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Biomolecules
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Advances in the Structure and Function of Microtubule-Associated Motor Proteins
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Advances in the Structure and Function of Microtubule-Associated Motor Proteins

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Molecular Biophysics: Structure, Dynamics, and Function".

Deadline for manuscript submissions: 20 May 2026 | Viewed by 4847

Special Issue Editor

Prof. Dr. Arne Gennerich

E-Mail Website
Guest Editor
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, USA
Interests: molecular mechanisms of microtubule-based motor proteins in health and disease; single-molecule biophysics, development and application of single-molecule technologies

Special Issue Information

Dear Colleagues,

Microtubule-associated motor proteins play fundamental roles in intracellular transport, cell division, and cytoskeletal organization. Kinesins and dyneins, the two major classes of these motors, drive these essential processes by generating force and directed motion along microtubules. Recent advances in cryo-electron microscopy, nanometer-precision fluorescence microscopy, and single-molecule biophysics have provided unprecedented insights into how these motors function and regulate their activities in response to cellular cues.

Despite these advances, critical questions remain regarding the molecular mechanisms of motor function, including cargo recognition and the effects of post-translational modifications and disease mutations. This Special Issue of Biomolecules aims to highlight recent progress in understanding the structure, mechanism, and regulation of microtubule-associated motor proteins. We welcome original research and review articles on the structure, motion, and force generation of motor proteins, as well as their allosteric regulation and the effects of post-translational modifications and disease-associated mutations on motor function.

We look forward to your contributions to this exciting collection.

Prof. Dr. Arne Gennerich
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 250 words) can be sent to the Editorial Office for assessment.

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 2700 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

  • microtubules
  • kinesin
  • dynein
  • CryoEM
  • post-translational modifications

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Published Papers (3 papers)

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Research

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21 pages, 3686 KB  
Article
Molecular Motors Orchestrate Pause-and-Run Dynamics to Facilitate Intracellular Transport
by Yusheng Shen and Kassandra M. Ori-McKenney
Biomolecules 2026, 16(2), 221; https://doi.org/10.3390/biom16020221 - 2 Feb 2026
Viewed by 425
Abstract
Intracellular transport is essential for cellular organization and function. This process is driven by molecular motors that ferry cargo along microtubules, but is characterized by intermittent motility, where cargoes switch between directed runs and prolonged pauses. The fundamental nature of these pauses has [...] Read more.
Intracellular transport is essential for cellular organization and function. This process is driven by molecular motors that ferry cargo along microtubules, but is characterized by intermittent motility, where cargoes switch between directed runs and prolonged pauses. The fundamental nature of these pauses has remained a mystery, specifically whether they are periods of motor detachment and passive drifting or states of active motor engagement. By combining single-particle tracking with large-scale motion analysis, we discovered that pauses are not passive. Instead, they are active, motor-driven states. We uncovered a unifying quantitative law: the diffusivity of a vesicle during a pause scales with the square of its velocity during a run. This parabolic relationship, Deff ∝ v2, holds true for both kinesin and dynein motors, different cargo types, and a variety of cellular perturbations. We show that this coupling arises because the number of engaged motors governs motility in both states. When we reduce motor engagement, vesicles move more slowly and become trapped in longer, less mobile pauses, collectively causing them to fail to reach their destination. Our work redefines transport pauses as an essential, motor-driven part of microtubule-based cargo delivery, revealing a quantitative principle that contributes to robust cargo transport through the crowded cellular environment. Full article
(This article belongs to the Special Issue Advances in the Structure and Function of Microtubule-Associated Motor Proteins)
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18 pages, 4193 KB  
Article
Distinct Clinical Phenotypes in KIF1A-Associated Neurological Disorders Result from Different Amino Acid Substitutions at the Same Residue in KIF1A
by Lu Rao, Wenxing Li, Yufeng Shen, Wendy K. Chung and Arne Gennerich
Biomolecules 2025, 15(5), 656; https://doi.org/10.3390/biom15050656 - 2 May 2025
Cited by 5 | Viewed by 2242
Abstract
KIF1A is a neuron-specific kinesin motor responsible for intracellular transport along axons. Pathogenic KIF1A mutations cause KIF1A-associated neurological disorders (KAND), a spectrum of severe neurodevelopmental and neurodegenerative conditions. While individual KIF1A mutations have been studied, how different substitutions at the same residue affect [...] Read more.
KIF1A is a neuron-specific kinesin motor responsible for intracellular transport along axons. Pathogenic KIF1A mutations cause KIF1A-associated neurological disorders (KAND), a spectrum of severe neurodevelopmental and neurodegenerative conditions. While individual KIF1A mutations have been studied, how different substitutions at the same residue affect motor function and disease progression remains unclear. Here, we systematically examine the molecular and clinical consequences of mutations at three key motor domain residues—R216, R254, and R307—using single-molecule motility assays and genotype–phenotype associations. We find that different substitutions at the same residue produce distinct molecular phenotypes, and that homodimeric mutant motor properties correlate with developmental outcomes. In addition, we present the first analysis of heterodimeric KIF1A motors—mimicking the heterozygous context in patients—and demonstrate that while heterodimers retain substantial motility, their properties are less predictive of clinical severity than homodimers. These results highlight the finely tuned mechanochemical properties of KIF1A and suggest that dysfunctional homodimers may disproportionately drive the diverse clinical phenotypes observed in KAND. By establishing residue-specific genotype–phenotype relationships, this work provides fundamental insights into KAND pathogenesis and informs targeted therapeutic strategies. Full article
(This article belongs to the Special Issue Advances in the Structure and Function of Microtubule-Associated Motor Proteins)
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Review

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30 pages, 16723 KB  
Review
Emerging Roles of Tubulin Isoforms and Their Post-Translational Modifications in Microtubule-Based Transport and Cellular Functions
by Aishwarya R. Nair, Nived Saroj and Ambarish Kunwar
Biomolecules 2026, 16(1), 81; https://doi.org/10.3390/biom16010081 - 4 Jan 2026
Viewed by 1592
Abstract
Microtubules are hollow cylindrical polymers made up of tubulin. This heterodimeric protein, tubulin, exists in multiple forms: tubulin isotypes and tubulin isoforms. Distinct α- and β-tubulin genes give rise to tubulin isotypes, which differ in their amino acid sequences and cellular [...] Read more.
Microtubules are hollow cylindrical polymers made up of tubulin. This heterodimeric protein, tubulin, exists in multiple forms: tubulin isotypes and tubulin isoforms. Distinct α- and β-tubulin genes give rise to tubulin isotypes, which differ in their amino acid sequences and cellular expression patterns. The tubulin post-translational modifications (PTMs) encode regulatory information within the microtubule lattice, modifying its biophysical characteristics and shaping interactions with motor proteins and microtubule-associated proteins. Different tubulin isotype compositions and post-translational modification patterns generate distinct tubulin isoforms. These isoforms are tissue-specific and regulate the functions of microtubules in specialized cells and cellular components such as cilia. Tubulin isoforms control cellular transport, regulate mechanosensitivity and shape the cytoskeleton, impacting the cellular functions and homeostasis. This review discusses the tubulin PTMs, including acetylation, methylation, palmitoylation, polyamination, glutamylation, glycylation, tyrosination, phosphorylation, SUMOylation, and ubiquitination, with emphasis on how isotype diversity and PTM-driven regulation together modulate microtubule behaviour, intracellular transport, and cellular functions. Full article
(This article belongs to the Special Issue Advances in the Structure and Function of Microtubule-Associated Motor Proteins)
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