Topic Editors

Prof. Dr. Malgorzata Kloc
Houston Methodist Hospital and Houston Methodist Research Institute, Houston, TX, USA
Dr. Jacek Kubiak
1. Laboratory of Molecular Oncology and Innovative Therapies, Military Institute of Medicine-National Research Institute (WIM-PIB), Warsaw, Poland
2. Dynamics and Mechanics of Epithelia Group, Faculty of Medicine, Institute of Genetics and Development of Rennes, University of Rennes, CNRS, UMR 6290, Rennes, France

New Insights into Cytoskeleton

Abstract submission deadline
31 January 2026
Manuscript submission deadline
31 March 2026
Viewed by
486

Topic Information

Dear Colleagues,

The cytoskeleton consists of microtubules, microfilaments, and intermediate filaments. In prokaryotic and eukaryotic cells (plants and animals), the cytoskeleton supports cell and organelle structure, facilitates cell movement, phagocytosis, cell adhesion, cell division, and chromosome separation, and transmits environmental signals to the cell. It regulates organellar fission and fusion, vesicular trafficking, and receptor recycling. In immune cells, the cytoskeleton regulates cell–cell interactions and immune response. The cytoskeleton and its molecular motors regulate the localization of coding and noncoding RNAs and proteins to specific destinations. The nuclear cytoskeleton supports nucleus morphology and shape and controls chromatin compaction, transcription, double-strand break mobility, and repair. Viruses and bacteria hijack the cytoskeleton for propagation, movement within the cell, and spreading between cells. For this Topic, we invite reviews and original papers detailing research on the cytoskeleton in animal and plant cells.

Prof. Dr. Malgorzata Kloc
Dr. Jacek Z. Kubiak
Topic Editors

Keywords

  • actin
  • microtubules
  • filaments
  • nuclear cytoskeleton
  • cytoskeleton
  • chromatin compaction
  • cell division
  • animals
  • plants

Participating Journals

Journal Name Impact Factor CiteScore Launched Year First Decision (median) APC
Biophysica
biophysica
1.4 2.3 2021 22.9 Days CHF 1200 Submit
Current Issues in Molecular Biology
cimb
3.0 3.7 1999 17.8 Days CHF 2200 Submit
Biology
biology
3.5 7.4 2012 17.4 Days CHF 2700 Submit
Membranes
membranes
3.6 7.9 2011 17 Days CHF 2200 Submit
International Journal of Molecular Sciences
ijms
4.9 9.0 2000 20.5 Days CHF 2900 Submit

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Published Papers (1 paper)

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25 pages, 9187 KiB  
Article
The Plus End-Directed Microtubule (Kinesin-3 Family) Motor Protein KIF13B Is Associated with the Photoreceptor Synaptic Ribbon Complex
by Shweta Suiwal, Karin Schwarz, Stephan Maxeiner and Frank Schmitz
Int. J. Mol. Sci. 2025, 26(13), 6044; https://doi.org/10.3390/ijms26136044 - 24 Jun 2025
Viewed by 244
Abstract
Retinal ribbon synapses are continuously active chemical synapses. The eponymous synaptic ribbon is anchored to the active zone neurotransmitter release sites of ribbon synapses, recruits synaptic vesicles and guides ribbon-associated synaptic vesicles to the release sites. RIBEYE is the major protein component of [...] Read more.
Retinal ribbon synapses are continuously active chemical synapses. The eponymous synaptic ribbon is anchored to the active zone neurotransmitter release sites of ribbon synapses, recruits synaptic vesicles and guides ribbon-associated synaptic vesicles to the release sites. RIBEYE is the major protein component of synaptic ribbons. But likely, additional proteins contribute to ribbon synapse function. The synaptic ribbon of photoreceptor synapses is embedded into a highly polarized microtubule cytoskeleton. Interestingly, proteins of the photoreceptor primary cilium, such as NPHP4 and other ciliary proteins, including KIF3A, were shown to be localized to photoreceptor synaptic ribbons. Previous studies demonstrated that the microtubule motor protein KIF13B catalyzes secretory vesicle transport to the plus ends of microtubules and identified an interaction of KIF13B with NPHP4 at primary cilia. However, the localization of KIF13B, a kinesin-3 family motor protein, in the retina is still unknown. In the present study, we used two different antibodies against KIF13B and high-resolution confocal microscopy, super-resolution structured illumination microscopy (SR-SIM), and post-embedding immunogold electron microscopy to determine the localization of KIF13B in retinal photoreceptors. Apart from its localization at the primary photoreceptor cilium, we found a strong enrichment of KIF13B at photoreceptor synaptic ribbons. The synaptic ribbon is needed for the synaptic enrichment of KIF13B as shown by analyses of synaptic ribbon-deficient RIBEYE knockout mice. These findings suggest that KIF13B performs vesicle trafficking functions at the photoreceptor synaptic ribbon complex at the interface between the synaptic ribbon and the presynaptic microtubule transport system. Full article
(This article belongs to the Topic New Insights into Cytoskeleton)
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