ArticleThe Journal of biological chemistry2011
Tyrosine phosphorylation as a conformational switch: a case study of integrin β3 cytoplasmic tail.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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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
19 citing papers in PubMed, 29 citations in OpenAlex.
- Alteration of CD40 Protein Expression by Tyrosine Phosphorylation of the NF-κB p50 Subunit.Chembiochem : a European journal of chemical biology · 2026Article
- Pleiotrophin Activates cMet- and mTORC1-Dependent Protein Synthesis through PTPRZ1-The Role of αInternational journal of molecular sciences · 2024Article
- The Role of the Microenvironment and Cell Adhesion Molecules in Chronic Lymphocytic Leukemia.Cancers · 2023Review
- Genetic deletion or tyrosine phosphatase inhibition of PTPRZ1 activates c-Met to up-regulate angiogenesis and lung adenocarcinoma growth.International journal of cancer · 2023Article
- Balanced Force Field ff03CMAP Improving the Dynamics Conformation Sampling of Phosphorylation Site.International journal of molecular sciences · 2022Article
- The MemMoRF database for recognizing disordered protein regions interacting with cellular membranes.Nucleic acids research · 2021Article
- The identification of nuclear αvβ3 integrin in ovarian cancer: non-paradigmal localization with cancer promoting actions.Oncogenesis · 2020Article
- Acquired resistance to temsirolimus is associated with integrin α7 driven chemotactic activity of renal cell carcinomaOncotarget · 2018Article
- Nanodiscs and Solution NMR: preparation, application and challenges.Nanotechnology reviews · 2017Article
- Integrin bondage: filamin takes control.Nature structural & molecular biology · 2015Article
- Phospho-Tyrosine(s) vs. Phosphatidylinositol Binding in Shc Mediated Integrin Signaling.American journal of molecular biology · 2015Article
- Article
- Distinct functions for Rap1 signaling in vascular morphogenesis and dysfunction.Experimental cell research · 2013Review
- Site-specific NMR mapping and time-resolved monitoring of serine and threonine phosphorylation in reconstituted kinase reactions and mammalian cell extracts.Nature protocols · 2013Article
- Cell signaling, post-translational protein modifications and NMR spectroscopy.Journal of biomolecular NMR · 2012Article
- β1 integrin NPXY motifs regulate kidney collecting-duct development and maintenance by induced-fit interactions with cytosolic proteins.Molecular and cellular biology · 2012Article
- Resistance to the mTOR-inhibitor RAD001 elevates integrin α2- and β1-triggered motility, migration and invasion of prostate cancer cells.British journal of cancer · 2012Article
- Integrin αIIb-mediated PI3K/Akt activation in platelets.PloS one · 2012Article
- Integrin β3 crosstalk with VEGFR accommodating tyrosine phosphorylation as a regulatory switch.PloS one · 2012Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Reversible protein phosphorylation is vital for many fundamental cellular processes. The actual impact of adding and removing phosphate group(s) is 3-fold: changes in the local/global geometry, alterations in the electrostatic potential and, as the result of both, modified protein-target interactions. Here we present a comprehensive structural investigation of the effects of phosphorylation on the conformational as well as functional states of a crucial cell surface receptor, α(IIb)β(3) integrin. We have analyzed phosphorylated (Tyr(747) and Tyr(759)) β(3) integrin cytoplasmic tail (CT) primarily by NMR, and our data demonstrate that under both aqueous and membrane-mimetic conditions, phosphorylation causes substantial conformational rearrangements. These changes originate from novel ionic interactions and revised phospholipid binding. Under aqueous conditions, the critical Tyr(747) phosphorylation prevents β(3)CT from binding to its heterodimer partner α(IIb)CT, thus likely maintaining an activated state of the receptor. This conclusion was tested in vivo and confirmed by integrin-dependent endothelial cells adhesion assay. Under membrane-mimetic conditions, phosphorylation results in a modified membrane embedding characterized by significant changes in the secondary structure pattern and the overall fold of β(3)CT. Collectively these data provide unique molecular insights into multiple regulatory roles of phosphorylation.
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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.