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 A Light-Inducible Strain for Genome-Wide Histone Turnover Profiling in Neurospora crassa

Genetics ◽  
2020 ◽  
Vol 215 (3) ◽  
pp. 569-578
Author(s):  
William K. Storck ◽  
Sabrina Z. Abdulla ◽  
Michael R. Rountree ◽  
Vincent T. Bicocca ◽  
Eric U. Selker
Keyword(s):  
Neurospora Crassa ◽  
Histone H3 ◽  
Chromatin Accessibility ◽  
Histone Octamer ◽  
Genome Wide ◽  
Incubation Periods ◽  
Mutant Strains ◽  
Functional Consequences ◽  
Dynamic Structures ◽  
Histone Exchange

In chromatin, nucleosomes are composed of ∼146 bp of DNA wrapped around a histone octamer, and are highly dynamic structures subject to remodeling and exchange. Histone turnover has previously been implicated in various processes including the regulation of chromatin accessibility, segregation of chromatin domains, and dilution of histone marks. Histones in different chromatin environments may turnover at different rates, possibly with functional consequences. Neurospora crassa sports a chromatin environment that is more similar to that of higher eukaryotes than yeasts, which have been utilized in the past to explore histone exchange. We constructed a simple light-inducible system to profile histone exchange in N. crassa on a 3xFLAG-tagged histone H3 under the control of the rapidly inducible vvd promoter. After induction with blue light, incorporation of tagged H3 into chromatin occurred within 20 min. Previous studies of histone turnover involved considerably longer incubation periods and relied on a potentially disruptive change of medium for induction. We used this reporter to explore replication-independent histone turnover at genes and examine changes in histone turnover at heterochromatin domains in different heterochromatin mutant strains. In euchromatin, H3-3xFLAG patterns were almost indistinguishable from that observed in wild-type in all mutant backgrounds tested, suggesting that loss of heterochromatin machinery has little effect on histone turnover in euchromatin. However, turnover at heterochromatin domains increased with loss of trimethylation of lysine 9 of histone H3 or HP1, but did not depend on DNA methylation. Our reporter strain provides a simple yet powerful tool to assess histone exchange across multiple chromatin contexts.

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 Microtubules and motor proteins support zebrafish neuronal migration by directing cargo

2020 ◽  
Vol 219 (10) ◽  
Author(s):  
Ulrike Theisen ◽  
Alexander U. Ernst ◽  
Ronja L.S. Heyne ◽  
Tobias P. Ring ◽  
Oliver Thorn-Seshold ◽  
...  
Keyword(s):  
Golgi Apparatus ◽  
Neuronal Migration ◽  
Motor Proteins ◽  
Zebrafish Embryos ◽  
Protein Distribution ◽  
Cell Type ◽  
Similar Extent ◽  
Functional Brain ◽  
Subcellular Imaging

Neuronal migration during development is necessary to form an ordered and functional brain. Postmitotic neurons require microtubules and dynein to move, but the mechanisms by which they contribute to migration are not fully characterized. Using tegmental hindbrain nuclei neurons in zebrafish embryos together with subcellular imaging, optogenetics, and photopharmacology, we show that, in vivo, the centrosome’s position relative to the nucleus is not linked to greatest motility in this cell type. Nevertheless, microtubules, dynein, and kinesin-1 are essential for migration, and we find that interference with endosome formation or the Golgi apparatus impairs migration to a similar extent as disrupting microtubules. In addition, an imbalance in the traffic of the model cargo Cadherin-2 also reduces neuronal migration. These results lead us to propose that microtubules act as cargo carriers to control spatiotemporal protein distribution, which in turn controls motility. This adds crucial insights into the variety of ways that microtubules can support successful neuronal migration in vivo.

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.

Sign in / Sign up

Export Citation Format

Share Document