Computational modeling of dynein motor proteins at work

2021 ◽  
Author(s):  
Mandira Dutta ◽  
Biman Jana
Keyword(s):  
Computational Modeling ◽  
Motor Proteins ◽  
Dynein Motor ◽  
Mechanochemical Cycle

Computational modeling of the mechanochemical cycle of dynein motor proteins.

Exploring the mechanochemical cycle of dynein motor proteins: structural evidence of crucial intermediates

2016 ◽  
Vol 18 (48) ◽  
pp. 33085-33093 ◽  
Author(s):  
Mandira Dutta ◽  
Biman Jana
Keyword(s):  
Motor Proteins ◽  
Biologically Relevant ◽  
Dynein Motor ◽  
Mechanochemical Cycle

Exploration of the biologically relevant pathways of dynein's mechanochemical cycle using structure based models.

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 Spontaneous oscillation and fluid–structure interaction of cilia

2018 ◽  
Vol 115 (17) ◽  
pp. 4417-4422 ◽  
Author(s):  
Jihun Han ◽  
Charles S. Peskin
Keyword(s):  
Motor Proteins ◽  
Phase Synchronization ◽  
Fluid Structure Interaction ◽  
3D Structure ◽  
Immersed Boundary ◽  
Limit Cycle Oscillation ◽  
Fluid Structure ◽  
Structure Interaction ◽  
Dynein Motor ◽  
Fluid Environment

The exact mechanism to orchestrate the action of hundreds of dynein motor proteins to generate wave-like ciliary beating remains puzzling and has fascinated many scientists. We present a 3D model of a cilium and the simulation of its beating in a fluid environment. The model cilium obeys a simple geometric constraint that arises naturally from the microscopic structure of a real cilium. This constraint allows us to determine the whole 3D structure at any instant in terms of the configuration of a single space curve. The tensions of active links, which model the dynein motor proteins, follow a postulated dynamical law, and together with the passive elasticity of microtubules, this dynamical law is responsible for the ciliary motions. In particular, our postulated tension dynamics lead to the instability of a symmetrical steady state, in which the cilium is straight and its active links are under equal tensions. The result of this instability is a stable, wave-like, limit cycle oscillation. We have also investigated the fluid–structure interaction of cilia using the immersed boundary (IB) method. In this setting, we see not only coordination within a single cilium but also, coordinated motion, in which multiple cilia in an array organize their beating to pump fluid, in particular by breaking phase synchronization.

scholarly journals The Mechanical Components of the Dynein Motor

2010 ◽  
Vol 10 ◽  
pp. 857-864 ◽  
Author(s):  
Peter Höök
Keyword(s):  
Motor Activity ◽  
Molecular Mechanism ◽  
Motor Proteins ◽  
The Other ◽  
Structural Components ◽  
Complex Interplay ◽  
Unique Role ◽  
Dynein Motor ◽  
Slow Progress ◽  
Mechanical Components

Unlike our understanding of the other two classes of cytoskeletal motor proteins, the myosins and kinesins, we have only recently begun to comprehend the molecular mechanism for how dynein produces force and movement. The slow progress has been attributed, in part, to the enormous size of the dynein force-producing head, but also to the complex interplay between its structural components, each of which has a unique role in regulating dynein motor activity. The integrated and highly coordinated mechanism by which these structures work together in powering the dynein machinery is discussed in this review.

scholarly journals Localized mRNA translation mediates maturation of cytoplasmic cilia in Drosophila spermatogenesis

2020 ◽  
Author(s):  
Jaclyn M Fingerhut ◽  
Yukiko M Yamashita
Keyword(s):  
Motor Proteins ◽  
Mrna Translation ◽  
Local Translation ◽  
Granule Formation ◽  
Male Gametes ◽  
Dynein Motor ◽  
Cilia Formation ◽  
Axonemal Dynein

AbstractCytoplasmic cilia, a specialized type of cilia in which the axoneme resides within the cytoplasm rather than within the ciliary compartment, are proposed to allow the efficient assembly of very long cilia. Despite being found diversely in male gametes (e.g. Plasmodium microgametocytes and human and Drosophila sperm), very little is known about cytoplasmic cilia assembly. Here we show that a novel RNP granule containing the mRNAs for axonemal dynein motor proteins becomes highly polarized to the distal end of the cilia during cytoplasmic ciliogenesis in Drosophila sperm. This allows for the localized translation of these axonemal dyneins and their incorporation into the axoneme directly from the cytoplasm. We found that this RNP granule contains the proteins Reptin and Pontin, loss of which perturbs granule formation and prevents incorporation of the axonemal dyneins, leading to sterility. We propose that cytoplasmic cilia require the local translation of key protein constituents such that these proteins are incorporated efficiently into the axoneme.Author SummaryCytoplasmic cilia, which are found in human and Drosophila sperm, are unique in that the axoneme is exposed to the cytoplasm. The authors show that a novel RNP granule containing axonemal dynein mRNAs facilitates localized translation of these axonemal proteins, facilitating cytoplasmic cilia formation.

scholarly journals Functions and mechanics of dynein motor proteins

2013 ◽  
Vol 14 (11) ◽  
pp. 713-726 ◽  
Author(s):  
Anthony J. Roberts ◽  
Takahide Kon ◽  
Peter J. Knight ◽  
Kazuo Sutoh ◽  
Stan A. Burgess
Keyword(s):  
Motor Proteins ◽  
Dynein Motor

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 mRNA localization mediates maturation of cytoplasmic cilia in Drosophila spermatogenesis

2020 ◽  
Vol 219 (9) ◽  
Author(s):  
Jaclyn M. Fingerhut ◽  
Yukiko M. Yamashita
Keyword(s):  
Plasmodium Falciparum ◽  
Drosophila Melanogaster ◽  
Motor Proteins ◽  
Mrna Localization ◽  
Precise Localization ◽  
Granule Formation ◽  
Male Gametes ◽  
Dynein Motor ◽  
Axonemal Dynein

Cytoplasmic cilia, a specialized type of cilia in which the axoneme resides within the cytoplasm rather than within the ciliary compartment, are proposed to allow for the efficient assembly of very long cilia. Despite being found diversely in male gametes (e.g., Plasmodium falciparum microgametocytes and human and Drosophila melanogaster sperm), very little is known about cytoplasmic cilia assembly. Here, we show that a novel RNP granule containing the mRNAs for axonemal dynein motor proteins becomes highly polarized to the distal end of the cilia during cytoplasmic ciliogenesis in Drosophila sperm. This allows for the incorporation of these axonemal dyneins into the axoneme directly from the cytoplasm, possibly by localizing translation. We found that this RNP granule contains the proteins Reptin and Pontin, loss of which perturbs granule formation and prevents incorporation of the axonemal dyneins, leading to sterility. We propose that cytoplasmic cilia assembly requires the precise localization of mRNAs encoding key axonemal constituents, allowing these proteins to incorporate efficiently into the axoneme.

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