ArticleProteomics2012
Proteomic analysis of α4β1 integrin adhesion complexes reveals α-subunit-dependent protein recruitment.
Article in Proteomics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed, 55 citations in OpenAlex.
- Mena regulates nesprin-2 to control actin-nuclear lamina associations, trans-nuclear membrane signalling and gene expression.Nature communications · 2023Article
- Characterisation of a nucleo-adhesome.Nature communications · 2022Article
- α4/α9 Integrins Coordinate Epithelial Cell Migration Through Local Suppression of MAP Kinase Signaling Pathways.Frontiers in cell and developmental biology · 2021Article
- Basement membrane ligands initiate distinct signalling networks to direct cell shape.Matrix biology : journal of the International Society for Matrix Biology · 2020Article
- c-MYC regulates mRNA translation efficiency and start-site selection in lymphoma.The Journal of experimental medicine · 2019Article
- Steps in Mechanotransduction Pathways that Control Cell Morphology.Annual review of physiology · 2019Review
- Cell surface nucleolin interacts with and internalizes Bothrops asper Lys49 phospholipase AScientific reports · 2018Article
- Integrin signaling in atherosclerosis.Cellular and molecular life sciences : CMLS · 2017Review
- Analyzing Cell Surface Adhesion Remodeling in Response to Mechanical Tension Using Magnetic Beads.Journal of visualized experiments : JoVE · 2017Article
- The integrin adhesome network at a glance.Journal of cell science · 2016Review
- Adhesion protein networks reveal functions proximal and distal to cell-matrix contacts.Current opinion in cell biology · 2016Review
- Rationalising the role of Keratin 9 as a biomarker for Alzheimer's disease.Scientific reports · 2016Article
- Modulation of FAK and Src adhesion signaling occurs independently of adhesion complex composition.The Journal of cell biology · 2016Article
- The enzyme L-isoaspartyl (D-aspartyl) methyltransferase is required for VEGF-dependent endothelial cell migration and tubulogenesis.Molecular and cellular biochemistry · 2016Article
- Definition of a consensus integrin adhesome and its dynamics during adhesion complex assembly and disassembly.Nature cell biology · 2015Article
- Isolation of integrin-based adhesion complexes.Current protocols in cell biology · 2015Article
- Defining the phospho-adhesome through the phosphoproteomic analysis of integrin signalling.Nature communications · 2015Article
- A proteomic approach reveals integrin activation state-dependent control of microtubule cortical targeting.Nature communications · 2015Article
- SP-R210 (Myo18A) Isoforms as Intrinsic Modulators of Macrophage Priming and Activation.PloS one · 2015Article
- The importance of podocyte adhesion for a healthy glomerulus.Frontiers in endocrinology · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Integrin adhesion receptors mediate cell-cell and cell-extracellular matrix interactions, which control cell morphology and migration, differentiation, and tissue integrity. Integrins recruit multimolecular adhesion complexes to their cytoplasmic domains, which provide structural and mechanosensitive signaling connections between the extracellular and intracellular milieux. The different functions of specific integrin heterodimers, such as α4β1 and α5β1, have been attributed to distinct signal transduction mechanisms that are initiated by selective recruitment of adhesion complex components to integrin cytoplasmic tails. Here, we report the isolation of ligand-induced adhesion complexes associated with wild-type α4β1 integrin, an activated α4β1 variant in the absence of the α cytoplasmic domain (X4C0), and a chimeric α4β1 variant with α5 leg and cytoplasmic domains (α4Pα5L), and the cataloguing of their proteomes by MS. Using hierarchical clustering and interaction network analyses, we detail the differential recruitment of proteins and highlight enrichment patterns of proteins to distinct adhesion complexes. We identify previously unreported components of integrin adhesion complexes and observe receptor-specific enrichment of molecules with previously reported links to cell migration and cell signaling processes. Furthermore, we demonstrate colocalization of MYO18A with active integrin in migrating cells. These datasets provide a resource for future studies of integrin receptor-specific signaling events.
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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.