Myosin Motor Proteins in the Cell Biology of Axons and Other Neuronal Compartments

2009 ◽  
pp. 191-205 ◽  
Author(s):  
Paul C Bridgman
Keyword(s):  
Cell Biology ◽  
Motor Proteins ◽  
Myosin Motor ◽  
Neuronal Compartments

Intracellular Transport and Kinesin Superfamily Proteins, KIFs: Structure, Function, and Dynamics

2008 ◽  
Vol 88 (3) ◽  
pp. 1089-1118 ◽  
Author(s):  
Nobutaka Hirokawa ◽  
Yasuko Noda
Keyword(s):  
Cell Biology ◽  
Intracellular Transport ◽  
Structural Changes ◽  
Motor Proteins ◽  
Protein Complexes ◽  
Molecular Genetic ◽  
Adaptor Protein ◽  
Binding Activity ◽  
Brain Functions ◽  
Kinesin Superfamily

Various molecular cell biology and molecular genetic approaches have indicated significant roles for kinesin superfamily proteins (KIFs) in intracellular transport and have shown that they are critical for cellular morphogenesis, functioning, and survival. KIFs not only transport various membrane organelles, protein complexes, and mRNAs for the maintenance of basic cellular activity, but also play significant roles for various mechanisms fundamental for life, such as brain wiring, higher brain functions such as memory and learning and activity-dependent neuronal survival during brain development, and for the determination of important developmental processes such as left-right asymmetry formation and suppression of tumorigenesis. Accumulating data have revealed a molecular mechanism of cargo recognition involving scaffolding or adaptor protein complexes. Intramolecular folding and phosphorylation also regulate the binding activity of motor proteins. New techniques using molecular biophysics, cryoelectron microscopy, and X-ray crystallography have detected structural changes in motor proteins, synchronized with ATP hydrolysis cycles, leading to the development of independent models of monomer and dimer motors for processive movement along microtubules.

scholarly journals Distribution and evolution of stable single α-helices (SAH domains) in myosin motor proteins

PLoS ONE ◽  
2017 ◽  
Vol 12 (4) ◽  
pp. e0174639 ◽  
Author(s):  
Dominic Simm ◽  
Klas Hatje ◽  
Martin Kollmar
Keyword(s):  
Motor Proteins ◽  
Myosin Motor

scholarly journals A diffusiophoretic mechanism for ATP-driven transport without motor proteins

2021 ◽  
Author(s):  
Beatrice Ramm ◽  
Andriy Goychuk ◽  
Alena Khmelinskaia ◽  
Philipp Blumhardt ◽  
Hiromune Eto ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Cell Biology ◽  
Spatial Organization ◽  
Motor Proteins ◽  
Reaction Diffusion ◽  
Specific Protein ◽  
A Cell ◽  
Healthy Growth ◽  
Diffusive Fluxes ◽  
Active Processes

AbstractThe healthy growth and maintenance of a biological system depends on the precise spatial organization of molecules within the cell through the dissipation of energy. Reaction–diffusion mechanisms can facilitate this organization, as can directional cargo transport orchestrated by motor proteins, by relying on specific protein interactions. However, transport of material through the cell can also be achieved by active processes based on non-specific, purely physical mechanisms, a phenomenon that remains poorly explored. Here, using a combined experimental and theoretical approach, we discover and describe a hidden function of the Escherichia coli MinDE protein system: in addition to forming dynamic patterns, this system accomplishes the directional active transport of functionally unrelated cargo on membranes. Remarkably, this mechanism enables the sorting of diffusive objects according to their effective size, as evidenced using modular DNA origami–streptavidin nanostructures. We show that the diffusive fluxes of MinDE and non-specific cargo couple via density-dependent friction. This non-specific process constitutes a diffusiophoretic mechanism, as yet unknown in a cell biology setting. This nonlinear coupling between diffusive fluxes could represent a generic physical mechanism for establishing intracellular organization.

scholarly journals MYO1C facilitates arrival at the Golgi apparatus through stabilization of branched actin

2018 ◽  
Author(s):  
Anahi Capmany ◽  
Azumi Yoshimura ◽  
Rachid Kerdous ◽  
Aurianne Lescure ◽  
Elaine Del Nery ◽  
...  
Keyword(s):  
Golgi Apparatus ◽  
Motor Proteins ◽  
Myosin Motor ◽  
Functional Consequences ◽  
Myosin Iia ◽  
Dynamic Structures

