ArticleThe Journal of cell biology2012
Mena binds α5 integrin directly and modulates α5β1 function.
Article in The Journal of cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers, 1 of them a synthesis that pooled it.
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
39 citing papers in PubMed, 1 synthesis or guideline pooled it, 61 citations in OpenAlex.
- The possible role of Mena protein and its splicing-derived variants in embryogenesis, carcinogenesis, and tumor invasion: a systematic review of the literature.BioMed research international · 2013Pooled it
- The mammalian actin elongation factor ENAH/MENA contributes to autophagosome formation via its actin regulatory function.Autophagy · 2024Article
- Review
- The role of matrix stiffness in breast cancer progression: a review.Frontiers in oncology · 2023Review
- Local mRNA translation and cytoskeletal reorganization: Mechanisms that tune neuronal responses.Frontiers in molecular neuroscience · 2022Review
- Cell surface integrin α5ß1 clustering negatively regulates receptor tyrosine kinase signaling in colorectal cancer cells via glycogen synthase kinase 3.Integrative biology : quantitative biosciences from nano to macro · 2021Article
- Fibronectin as a multiregulatory molecule crucial in tumor matrisome: from structural and functional features to clinical practice in oncology.Journal of experimental & clinical cancer research : CR · 2021Review
- Actin Cytoskeleton and Regulation of TGFβ Signaling: Exploring Their Links.Biomolecules · 2021Review
- Loss of Ena/VASP interferes with lamellipodium architecture, motility and integrin-dependent adhesion.eLife · 2020Article
- Scaffold stiffness influences breast cancer cell invasion via EGFR-linked Mena upregulation and matrix remodeling.Matrix biology : journal of the International Society for Matrix Biology · 2020Article
- Tumor Cellular and Microenvironmental Cues Controlling Invadopodia Formation.Frontiers in cell and developmental biology · 2020Review
- Mechanical Cues Affect Migration and Invasion of Cells From Three Different Directions.Frontiers in cell and developmental biology · 2020Review
- Mechanosensing during directed cell migration requires dynamic actin polymerization at focal adhesions.The Journal of cell biology · 2019Article
- Integrin α5β1 regulates PP2A complex assembly through PDE4D in atherosclerosis.The Journal of clinical investigation · 2019Article
- Every step of the way: integrins in cancer progression and metastasis.Nature reviews. Cancer · 2018Review
- Nischarin regulates focal adhesion and Invadopodia formation in breast cancer cells.Molecular cancer · 2018Article
- Review
- A Requirement for Mena, an Actin Regulator, in Local mRNA Translation in Developing Neurons.Neuron · 2017Article
- Tumor Cell Invadopodia: Invasive Protrusions that Orchestrate Metastasis.Trends in cell biology · 2017Review
- Blood vessel endothelium-directed tumor cell streaming in breast tumors requires the HGF/C-Met signaling pathway.Oncogene · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Mena is an Ena/VASP family actin regulator with roles in cell migration, chemotaxis, cell-cell adhesion, tumor cell invasion, and metastasis. Although enriched in focal adhesions, Mena has no established function within these structures. We find that Mena forms an adhesion-regulated complex with α5β1 integrin, a fibronectin receptor involved in cell adhesion, motility, fibronectin fibrillogenesis, signaling, and growth factor receptor trafficking. Mena bound directly to the carboxy-terminal portion of the α5 cytoplasmic tail via a 91-residue region containing 13 five-residue "LERER" repeats. In fibroblasts, the Mena-α5 complex was required for "outside-in" α5β1 functions, including normal phosphorylation of FAK and paxillin and formation of fibrillar adhesions. It also supported fibrillogenesis and cell spreading and controlled cell migration speed. Thus, fibroblasts require Mena for multiple α5β1-dependent processes involving bidirectional interactions between the extracellular matrix and cytoplasmic focal adhesion proteins.
Indexed as
Identifiers
What OpenQuestion holds
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.