An actomyosin motor.

H Shimizu

doi:10.1007/978-1-4684-4703-3_38

Home/Archive/PubMed

PubMed · 6377847

An actomyosin motor.

H Shimizu

View original source ↗Export metadata ↓

Abstract

I would like to report some results obtained by Yano , Yamamoto and myself on a novel system ( Yano et al., 1982) we have named the actomyosin motor in which a rotor with attached F-actin rotates in a specific direction, driven by the ATP-splitting interaction with active fragments of myosin, heavy meromyosin or subfragment-1, in a solution containing MgATP. The actomyosin motor is not only interesting as a new kind of motor made of biological material but also, as a stream cell ( Yano , 1978; Yano et al., 1978; Yano & Shimizu, 1978; Shimizu & Yano , 1978; Shimizu, 1979), is suitable for the study of chemo-mechanical coupling by actin and active fragments of myosin. Active motion of the motor was observed in almost 100% of the experiments, when carefully performed.

Explore related subjects

Actomyosin Adenosine Triphosphate Animals Kinetics Muscle Contraction Muscles Myosin Subfragments Myosins Peptide Fragments Rotation Journal Article

Keep this discovery

Explore connections, maps & timelines

BibTeX RIS

H Shimizu. 1984. An actomyosin motor.. https://doi.org/10.1007/978-1-4684-4703-3_38

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2007

Two distinct modes of myosin assembly and dynamics during epithelial wound closure.

Actomyosin contraction powers the sealing of epithelial sheets during embryogenesis and wound closure; however, the mechanisms are poorly understood. After laser ablation wounding of Madin-Darby canine kidney cell monolayers, we observed distinct steps in wound closure from time-lapse images of myosin distribution during resealing. Immediately upon wounding, actin and myosin II regulatory light chain accumulated at two locations: (1) in a ring adjacent to the tight junction that circumscribed the wound and (2) in fibers at the base of the cell in membranes extending over the wound site. Rho-kinase activity was required for assembly of the myosin ring, and myosin II activity was required for contraction but not for basal membrane extension. As it contracted, the myosin ring moved toward the basal membrane with ZO-1 and Rho-kinase. Thus, we suggest that tight junctions serve as attachment points for the actomyosin ring during wound closure and that Rho-kinase is required for localization and activation of the contractile ring.

Actomyosin↗

PubMed2006

Understanding ERM proteins--the awesome power of genetics finally brought to bear.

In epithelial cells, the Ezrin, Radixin and Moesin (ERM) proteins are involved in many cellular functions, including regulation of actin cytoskeleton, control of cell shape, adhesion and motility, and modulation of signaling pathways. However, discerning the specific cellular roles of ERMs has been complicated by redundancy between these proteins. Recent genetic studies in model organisms have identified unique roles for ERM proteins. These include the regulation of morphogenesis and maintenance of integrity of epithelial cells, stabilization of intercellular junctions, and regulation of the Rho small GTPase. These studies also suggest that ERMs have roles in actomyosin contractility and vesicular trafficking in the apical domain of epithelial cells. Thus, genetic analysis has enhanced our understanding of these widely expressed membrane-associated proteins.

Actomyosin↗

PubMed2006

Rhizoids and protonemata of characean algae: model cells for research on polarized growth and plant gravity sensing.

Gravitropically tip-growing rhizoids and protonemata of characean algae are well-established unicellular plant model systems for research on gravitropism. In recent years, considerable progress has been made in the understanding of the cellular and molecular mechanisms underlying gravity sensing and gravity-oriented growth. While in higher-plant statocytes the role of cytoskeletal elements, especially the actin cytoskeleton, in the mechanisms of gravity sensing is still enigmatic, there is clear evidence that in the characean cells actin is intimately involved in polarized growth, gravity sensing, and the gravitropic response mechanisms. The multiple functions of actin are orchestrated by a variety of actin-binding proteins which control actin polymerisation, regulate the dynamic remodelling of the actin filament architecture, and mediate the transport of vesicles and organelles. Actin and a steep gradient of cytoplasmic free calcium are crucial components of a feedback mechanism that controls polarized growth. Experiments performed in microgravity provided evidence that actomyosin is a key player for gravity sensing: it coordinates the position of statoliths and, upon a change in the cell's orientation, directs sedimenting statoliths to specific areas of the plasma membrane, where contact with membrane-bound gravisensor molecules elicits short gravitropic pathways. In rhizoids, gravitropic signalling leads to a local reduction of cytoplasmic free calcium and results in differential growth of the opposite subapical cell flanks. The negative gravitropic response of protonemata involves actin-dependent relocation of the calcium gradient and displacement of the centre of maximal growth towards the upper flank. On the basis of the results obtained from the gravitropic model cells, a similar fine-tuning function of the actomyosin system is discussed for the early steps of gravity sensing in higher-plant statocytes.

Actomyosin↗