Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
9.4
4.8
Journals
Biomolecules
Special Issues
Advances in the Structure and Function of Microtubule-Associated Motor Proteins
share announcement

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 November 2025 | Viewed by 512

Special Issue Editor

Prof. Dr. Arne Gennerich

E-Mail Website
Guest Editor
Department of Biochemistry and Gruss Lipper Biophotonics Center, Albert Einstein College of Medicine, Bronx, NY 10461, USA
Interests: molecular mechanisms of microtubule-based motor proteins in health and disease; transcription elongation by RNA polymerases II and III; 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 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 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

Benefits of Publishing in a Special Issue

  • Ease of navigation: Grouping papers by topic helps scholars navigate broad scope journals more efficiently.
  • Greater discoverability: Special Issues support the reach and impact of scientific research. Articles in Special Issues are more discoverable and cited more frequently.
  • Expansion of research network: Special Issues facilitate connections among authors, fostering scientific collaborations.
  • External promotion: Articles in Special Issues are often promoted through the journal's social media, increasing their visibility.
  • Reprint: MDPI Books provides the opportunity to republish successful Special Issues in book format, both online and in print.

Further information on MDPI's Special Issue policies can be found here.

Published Papers (1 paper)

Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

18 pages, 4193 KiB  
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
Viewed by 352
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)
►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-1
Back to TopTop