Non-muscle Myosin II Motor Proteins in Human Health and Diseases

2017 ◽  
pp. 79-107
Author(s):  
Venkaiah Betapudi
Keyword(s):  
Human Health ◽  
Motor Proteins ◽  
Myosin Ii ◽  
Muscle Myosin

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 Non-muscle myosin II drives vesicle loss during human reticulocyte maturation

Haematologica ◽  
2018 ◽  
Vol 103 (12) ◽  
pp. 1997-2007 ◽  
Author(s):  
Pedro L. Moura ◽  
Bethan R. Hawley ◽  
Tosti J. Mankelow ◽  
Rebecca E. Griffiths ◽  
Johannes G.G. Dobbe ◽  
...  
Keyword(s):  
Myosin Ii ◽  
Reticulocyte Maturation ◽  
Muscle Myosin

scholarly journals Non-muscle myosin II in kidney morphogenesis

2017 ◽  
Vol 13 (7) ◽  
pp. 384-384
Author(s):  
Katharine H. Wrighton
Keyword(s):  
Myosin Ii ◽  
Kidney Morphogenesis ◽  
Muscle Myosin

scholarly journals Fibroblast Migration in 3D is Controlled by Haptotaxis in a Non-muscle Myosin II-Dependent Manner

2015 ◽  
Vol 43 (12) ◽  
pp. 3025-3039 ◽  
Author(s):  
O. Moreno-Arotzena ◽  
C. Borau ◽  
N. Movilla ◽  
M. Vicente-Manzanares ◽  
J. M. García-Aznar
Keyword(s):  
Myosin Ii ◽  
Dependent Manner ◽  
Fibroblast Migration ◽  
Muscle Myosin

Molecular Motors: Force and Movement Generated by Single Myosin II Molecules

Physiology ◽  
2002 ◽  
Vol 17 (5) ◽  
pp. 213-218 ◽  
Author(s):  
Caspar Rüegg ◽  
Claudia Veigel ◽  
Justin E. Molloy ◽  
Stephan Schmitz ◽  
John C. Sparrow ◽  
...  
Keyword(s):  
Optical Tweezers ◽  
Single Molecule ◽  
Molecular Motors ◽  
Molecular Motor ◽  
Myosin Ii ◽  
Force Production ◽  
Myosin Isoforms ◽  
Single Molecule Level ◽  
Recent Developments ◽  
Muscle Myosin

Muscle myosin II is an ATP-driven, actin-based molecular motor. Recent developments in optical tweezers technology have made it possible to study movement and force production on the single-molecule level and to find out how different myosin isoforms may have adapted to their specific physiological roles.

scholarly journals Dia- and Rok-dependent enrichment of capping proteins in a cortical region

2021 ◽  
Author(s):  
Anja Schmidt ◽  
Long Li ◽  
Zhiyi Lv ◽  
Shuling Yan ◽  
Jörg Großhans
Keyword(s):  
Myosin Ii ◽  
Rho Kinase ◽  
Cortical Region ◽  
Protein Enrichment ◽  
Cortical Actin ◽  
Capping Protein ◽  
Capping Proteins ◽  
Muscle Myosin ◽  
Drosophila Embryos

Rho signaling with its major targets the formin Dia, Rho kinase (Rok) and non-muscle myosin II control turnover, amount and contractility of actomyosin. Much less investigated has been a potential function for the distribution of F-actin plus and minus ends. In syncytial Drosophila embryos Rho1 signaling is high between actin caps, i. e. the cortical intercap region. Capping protein binds to free plus ends of F-actin to prevent elongation of the filament. Capping protein has served as a marker to visualize the distribution of F-actin plus ends in cells and in vitro. Here, we probed the distribution of plus ends with capping protein in syncytial Drosophila embryos. We found that Capping proteins are specifically enriched in the intercap region similar to Dia and MyoII but distinct from overall F-actin. The intercap enrichment of Capping protein was impaired in dia mutants and embryos, in which Rok and MyoII activation was inhibited. Our observations reveal that Dia and Rok/MyoII control Capping protein enrichment and support a model that Dia and Rok/MyoII control the organization of cortical actin cytoskeleton downstream of Rho1 signaling.