AbstractWe aim at the identification of myosin motor proteins that control trafficking at the Golgi apparatus. In addition to the known Golgi-associated myosins MYO6, MYO18A and MYH9 (myosin IIA), we identify MYO1C as a novel player at the Golgi. We demonstrate that depletion of MYO1C induces Golgi apparatus fragmentation and decompaction. MYO1C accumulates at dynamic structures around the Golgi apparatus that colocalize with Golgi-associated actin dots. Interestingly, MYO1C depletion leads to loss of cellular F-actin, and Golgi apparatus decompaction is also observed after the inhibition or loss of the Arp2/3 complex. We show that the functional consequences of MYO1C depletion is a delay in the arrival of incoming transport carriers, both from the anterograde and retrograde routes. We propose that MYO1C stabilizes branched actin at the Golgi apparatus that facilitates the arrival of incoming transport at the Golgi.

scholarly journals Potential roles of myosin VI in cell motility

2009 ◽  
Vol 37 (5) ◽  
pp. 966-970 ◽  
Author(s):  
Margarita V. Chibalina ◽  
Claudia Puri ◽  
John Kendrick-Jones ◽  
Folma Buss
Keyword(s):  
Cell Motility ◽  
Actin Filament ◽  
Motor Proteins ◽  
Leading Edge ◽  
Potential Functions ◽  
Present Review ◽  
Myosin Vi ◽  
Adhesion Proteins ◽  
Myosin Motor ◽  
Migrating Cells

There is now increasing evidence that myosin motor proteins, together with the dynamic actin filament machinery and associated adhesion proteins, play crucial roles in the events leading to motility at the leading edge of migrating cells. Myosins exist as a large superfamily of diverse ATP-dependent motors, and in the present review, we focus on the unique minus-end-directed myosin VI, briefly discussing its potential functions in cell motility.

scholarly journals Myosin motor proteins are involved in the final stages of the secretory pathways

2011 ◽  
Vol 39 (5) ◽  
pp. 1115-1119 ◽  
Author(s):  
Lisa M. Bond ◽  
Hemma Brandstaetter ◽  
James R. Sellers ◽  
John Kendrick-Jones ◽  
Folma Buss
Keyword(s):  
Plasma Membrane ◽  
Recent Work ◽  
Secretory Pathway ◽  
Motor Proteins ◽  
Myosin Ii ◽  
Secretory Vesicles ◽  
Secretory Pathways ◽  
Unconventional Myosin ◽  
Myosin Motor ◽  
Muscle Myosin

In eukaryotes, the final steps in both the regulated and constitutive secretory pathways can be divided into four distinct stages: (i) the ‘approach’ of secretory vesicles/granules to the PM (plasma membrane), (ii) the ‘docking’ of these vesicles/granules at the membrane itself, (iii) the ‘priming’ of the secretory vesicles/granules for the fusion process, and, finally, (iv) the ‘fusion’ of vesicular/granular membranes with the PM to permit content release from the cell. Recent work indicates that non-muscle myosin II and the unconventional myosin motor proteins in classes 1c/1e, Va and VI are specifically involved in these final stages of secretion. In the present review, we examine the roles of these myosins in these stages of the secretory pathway and the implications of their roles for an enhanced understanding of secretion in general.

scholarly journals Myosin driven Actin Filament Sliding is Responsible for Endoplasmic Reticulum and Golgi Movement

2018 ◽  
Author(s):  
Joseph F McKenna ◽  
Stephen E D Webb ◽  
Verena Kriechbaumer ◽  
Chris Hawes
Keyword(s):  
Endoplasmic Reticulum ◽  
Actin Cytoskeleton ◽  
Actin Filament ◽  
Secretory Pathway ◽  
Motor Proteins ◽  
In Planta ◽  
Cell Dynamics ◽  
Myosin Motor ◽  
Golgi Bodies ◽  
Early Secretory Pathway

AbstractThe plant secretory pathway is responsible for the production of the majority of proteins and carbohydrates consumed on the planet. The early secretory pathway is composed of Golgi bodies and the endoplasmic reticulum (ER) and is highly mobile in plants with rapid remodelling of the ER network. The dynamics of the ER and Golgi bodies is driven by the actin cytoskeleton and myosin motor proteins play a key role in this. However, exactly how myosin motor proteins drive remodelling in plants is currently a contentious issue. Here, using a combination of live cell microscopy and over-expression of non-functional myosins we demonstrate that myosin motor proteins drive actin filament sliding and subsequently the dynamics of the secretory pathway.SummaryIn plants, the actin cytoskeleton and myosins are fundamental for normal dynamics of the endomembrane system and cytoplasmic streaming. We demonstrate that this is in part due to myosin driven sliding of actin filaments within a bundle. This generates, at least in part, the motive force required for cell dynamics in planta.

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