ArticleJournal of cell science2022
Integrin α6β4 requires plectin and vimentin for adhesion complex distribution and invasive growth.
Article in Journal of cell science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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The trial behind it
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
- AI-guided design of plectin-1-targetedJournal of nanobiotechnology · 2026Article
- Integrin-mediated mechanotransduction in the tumor microenvironment: macrophage-centered signaling mechanisms and immune remodeling.Journal of translational medicine · 2026Review
- Prenatal Identification of a NovelClinical case reports · 2026Article
- Phosphorylation of plectin by Akt3 promotes triple-negative breast cancer cell invasive migration.iScience · 2025Article
- Article
- How cytoskeletal crosstalk makes cells move: Bridging cell-free and cell studies.Biophysics reviews · 2024Review
- The mechanism of ITGB4 in tumor migration and invasion.Frontiers in oncology · 2024Review
- Activation of GRP78 ATPase suppresses A549 lung cancer cell migration by promoting ITGB4 degradation.Cell adhesion & migration · 2022Article
- Ancient Origins of Cytoskeletal Crosstalk: Spectraplakin-like Proteins Precede the Emergence of Cortical Microtubule Stabilization Complexes as Crosslinkers.International journal of molecular sciences · 2022Article
- Integrin α6β4 signals through DNA damage response pathway to sensitize breast cancer cells to cisplatin.Frontiers in oncology · 2022Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Integrin α6β4 binds plectin to associate with vimentin; however, the biological function remains unclear. Here, we utilized various integrin β4 mutants and CRISPR-Cas9 editing to investigate this association. Upon laminin binding, integrin α6β4 distinctly distributed peripherally as well as centrally, proximal to the nucleus. Upon fibronectin addition, integrin α6β4 was centrally recruited to large focal adhesions (FAs) and enhanced Fak (also known as PTK2) phosphorylation. Integrin β4 plectin-binding mutants or genetic deletion of plectin inhibited β4 recruitment to FAs and integrin α6β4-enhanced cell spreading, migration and three-dimensional invasive growth. Loss of the β4 signaling domain (but retaining plectin binding) blocked migration and invasiveness but not cell spreading, recruitment to FAs or colony growth. Immunostaining revealed that integrin α6β4 redistributed vimentin perinuclearly, where it colocalized with plectin and FAs. Depletion of vimentin completely blocked integrin β4-enhanced invasive growth, Fak phosphorylation and proliferation in three dimensions but not two dimensions. In summary, we demonstrate the essential roles of plectin and vimentin in promoting an invasive phenotype downstream of integrin α6β4. This article has an associated First Person interview with the first author of the paper.
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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.