ArticleJournal of cell science2013
Phosphorylation of serine 4,642 in the C-terminus of plectin by MNK2 and PKA modulates its interaction with intermediate filaments.
Article in Journal of cell science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 35 citations in OpenAlex.
- Regulation of mechanical intercellular junctions and components of the mitochondrial electron transport chain and the TCA cycle in the hypertrophic heart by pyridostigmine or trandolapril.Frontiers in molecular biosciences · 2026Article
- Phosphorylation of plectin by Akt3 promotes triple-negative breast cancer cell invasive migration.iScience · 2025Article
- Mechanics of cell sheets: plectin as an integrator of cytoskeletal networks.Open biology · 2025Review
- Desmoplakin CSM models unravel mechanisms regulating the binding to intermediate filaments and putative therapeutics for cardiocutaneous diseases.Scientific reports · 2024Article
- PP2A-B55alpha controls keratinocyte adhesion through dephosphorylation of the Desmoplakin C-terminus.Scientific reports · 2023Article
- Proteomics of Plasma and Plasma-Treated Podocytes: Application to Focal and Segmental Glomerulosclerosis.International journal of molecular sciences · 2023Article
- Review
- MNK Proteins as Therapeutic Targets in Leukemia.OncoTargets and therapy · 2023Review
- Plectin pulls it together, coupling the cortical actin and intermediate filament cytoskeletons.The Journal of cell biology · 2022Article
- Regulation of intestinal epithelial intercellular adhesion and barrier function by desmosomal cadherin desmocollin-2.Molecular biology of the cell · 2021Article
- SUMOylation of periplakin is critical for efficient reorganization of keratin filament network.Molecular biology of the cell · 2019Article
- Specter: linear deconvolution for targeted analysis of data-independent acquisition mass spectrometry proteomics.Nature methods · 2018Article
- Mammalian Plakins, Giant Cytolinkers: Versatile Biological Functions and Roles in Cancer.International journal of molecular sciences · 2018Review
- Article
- Intermediate Filaments and the Plasma Membrane.Cold Spring Harbor perspectives in biology · 2017Review
- GSK3- and PRMT-1-dependent modifications of desmoplakin control desmoplakin-cytoskeleton dynamics.The Journal of cell biology · 2015Article
- Article
- Interaction of plectin with keratins 5 and 14: dependence on several plectin domains and keratin quaternary structure.The Journal of investigative dermatology · 2014Article
- Mnk kinase pathway: Cellular functions and biological outcomes.World journal of biological chemistry · 2014Review
- Plakins, a versatile family of cytolinkers: roles in skin integrity and in human diseases.The Journal of investigative dermatology · 2014Review
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Plectin is a versatile cytolinker of the plakin family conferring cell resilience to mechanical stress in stratified epithelia and muscles. It acts as a critical organizer of the cytoskeletal system by tethering various intermediate filament (IF) networks through its C-terminal IF-binding domain (IFBD). Mutations affecting the IFBD cause devastating human diseases. Here, we show that serine 4642, which is located in the extreme C-terminus of plectin, is phosphorylated in different cell lines. Phosphorylation of S4642 decreased the ability of plectin IFBD to associate with various IFs, as assessed by immunofluorescence microscopy and cell fractionation studies, as well as in yeast two-hybrid assays. Plectin phosphorylated at S4642 was reduced at sites of IF network anchorage along cell-substrate contacts in both skin and cultured keratinocytes. Treatment of SK-MEL-2 and HeLa cells with okadaic acid increased plectin S4642 phosphorylation, suggesting that protein phosphatase 2A dephosphorylates this residue. Moreover, plectin S4642 phosphorylation was enhanced after cell treatment with EGF, phorbol ester, sorbitol and 8-bromo-cyclic AMP, as well as during wound healing and protease-mediated cell detachment. Using selective protein kinase inhibitors, we identified two different kinases that modulate the phosphorylation of plectin S4642 in HeLa cells: MNK2, which is downstream of the ERK1/2-dependent MAPK cascade, and PKA. Our study indicates that phosphorylation of S4642 has an important regulatory role in the interaction of plectin with IFs and identifies a novel link between MNK2 and the cytoskeleton.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.