ijms-logo

Journal Browser

Journal Browser

Special Issue "Cytoskeletal Dynamics and Regulation of Cell Cycle Progression"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: 31 July 2021.

Special Issue Editors

Prof. Dr. Leah Gheber
E-Mail Website
Guest Editor
Ben-Gurion University of the Negev | bgu · Department of Chemistry
Interests: mitotic-spindle kinesin-related motor proteins cell-cycle cancer microtubule cytoskeleton
Prof. Dr. Mart Loog
E-Mail
Guest Editor
University of Tartudisabled, Tartu, Estonia

Special Issue Information

Dear Colleagues,

The correct transmission of genetic information from one generation to the next and the successful completion of mitosis depend on the temporal and spatial coordination of many mitotic processes such as mitotic spindle assembly, chromosome segregation and spindle elongation, spindle disassembly, and cytokinesis. To ensure correct chromosome segregation, spindle morphogenesis and cell cycle progression are monitored by multiple surveillance systems that include a number of protein kinases and phosphatases controlling and affecting the phosphorylation of mitotic proteins, thus regulating their activity and intracellular localization.

Morphological changes of the mitotic spindle are governed, in part, by the dynamics of cytoskeletal filaments—actin filaments and microtubules—and by the functions of molecular motors of the myosin, dynein, and kinesin superfamilies, which utilize energy from ATP hydrolysis to produce nanometric directional steps along the filaments of the cytoskeleton. The regulation and coordination of cytoskeletal dynamics and of molecular motors is of critical importance to correctly segregate chromosomes and allow cell cycle progression. Despite major research efforts during the last decades, the mechanisms by which cytoskeletal dynamics is controlled and coordinated by the cell cycle surveillance machinery remain elusive. 

In recent years, new advances in microscopic imaging and biophysical and biochemical techniques, as well as advances in cryo-electron microscopy have led to scientific breakthroughs allowing a new understanding of the regulation mechanisms and cytoskeletal dynamics during cell cycle progression. In this Special Issue, we will highlight the recent advances in this field and discuss open questions and future directions.

Prof. Dr. Leah Gheber
Prof. Dr. Mart Loog
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • kinesin
  • dynein
  • myosin
  • mitosis, cell cycle
  • kinases, phosphatases, microtubules
  • actin filaments
  • intracellular trafficking

Published Papers (1 paper)

Order results
Result details
Select all
Export citation of selected articles as:

Research

Open AccessArticle
The Putative RNA-Binding Protein Dri1 Promotes the Loading of Kinesin-14/Klp2 to the Mitotic Spindle and Is Sequestered into Heat-Induced Protein Aggregates in Fission Yeast
Int. J. Mol. Sci. 2021, 22(9), 4795; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22094795 - 30 Apr 2021
Viewed by 300
Abstract
Cells form a bipolar spindle during mitosis to ensure accurate chromosome segregation. Proper spindle architecture is established by a set of kinesin motors and microtubule-associated proteins. In most eukaryotes, kinesin-5 motors are essential for this process, and genetic or chemical inhibition of their [...] Read more.
Cells form a bipolar spindle during mitosis to ensure accurate chromosome segregation. Proper spindle architecture is established by a set of kinesin motors and microtubule-associated proteins. In most eukaryotes, kinesin-5 motors are essential for this process, and genetic or chemical inhibition of their activity leads to the emergence of monopolar spindles and cell death. However, these deficiencies can be rescued by simultaneous inactivation of kinesin-14 motors, as they counteract kinesin-5. We conducted detailed genetic analyses in fission yeast to understand the mechanisms driving spindle assembly in the absence of kinesin-5. Here, we show that deletion of the dri1 gene, which encodes a putative RNA-binding protein, can rescue temperature sensitivity caused by cut7-22, a fission yeast kinesin-5 mutant. Interestingly, kinesin-14/Klp2 levels on the spindles in the cut7 mutants were significantly reduced by the dri1 deletion, although the total levels of Klp2 and the stability of spindle microtubules remained unaffected. Moreover, RNA-binding motifs of Dri1 are essential for its cytoplasmic localization and function. We have also found that a portion of Dri1 is spatially and functionally sequestered by chaperone-based protein aggregates upon mild heat stress and limits cell division at high temperatures. We propose that Dri1 might be involved in post-transcriptional regulation through its RNA-binding ability to promote the loading of Klp2 on the spindle microtubules. Full article
(This article belongs to the Special Issue Cytoskeletal Dynamics and Regulation of Cell Cycle Progression)
Show Figures

Figure 1

Back to TopTop