics of dynein motor proteins

TL;DR: A model for the mechanochemical cycle of dynein is emerging, in which nucleotide-driven flexing motions within the AAA+ ring of Dynein alter the affinity of its microtubule-binding stalk and reshape its mechanical element to generate movement.
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Probing the Stochastic, Motor-Driven Properties of the Cytoplasm Using Force Spectrum Microscopy

TL;DR: This work introduces force-spectrum-microscopy (FSM) to directly quantify random forces within the cytoplasm of cells and thereby probe stochastic motor activity, and shows that force fluctuations substantially enhance intracellular movement of small and large components.
Journal ArticleDOI

Mechanism and regulation of cytoplasmic dynein.

TL;DR: This work provides a synthesis of recent data to describe the current model of dynein's mechanochemical cycle and discusses regulators of Dynein, with particular focus on those that directly interact with the motor to modulate its recruitment to microtubules, initiate cargo transport, or activate minus-end-directed motility.
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Autoinhibition and cooperative activation mechanisms of cytoplasmic dynein

TL;DR: A mechanism of autonomous on–off switching of cargo transport is proposed, in which single dynein molecules in the cell are autoinhibited through intramolecular head–head stacking and become active when they assemble as a team on a cargo.
Journal ArticleDOI

Local Cytoskeletal and Organelle Interactions Impact Molecular-Motor-Driven Early Endosomal Trafficking

TL;DR: The results indicate that the crowded cellular environment significantly impacts the motor-driven motility of organelles and suggest that endosomal membrane tension is high during directed run termination.
References
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Heterologous modules for efficient and versatile PCR-based gene targeting in Schizosaccharomyces pombe

TL;DR: A straightforward PCR‐based approach to the deletion, tagging, and overexpression of genes in their normal chromosomal locations in the fission yeast Schizosaccharomyces pombe, and a series of plasmids containing the kanMX6 module, which allows selection of G418‐resistant cells and thus provides a new heterologous marker for use in S. pom be.
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The molecular structure of green fluorescent protein

TL;DR: The crystal structure of recombinant wild-type green fluorescent protein (GFP) has been solved to a resolution of 1.9 Å by multiwavelength anomalous dispersion phasing methods and the identification of the dimer contacts may allow mutagenic control of the state of assembly of the protein.
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Highly inclined thin illumination enables clear single-molecule imaging in cells.

TL;DR: A simple illumination method of fluorescence microscopy for molecular imaging yielded clear single-molecule images and three-dimensional images using cultured mammalian cells, enabling one to visualize and quantify molecular dynamics, interactions and kinetics in cells for molecular systems biology.
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Protein mobility in the cytoplasm of Escherichia coli

TL;DR: Noninvasive measurements of the apparent diffusion coefficient of green fluorescent protein (GFP) in the cytoplasm of Escherichia coli have implications for the understanding of intracellular biochemical networks.
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Single-Molecule Analysis of Dynein Processivity and Stepping Behavior

TL;DR: The results suggest that cytoplasmic dynein moves processively through the coordination of its two motor domains, but its variable step size and direction suggest a considerable diffusional component to its step, which differs from Kinesin-1 and is more akin to myosin VI.
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