scholarly journals Role of AAA3 Domain in Allosteric Communication of Dynein Motor Proteins

ACS Omega ◽  
2019 ◽  
Vol 4 (26) ◽  
pp. 21921-21930 ◽  
Author(s):  
Mandira Dutta ◽  
Biman Jana
Keyword(s):  
Motor Proteins ◽  
Allosteric Communication ◽  
Dynein Motor

scholarly journals Functional interaction between dynein light chain and intermediate chain is required for mitotic spindle positioning

2011 ◽  
Vol 22 (15) ◽  
pp. 2690-2701 ◽  
Author(s):  
Melissa D. Stuchell-Brereton ◽  
Amanda Siglin ◽  
Jun Li ◽  
Jeffrey K. Moore ◽  
Shubbir Ahmed ◽  
...  
Keyword(s):  
Light Chain ◽  
Direct Evidence ◽  
Retrograde Transport ◽  
Cytoplasmic Dynein ◽  
Dynein Light Chain ◽  
Spindle Positioning ◽  
Dynein Motor ◽  
Intermediate Chains ◽  
Activator Complex

Cytoplasmic dynein is a large multisubunit complex involved in retrograde transport and the positioning of various organelles. Dynein light chain (LC) subunits are conserved across species; however, the molecular contribution of LCs to dynein function remains controversial. One model suggests that LCs act as cargo-binding scaffolds. Alternatively, LCs are proposed to stabilize the intermediate chains (ICs) of the dynein complex. To examine the role of LCs in dynein function, we used Saccharomyces cerevisiae, in which the sole function of dynein is to position the spindle during mitosis. We report that the LC8 homologue, Dyn2, localizes with the dynein complex at microtubule ends and interacts directly with the yeast IC, Pac11. We identify two Dyn2-binding sites in Pac11 that exert differential effects on Dyn2-binding and dynein function. Mutations disrupting Dyn2 elicit a partial loss-of-dynein phenotype and impair the recruitment of the dynein activator complex, dynactin. Together these results indicate that the dynein-based function of Dyn2 is via its interaction with the dynein IC and that this interaction is important for the interaction of dynein and dynactin. In addition, these data provide the first direct evidence that LC occupancy in the dynein motor complex is important for function.

scholarly journals Role of cytoskeletal motor proteins in viral infection

2012 ◽  
Vol 66 ◽  
pp. 810-817 ◽  
Author(s):  
Anna Słońska ◽  
Rafał Polowy ◽  
Anna Golke ◽  
Joanna Cymerys
Keyword(s):  
Viral Infection ◽  
Motor Proteins

scholarly journals Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7–RILP–p150Glued and late endosome positioning

2009 ◽  
Vol 185 (7) ◽  
pp. 1209-1225 ◽  
Author(s):  
Nuno Rocha ◽  
Coenraad Kuijl ◽  
Rik van der Kant ◽  
Lennert Janssen ◽  
Diane Houben ◽  
...  
Keyword(s):  
Motor Proteins ◽  
Oxysterol Binding Protein ◽  
Membrane Contact Sites ◽  
Cholesterol Levels ◽  
Dynein Motor ◽  
Late Endosomes ◽  
In Trans ◽  
Membrane Contact ◽  
Cholesterol Control ◽  
Niemann Pick

Late endosomes (LEs) have characteristic intracellular distributions determined by their interactions with various motor proteins. Motor proteins associated to the dynactin subunit p150Glued bind to LEs via the Rab7 effector Rab7-interacting lysosomal protein (RILP) in association with the oxysterol-binding protein ORP1L. We found that cholesterol levels in LEs are sensed by ORP1L and are lower in peripheral vesicles. Under low cholesterol conditions, ORP1L conformation induces the formation of endoplasmic reticulum (ER)–LE membrane contact sites. At these sites, the ER protein VAP (VAMP [vesicle-associated membrane protein]-associated ER protein) can interact in trans with the Rab7–RILP complex to remove p150Glued and associated motors. LEs then move to the microtubule plus end. Under high cholesterol conditions, as in Niemann-Pick type C disease, this process is prevented, and LEs accumulate at the microtubule minus end as the result of dynein motor activity. These data explain how the ER and cholesterol control the association of LEs with motor proteins and their positioning in cells.

scholarly journals The Role of Molecular Microtubule Motors and the Microtubule Cytoskeleton in Stress Granule Dynamics

2011 ◽  
Vol 2011 ◽  
pp. 1-9 ◽  
Author(s):  
Kristen M. Bartoli ◽  
Darryl L. Bishop ◽  
William S. Saunders
Keyword(s):  
Current Literature ◽  
Motor Proteins ◽  
Stress Granules ◽  
Stress Granule ◽  
Microtubule Cytoskeleton ◽  
Microtubule Motors ◽  
Key Players ◽  
Underlying Mechanisms ◽  
Main Components

Stress granules (SGs) are cytoplasmic foci that appear in cells exposed to stress-induced translational inhibition. SGs function as a triage center, where mRNAs are sorted for storage, degradation, and translation reinitiation. The underlying mechanisms of SGs dynamics are still being characterized, although many key players have been identified. The main components of SGs are stalled 48S preinitiation complexes. To date, many other proteins have also been found to localize in SGs and are hypothesized to function in SG dynamics. Most recently, the microtubule cytoskeleton and associated motor proteins have been demonstrated to function in SG dynamics. In this paper, we will discuss current literature examining the function of microtubules and the molecular microtubule motors in SG assembly, coalescence, movement, composition, organization, and disassembly.

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