ArticleBiochemistry2016
Phosphatidylinositol 4,5-Bisphosphate Modulates the Affinity of Talin-1 for Phospholipid Bilayers and Activates Its Autoinhibited Form.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 39 citations in OpenAlex.
- Molecular insights into profilin 1-dependent regulation of cellular phosphatidylinositol (4,5)-bisphosphate.Journal of cell science · 2026Article
- Molecular insights into Profilin1-dependent regulation of cellular phosphatidylinositol-(4,5)-bisphosphate.bioRxiv : the preprint server for biology · 2025Article
- Review
- Phosphoinositide signalling in cell motility and adhesion.Nature cell biology · 2025Review
- Focal adhesion in the tumour metastasis: from molecular mechanisms to therapeutic targets.Biomarker research · 2025Review
- A single-particle analysis method for detecting membrane remodelling and curvature sensing.Journal of cell science · 2024Article
- Review
- Defects in integrin complex formation promoteLife science alliance · 2024Article
- Membrane-induced 2D phase separation of the focal adhesion protein talin.Nature communications · 2024Article
- Long-term depression in neurons involves temporal and ultra-structural dynamics of phosphatidylinositol-4,5-bisphosphate relying on PIP5K, PTEN and PLC.Communications biology · 2023Article
- Talin‑1 interaction network in cellular mechanotransduction (Review).International journal of molecular medicine · 2022Review
- Structures and Dynamics of Anionic Lipoprotein Nanodiscs.The journal of physical chemistry. B · 2022Article
- Avian Hepatitis E Virus ORF2 Protein Interacts with Rap1b to Induce Cytoskeleton Rearrangement That Facilitates Virus Internalization.Microbiology spectrum · 2022Article
- β2 integrin activation and signal transduction in leukocyte recruitment.American journal of physiology. Cell physiology · 2021Review
- Nanodiscs: A toolkit for membrane protein science.Protein science : a publication of the Protein Society · 2021Review
- Fluorescence Correlation Spectroscopy Reveals Interaction of Some Microdomain-Associated Lipids with Cellular Focal Adhesion Sites.International journal of molecular sciences · 2020Article
- Dark, Ultra-Dark and Ultra-Bright Nanodiscs for membrane protein investigations.Analytical biochemistry · 2020Article
- The F1 loop of the talin head domain acts as a gatekeeper in integrin activation and clustering.Journal of cell science · 2020Article
- A distinct talin2 structure directs isoform specificity in cell adhesion.The Journal of biological chemistry · 2020Article
- Talin1 controls dendritic cell activation by regulating TLR complex assembly and signaling.The Journal of experimental medicine · 2020Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Integrins are vital transmembrane receptors that mediate cell-cell and cell-extracellular matrix interactions and signaling. Talin is a 270 kDa protein and is considered a key regulator of integrin activity. The interaction between talin and integrin is commonly regarded as the final step of inside-out activation. In the cytosol, talin adopts an autoinhibited conformation, in which the C-terminal rod domain binds the N-terminal head domain, preventing the interactions of the head domain with the membrane surface and the integrin cytoplasmic domain. It has long been suggested that the presence of phosphatidylinositol 4,5-bisphosphate (PIP2) at focal adhesions plays a role in activating talin. However, a detailed picture and mechanism of PIP2 activation of autoinhibited talin remains elusive. Here, we use a fluorescence resonance energy transfer-based binding assay to measure the affinity of talin and lipid bilayers harboring anionic lipids. Results show that the R9 and R12R13 segments of the talin rod domain inhibit the binding of the talin head domain (THD) to anionic lipid bilayers. In contrast, we show that the binding of the THD to bilayers containing PIP2 is insensitive to the presence of the inhibitor domains, thereby directly implicating PIP2 as an effective activator of talin. Furthermore, we have mapped the activation to the interaction of PIP2 with the F2F3 domain of the talin head, showing that PIP2 plays a critical role in the regulation of the autoinhibited form of talin and stimulates recruitment of talin to the membrane, which is essential for integrin inside-out signaling.
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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.