Cytoskeleton and Molecular Motors

A special issue of Life (ISSN 2075-1729). This special issue belongs to the section "Cell Biology and Tissue Engineering".

Deadline for manuscript submissions: closed (30 May 2022) | Viewed by 2644

Special Issue Editors


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Guest Editor
Institute of Zoology, Chinese Academy of Sciences, Beijing 100107, China
Interests: actin; cytoskeleton; enzyme regulation; intracellular trafficking; molecular motor; muscle; myosin

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Guest Editor
College of Life Sciences, Beijing Normal University, Beijing 100875, China
Interests: major sperm protein; cell polarity establishment; vesicle trafficking; spermatogenesis; spermiogenesis; cell migration; C. elegans

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Guest Editor
School of Life Science, Lanzhou University, Lanzhou 730000, China
Interests: actin cytoskeleton; pollen tube growth; vesicle trafficking

Special Issue Information

Dear Colleagues,

The cytoskeleton consists of three types of protein filaments: actin, microtubule, and intermediate filaments. Each filament interacts with a large number of accessory proteins. One type of accessory proteins is molecular motor, including the microtubule-based motors dynein and kinesin, and actin-based motor myosin. By harnessing the energy from ATP hydrolysis, molecular motors are able to generate force and move along the cytoskeleton track unidirectionally. Cytoskeleton and molecular motors are essential for many cellular activities, including cell movement (motility), cell division, intracellular trafficking, and signaling transduction. While the basic structure and function of cytoskeleton are fairly well understood, as are the basic components and the dynamics of cytoskeleton, many novel functions of cytoskeleton are revealed recently. Myosin and kinesin each constitute a large superfamily with dozens of classes and only a few of them have been well studied so far. Investigation of cellular function and molecular regulation of molecular motors will provide key information on how the components within a cell move to the right place at the right time.

The present Special issue is aimed to gather the latest advances and outstanding research in the field of cytoskeleton and molecular motor. We invite research publications and review articles including, but not limited to, the following topics:

  • The dynamics of cytoskeleton and the related cellular functions
  • Signaling molecules and cytoskeleton
  • Cytoskeleton-associated development disorders and diseases
  • Structure and function of molecular motor proteins, including myosin, kinesin and dynein.
  • Regulation of the motor functions of myosin, kinesin and dynein.

Prof. Dr. Xiangdong Li
Prof. Dr. Long Miao
Prof. Dr. Yun Xiang
Guest Editors

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Keywords

  • actin
  • cytoskeleton
  • dynein
  • intracellular trafficking
  • kinesin
  • microtubule
  • myosin

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Published Papers (1 paper)

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Research

12 pages, 5894 KiB  
Article
Structural Analysis of Human Fascin-1: Essential Protein for Actin Filaments Bundling
by Jeong Min Chung, Osamu Sato, Reiko Ikebe, Sangmin Lee, Mitsuo Ikebe and Hyun Suk Jung
Life 2022, 12(6), 843; https://doi.org/10.3390/life12060843 - 6 Jun 2022
Cited by 5 | Viewed by 2183
Abstract
Fascin, a major actin cross-linking protein, is expressed in most vertebrate epithelial tissues. It organizes actin filaments into well-ordered bundles that are responsible for the extension of dynamic membrane protrusions, including microspikes, filopodia, and invadopodia from cell surfaces, which are involved in cell [...] Read more.
Fascin, a major actin cross-linking protein, is expressed in most vertebrate epithelial tissues. It organizes actin filaments into well-ordered bundles that are responsible for the extension of dynamic membrane protrusions, including microspikes, filopodia, and invadopodia from cell surfaces, which are involved in cell migration and invasion as critical components of cancer metastasis. However, it is not well-understood how fascin-1 induces actin binding/bundling and where fascin-1 localizes along the actin filaments, thus facilitating actin bundle formation. In the present study, we attempted to clarify these problems by using biochemical and electron microscopic analyses using various fascin-1 constructs. Three dimensional structures of actin/fascin-1 complex were obtained by electron microscopy (EM) with iterative helical real-space reconstruction (IHRSR) and tomography. We revealed that the N-terminal region containing the Actin-Binding Site 2 (ABS2) of fascin-1 is responsible for actin bundling and the C-terminal region is important for the dimerization of fascin-1. We also found that the dimerization of fascin-1 through intermolecular interactions of the C-terminal region is essential for actin bundling. Since fascin is an important factor in cancer development, it is expected that the findings of present study will provide useful information for development of therapeutic strategies for cancer. Full article
(This article belongs to the Special Issue Cytoskeleton and Molecular Motors)
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