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Biomolecules
Special Issues
Molecular Functions of Microtubules
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Special Issue "Molecular Functions of Microtubules"

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Molecular Biophysics".

Deadline for manuscript submissions: 20 May 2023 | Viewed by 1696

Special Issue Editor

Dr. Scott Forth

E-Mail Website
Guest Editor
Department of Biological Sciences, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA
Interests: microtubule; optics and photonics; optics and lasers; optical imaging; fluorescence imaging; cell mechanics; microscopy

Special Issue Information

Dear Colleagues,

The microtubule cytoskeleton provides cells with structural support, a means to perform mechanical work, cargo tracks for directional transport of vesicles and organelles, and a mechanism to segregate chromosomes during mitosis. To accomplish this wide array of tasks, microtubules are regulated by a host of motor and non-motor proteins, as well as directly modified via post-translational modifications. These factors alter microtubule polymerization dynamics, define new sites of nucleation, remodel filaments, and organize higher-order microtubule network architectures. Structural, biochemical, in vitro reconstitution, theoretical, and cell-based studies over the past few years have revealed many novel mechanisms by which microtubule function is regulated and have opened up new and exciting avenues of inquiry. Original manuscripts and reviews dealing with any and all aspects of molecular regulation of microtubules are solicited and welcome.

Dr. Scott Forth
Guest Editor

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 submissions that pass pre-check are 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. Biomolecules is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2300 CHF (Swiss Francs). 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

  • cytoskeleton
  • microtubule structure
  • microtubule-associated proteins
  • motor proteins
  • microtubule polymerization dynamics
  • microtubule post-translational modifications
  • microtubules in disease
  • microtubule networks
  • directional transport
  • modeling microtubules

Published Papers (2 papers)

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Research

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Article
Mechanistic Analysis of CCP1 in Generating ΔC2 α-Tubulin in Mammalian Cells and Photoreceptor Neurons
by
Takashi Hotta
,
Alexandra Plemmons
,
Margo Gebbie
,
Trevor A. Ziehm
,
Teresa Lynne Blasius
,
Craig Johnson
,
Kristen J. Verhey
,
Jillian N. Pearring
and
Ryoma Ohi
Biomolecules 2023, 13(2), 357; https://doi.org/10.3390/biom13020357 - 12 Feb 2023
Viewed by 676
Abstract
An important post-translational modification (PTM) of α-tubulin is the removal of amino acids from its C-terminus. Removal of the C-terminal tyrosine residue yields detyrosinated α-tubulin, and subsequent removal of the penultimate glutamate residue produces ΔC2-α-tubulin. These PTMs alter the ability of the α-tubulin [...] Read more.
An important post-translational modification (PTM) of α-tubulin is the removal of amino acids from its C-terminus. Removal of the C-terminal tyrosine residue yields detyrosinated α-tubulin, and subsequent removal of the penultimate glutamate residue produces ΔC2-α-tubulin. These PTMs alter the ability of the α-tubulin C-terminal tail to interact with effector proteins and are thereby thought to change microtubule dynamics, stability, and organization. The peptidase(s) that produces ΔC2-α-tubulin in a physiological context remains unclear. Here, we take advantage of the observation that ΔC2-α-tubulin accumulates to high levels in cells lacking tubulin tyrosine ligase (TTL) to screen for cytosolic carboxypeptidases (CCPs) that generate ΔC2-α-tubulin. We identify CCP1 as the sole peptidase that produces ΔC2-α-tubulin in TTLΔ HeLa cells. Interestingly, we find that the levels of ΔC2-α-tubulin are only modestly reduced in photoreceptors of ccp1−/− mice, indicating that other peptidases act synergistically with CCP1 to produce ΔC2-α-tubulin in post-mitotic cells. Moreover, the production of ΔC2-α-tubulin appears to be under tight spatial control in the photoreceptor cilium: ΔC2-α-tubulin persists in the connecting cilium of ccp1−/− but is depleted in the distal portion of the photoreceptor. This work establishes the groundwork to pinpoint the function of ΔC2-α-tubulin in proliferating and post-mitotic mammalian cells. Full article
(This article belongs to the Special Issue Molecular Functions of Microtubules)
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Review

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Review
Computational Approaches to the Rational Design of Tubulin-Targeting Agents
by
Helena Pérez-Peña
,
Anne-Catherine Abel
,
Maxim Shevelev
,
Andrea E. Prota
,
Stefano Pieraccini
and
Dragos Horvath
Biomolecules 2023, 13(2), 285; https://doi.org/10.3390/biom13020285 - 02 Feb 2023
Viewed by 722
Abstract
Microtubules are highly dynamic polymers of α,β-tubulin dimers which play an essential role in numerous cellular processes such as cell proliferation and intracellular transport, making them an attractive target for cancer and neurodegeneration research. To date, a large number of known tubulin binders [...] Read more.
Microtubules are highly dynamic polymers of α,β-tubulin dimers which play an essential role in numerous cellular processes such as cell proliferation and intracellular transport, making them an attractive target for cancer and neurodegeneration research. To date, a large number of known tubulin binders were derived from natural products, while only one was developed by rational structure-based drug design. Several of these tubulin binders show promising in vitro profiles while presenting unacceptable off-target effects when tested in patients. Therefore, there is a continuing demand for the discovery of safer and more efficient tubulin-targeting agents. Since tubulin structural data is readily available, the employment of computer-aided design techniques can be a key element to focus on the relevant chemical space and guide the design process. Due to the high diversity and quantity of structural data available, we compiled here a guide to the accessible tubulin-ligand structures. Furthermore, we review different ligand and structure-based methods recently used for the successful selection and design of new tubulin-targeting agents. Full article
(This article belongs to the Special Issue Molecular Functions of Microtubules)
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