ArticleMolecular biology of the cell2013
Intermediate filament-associated cytolinker plectin 1c destabilizes microtubules in keratinocytes.
Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
28 citing papers in PubMed.
- Characterization of multiple binding sites on microtubule associated protein 2c recognized by dimeric and monomeric 14-3-3ζ.The FEBS journal · 2025Article
- Plectin, a novel regulator in migration, invasion and adhesion of ovarian cancer.Cell & bioscience · 2025Article
- Mechanics of cell sheets: plectin as an integrator of cytoskeletal networks.Open biology · 2025Review
- MAP2 phosphorylation: mechanisms, functional consequences, and emerging insights.Frontiers in cellular neuroscience · 2025Review
- Regulation of Kinase Signaling Pathways by α6β4-Integrins and Plectin in Prostate Cancer.Cancers · 2022Review
- Junctional epithelium and hemidesmosomes: Tape and rivets for solving the "percutaneous device dilemma" in dental and other permanent implants.Bioactive materials · 2022Review
- Intermediate Filaments in Cellular Mechanoresponsiveness: Mediating Cytoskeletal Crosstalk From Membrane to Nucleus and Back.Frontiers in cell and developmental biology · 2022Review
- Review
- Review
- Plectin dysfunction in neurons leads to tau accumulation on microtubules affecting neuritogenesis, organelle trafficking, pain sensitivity and memory.Neuropathology and applied neurobiology · 2021Article
- Review
- Scaling up single-cell mechanics to multicellular tissues - the role of the intermediate filament-desmosome network.Journal of cell science · 2020Review
- The plakin domain ofDevelopment (Cambridge, England) · 2019Article
- Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences.Biomolecules · 2019Review
- Functionally specific binding regions of microtubule-associated protein 2c exhibit distinct conformations and dynamics.The Journal of biological chemistry · 2018Article
- Mammalian Plakins, Giant Cytolinkers: Versatile Biological Functions and Roles in Cancer.International journal of molecular sciences · 2018Review
- The mechano-sensing role of the unique SH3 insertion in plakin domains revealed by Molecular Dynamics simulations.Scientific reports · 2017Article
- Quantitative mapping of microtubule-associated protein 2c (MAP2c) phosphorylation and regulatory protein 14-3-3ζ-binding sites reveals key differences between MAP2c and its homolog Tau.The Journal of biological chemistry · 2017Article
- Plectin is a novel regulator for apical extrusion of RasV12-transformed cells.Scientific reports · 2017Article
- Molecular Biology and Clinical Mitigation of Cancer Treatment-Induced Neuropathy.Clinical Medicine Insights. Oncology · 2016Review
Corrections and comments
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8 authors.
Funding
Abstract
The transition of microtubules (MTs) from an assembled to a disassembled state plays an essential role in several cellular functions. While MT dynamics are often linked to those of actin filaments, little is known about whether intermediate filaments (IFs) have an influence on MT dynamics. We show here that plectin 1c (P1c), one of the multiple isoforms of the IF-associated cytolinker protein plectin, acts as an MT destabilizer. We found that MTs in P1c-deficient (P1c(-/-)) keratinocytes are more resistant toward nocodazole-induced disassembly and display increased acetylation. In addition, live imaging of MTs in P1c(-/-), as well as in plectin-null, cells revealed decreased MT dynamics. Increased MT stability due to P1c deficiency led to changes in cell shape, increased velocity but loss of directionality of migration, smaller-sized focal adhesions, higher glucose uptake, and mitotic spindle aberrations combined with reduced growth rates of cells. On the basis of ex vivo and in vitro experimental approaches, we suggest a mechanism for MT destabilization in which isoform-specific binding of P1c to MTs antagonizes the MT-stabilizing and assembly-promoting function of MT-associated proteins through an inhibitory function exerted by plectin's SH3 domain. Our results open new perspectives on cytolinker-coordinated IF-MT interaction and its physiological significance.
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