ArticleThe Journal of cell biology2006
Genetic analysis of beta1 integrin "activation motifs" in mice.
Article in The Journal of cell biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
What it found
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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
58 citing papers in PubMed, 98 citations in OpenAlex.
- Kindlins regulate integrin- and growth factor-dependent ureteric bud formation.Development (Cambridge, England) · 2026Article
- The phosphatase PPM1F, a negative regulator of integrin activity, is essential for embryonic development and controls tumor cell invasion.BMC biology · 2025Article
- Dynamic regulation of integrin β1 phosphorylation supports invasion of breast cancer cells.Nature cell biology · 2025Article
- Ligand-independent integrin β1 signaling supports lung adenocarcinoma development.JCI insight · 2022Article
- New insights into the phosphorylation of the threonine motif of the β1 integrin cytoplasmic domain.Life science alliance · 2022Article
- PPM1F controls integrin activity via a conserved phospho-switch.The Journal of cell biology · 2020Article
- Cellular tension encodes local Src-dependent differential βMolecular biology of the cell · 2019Article
- A Novel Mutation in an NPXY Motif of β Integrin Reveals Phenotypes Similar toFrontiers in cell and developmental biology · 2019Article
- On the contributing role of the transmembrane domain for subunit-specific sensitivity of integrin activation.Scientific reports · 2018Article
- β1-integrin-matrix interactions modulate cerebral microvessel endothelial cell tight junction expression and permeability.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2018Article
- Talin regulates integrin β1-dependent and -independent cell functions in ureteric bud development.Development (Cambridge, England) · 2017Article
- Article
- The dual structural roles of the membrane distal region of the α-integrin cytoplasmic tail during integrin inside-out activation.Journal of cell science · 2015Article
- Contributions of the integrin β1 tail to cell adhesive forces.Experimental cell research · 2015Article
- The interaction between uPAR and vitronectin triggers ligand-independent adhesion signalling by integrins.The EMBO journal · 2014Article
- The talin head domain reinforces integrin-mediated adhesion by promoting adhesion complex stability and clustering.PLoS genetics · 2014Article
- The late endosomal p14-MP1 (LAMTOR2/3) complex regulates focal adhesion dynamics during cell migration.The Journal of cell biology · 2014Article
- Podocyte-associated talin1 is critical for glomerular filtration barrier maintenance.The Journal of clinical investigation · 2014Article
- Integrin cytoplasmic tail interactions.Biochemistry · 2014Review
- β1 integrins with individually disrupted cytoplasmic NPxY motifs are embryonic lethal but partially active in the epidermis.The Journal of investigative dermatology · 2013Article
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 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Akey feature of integrins is their ability to regulate the affinity for ligands, a process termed integrin activation. The final step in integrin activation is talin binding to the NPXY motif of the integrin beta cytoplasmic domains. Talin binding disrupts the salt bridge between the alpha/beta tails, leading to tail separation and integrin activation. We analyzed mice in which we mutated the tyrosines of the beta1 tail and the membrane-proximal aspartic acid required for the salt bridge. Tyrosine-to-alanine substitutions abolished beta1 integrin functions and led to a beta1 integrin-null phenotype in vivo. Surprisingly, neither the substitution of the tyrosines with phenylalanine nor the aspartic acid with alanine resulted in an obvious defect. These data suggest that the NPXY motifs of the beta1 integrin tail are essential for beta1 integrin function, whereas tyrosine phosphorylation and the membrane-proximal salt bridge between alpha and beta1 tails have no apparent function under physiological conditions in vivo.
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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.