scholarly journals Mechanical bistability enabled by ectodermal compression facilitates Drosophila mesoderm invagination

2021 ◽  
Author(s):  
Hanqing Guo ◽  
Michael Swan ◽  
Shicheng Huang ◽  
Bing He
Keyword(s):  
Myosin Ii ◽  
Cell Sheet ◽  
Apical Surface ◽  
Apical Constriction ◽  
Out Of Plane ◽  
A Cell ◽  
Plane Compression ◽  
Contractile Forces ◽  
Tissue Relaxation ◽  
Muscle Myosin

Apical constriction driven by non-muscle myosin II (″myosin″) provides a well-conserved mechanism to mediate epithelial folding. It remains unclear how contractile forces near the apical surface of a cell sheet drive out-of-plane bending of the sheet and whether myosin contractility is required throughout folding. By optogenetic-mediated acute inhibition of myosin, we find that during Drosophila mesoderm invagination, myosin contractility is critical to prevent tissue relaxation during the early, ″priming″ stage of folding but is dispensable for the actual folding step after the tissue passes through a stereotyped transitional configuration, suggesting that the mesoderm is mechanically bistable during gastrulation. Combining computer modeling and experimental measurements, we show that the observed mechanical bistability arises from an in-plane compression from the surrounding ectoderm, which promotes mesoderm invagination by facilitating a buckling transition. Our results indicate that Drosophila mesoderm invagination requires a joint action of local apical constriction and global in-plane compression to trigger epithelial buckling.

scholarly journals A Genetically Encoded Biosensor Strategy for Quantifying Non-muscle Myosin II Phosphorylation Dynamics in Living Cells and Organisms

Cell Reports ◽  
2018 ◽  
Vol 24 (4) ◽  
pp. 1060-1070.e4 ◽  
Author(s):  
Michele L. Markwardt ◽  
Nicole E. Snell ◽  
Min Guo ◽  
Yicong Wu ◽  
Ryan Christensen ◽  
...  
Keyword(s):  
Myosin Ii ◽  
Living Cells ◽  
Muscle Myosin ◽  
Genetically Encoded Biosensor

scholarly journals Linking the Landscape of MYH9-Related Diseases to the Molecular Mechanisms that Control Non-Muscle Myosin II-A Function in Cells

Cells ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 1458 ◽  
Author(s):  
Gloria Asensio-Juárez ◽  
Clara Llorente-González ◽  
Miguel Vicente-Manzanares
Keyword(s):  
Molecular Mechanisms ◽  
Clinical Presentation ◽  
Molecular Motor ◽  
Myosin Ii ◽  
Residual Activity ◽  
Cellular Level ◽  
Actin Binding ◽  
Compensatory Mechanisms ◽  
Myh9 Gene ◽  
Muscle Myosin

The MYH9 gene encodes the heavy chain (MHCII) of non-muscle myosin II A (NMII-A). This is an actin-binding molecular motor essential for development that participates in many crucial cellular processes such as adhesion, cell migration, cytokinesis and polarization, maintenance of cell shape and signal transduction. Several types of mutations in the MYH9 gene cause an array of autosomal dominant disorders, globally known as MYH9-related diseases (MYH9-RD). These include May-Hegglin anomaly (MHA), Epstein syndrome (EPS), Fechtner syndrome (FTS) and Sebastian platelet syndrome (SPS). Although caused by different MYH9 mutations, all patients present macrothrombocytopenia, but may later display other pathologies, including loss of hearing, renal failure and presenile cataracts. The correlation between the molecular and cellular effects of the different mutations and clinical presentation are beginning to be established. In this review, we correlate the defects that MYH9 mutations cause at a molecular and cellular level (for example, deficient filament formation, altered ATPase activity or actin-binding) with the clinical presentation of the syndromes in human patients. We address why these syndromes are tissue restricted, and the existence of possible compensatory mechanisms, including residual activity of mutant NMII-A and/or the formation of heteropolymers or co-polymers with other NMII isoforms.

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