Microtubules: Organization, Dynamics and Functions

A special issue of Cells (ISSN 2073-4409). This special issue belongs to the section "Intracellular and Plasma Membranes".

Deadline for manuscript submissions: closed (30 December 2023) | Viewed by 3097

Special Issue Editors

Laboratory of Cytoskeleton and Cilia Biology, Nencki Institute of Experimental Biology, Polish Academy of Sciences, 3 Pasteur Street, 02-093 Warsaw, Poland
Interests: cytoskeleton; flagella; cilia; centrosome; centriole; basal body; microtubules; tubulin posttranslational modifications

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Guest Editor
Laboratory of Cytoskeleton and Cilia Biology, Nencki Institute of Experimental Biology, Polish Academy of Sciences, 3 Pasteur Street, 02-093 Warsaw, Poland
Interests: tubulin; non-microtubular tubulins; tubulin posttranslational modifications; basal body; centriole; cilia; flagella

Special Issue Information

Dear Colleagues,

In different cell types, or even within specific cell regions, the organization of microtubules can have different levels of sophistication. Microtubules can vary from a network of cytoplasmic microtubules or bundles of filaments supporting intracellular transport and cell shape to complex structures enabling cell division or serving as scaffolds of the centriole, basal body, and cilium. The formation, maintenance, and remodeling of such diverse microtubular assemblies is strictly regulated and involves numerous factors, including tubulin post translational modifications and microtubule-interacting proteins. In recent years, a number of excellent studies significantly improved our understanding of  the structure, dynamics and function of microtubules.

This Special Issue of Cells intends to gather publications that present cutting-edge research in the field. We call for manuscripts, either in the form of original research articles, short communications, or reviews, which are related to the following topics: the organization and regulation of microtubular cytoskeleton in organisms from various eukaryotic clades (animals, plants, fungi, protists); intracellular transport and motor proteins; the role of microtubules in cell motility, division, senescence and carcinogenesis; and intrinsic (tubulin isotypes, posttranslational modifications, microtubule interacting proteins) and extrinsic factors (drugs) affecting microtubule dynamics, including potential anti-cancer agents.

Dr. Dorota Włoga
Dr. Ewa Joachimiak
Guest Editors

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Keywords

  • tubulin
  • microtubule
  • microtubule organization
  • tubulin posttranslational modifications
  • microtubule interacting proteins
  • mitotic and meiotic spindle
  • centriole
  • basal body
  • cilium
  • microtubules in cancer
  • anti-cancer drugs

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Published Papers (1 paper)

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Research

22 pages, 4585 KiB  
Article
Cfap91-Dependent Stability of the RS2 and RS3 Base Proteins and Adjacent Inner Dynein Arms in Tetrahymena Cilia
by Marta Bicka, Ewa Joachimiak, Paulina Urbanska, Anna Osinka, Anna Konopka, Ewa Bulska and Dorota Wloga
Cells 2022, 11(24), 4048; https://doi.org/10.3390/cells11244048 - 14 Dec 2022
Cited by 9 | Viewed by 2612
Abstract
Motile cilia and eukaryotic flagella are specific cell protrusions that are conserved from protists to humans. They are supported by a skeleton composed of uniquely organized microtubules—nine peripheral doublets and two central singlets (9 × 2 + 2). Microtubules also serve as docking [...] Read more.
Motile cilia and eukaryotic flagella are specific cell protrusions that are conserved from protists to humans. They are supported by a skeleton composed of uniquely organized microtubules—nine peripheral doublets and two central singlets (9 × 2 + 2). Microtubules also serve as docking sites for periodically distributed multiprotein ciliary complexes. Radial spokes, the T-shaped ciliary complexes, repeat along the outer doublets as triplets and transduce the regulatory signals from the cilium center to the outer doublet-docked dynein arms. Using the genetic, proteomic, and microscopic approaches, we have shown that lack of Tetrahymena Cfap91 protein affects stable docking/positioning of the radial spoke RS3 and the base of RS2, and adjacent inner dynein arms, possibly due to the ability of Cfap91 to interact with a molecular ruler protein, Ccdc39. The localization studies confirmed that the level of RS3-specific proteins, Cfap61 and Cfap251, as well as RS2-associated Cfap206, are significantly diminished in Tetrahymena CFAP91-KO cells. Cilia of Tetrahymena cells with knocked-out CFAP91 beat in an uncoordinated manner and their beating frequency is dramatically reduced. Consequently, CFAP91-KO cells swam about a hundred times slower than wild-type cells. We concluded that Tetrahymena Cfap91 localizes at the base of radial spokes RS2 and RS3 and likely plays a role in the radial spoke(s) positioning and stability. Full article
(This article belongs to the Special Issue Microtubules: Organization, Dynamics and Functions)
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