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Microtubule Cytoskeleton, Motor Proteins, and Other Cytoskeleton-Associated Proteins

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (31 December 2025) | Viewed by 390

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Institute of Enzymology, Research Centre for Natural Sciences, ELKH, 1117 Budapest, Hungary
Interests: cytoskeleton; GPCR; protein–protein interaction; Parkinson’s disease; cancer
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

This Special Issue invites original research articles, reviews, and short communications focusing on the Microtubule Cytoskeleton, Motor Proteins, and Other Cytoskeleton-Associated Proteins. Manuscripts should aim to elucidate the fundamental organization, assembly, and dynamic behavior of microtubules, while clarifying the mechanistic roles of motor proteins—such as kinesins and dyneins—in facilitating intracellular transport. In addition, authors are encouraged to explore the contributions of other cytoskeletal proteins to the regulation of structural integrity and cellular signaling. Topics may encompass cellular processes like mitosis, cell migration, and polarity, as well as insights into how disruptions in cytoskeletal organization can lead to disease. We welcome studies that employ advanced experimental techniques, high-resolution imaging, biochemical assays, and computational modeling to provide a comprehensive understanding of cytoskeletal regulation. This Special Issue seeks to bridge the gap between basic cellular insights and their translational applications, advancing our knowledge of cytoskeletal function and its impact on cell physiology and pathology.

Dr. Tibor Szénási
Guest Editor

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Keywords

  • microtubule cytoskeleton
  • motor proteins (kinesins and dyneins)
  • cytoskeleton-associated proteins
  • cytoskeletal “cross-talk”
  • intracellular transport
  • cellular signaling and regulation
  • cellular processes (mitosis, migration, and polarity)

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Published Papers (1 paper)

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Research

20 pages, 5392 KB  
Article
Cyclin D1/D2–CDK4 Drives Cell Migration by Orchestrating Cytoskeletal Dynamics Through a TGFβ–FAK–Rac1 Axis
by Ruifang Guo, Yihang Wang, Aiwen Zhang, Siwanon Jirawatnotai, Chen Chu and Lijun Liu
Int. J. Mol. Sci. 2026, 27(3), 1228; https://doi.org/10.3390/ijms27031228 - 26 Jan 2026
Viewed by 99
Abstract
Beyond their canonical role in promoting G1/S progression, the complexes formed by cyclin D and cyclin-dependent kinase (CDK) 4/6 have emerged as contributors to enhanced cell migration. However, a direct link between this complex and cytoskeletal remodeling during cell motility has remained poorly [...] Read more.
Beyond their canonical role in promoting G1/S progression, the complexes formed by cyclin D and cyclin-dependent kinase (CDK) 4/6 have emerged as contributors to enhanced cell migration. However, a direct link between this complex and cytoskeletal remodeling during cell motility has remained poorly understood. Here, we show that CDK4/6 inhibition in HeLa cells disrupts lamellipodia formation and subsequent focal adhesion assembly, leading to a reduction in cell migration and invasion. Notably, CDK4, but not CDK6, in complex with cyclin D1/D2, localizes to membrane ruffles to facilitate cytoskeletal reorganization. Mechanistically, proteomic and phosphoproteomic analyses revealed that CDK4 inhibition attenuates the transforming growth factor β (TGFβ) pathway via reduced Smad3 phosphorylation at Thr8, downregulating integrin subunits (α5, α6, and β1). Furthermore, CDK4 inhibition significantly decreased focal adhesion kinase (FAK) phosphorylation at Tyr397 and Rac1-GTP levels. Importantly, the resulting migration defect was largely restored by activation of either Rac1 or FAK. Thus, our data support a model in which cyclin D1/D2–CDK4 promotes phosphorylation of Smad3, leading to upregulation of integrin subunits, activation of FAK and Rac1, and consequent lamellipodia formation and cell migration. These findings provide direct evidence that CDK4 regulates actin cytoskeletal reorganization during cell migration and suggest that CDK4/6 inhibitors may dampen cytoskeleton-dependent tumor invasion, in addition to their antiproliferative effects. Full article
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