ArticleStructure (London, England : 1993)2021
Phosphorylation of RIAM by src promotes integrin activation by unmasking the PH domain of RIAM.
Article in Structure (London, England : 1993), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed, 18 citations in OpenAlex.
- Regulated RIAM-Talin Engagement Controls Adhesion Stability and Mechanical Output.bioRxiv : the preprint server for biology · 2026Article
- The cytoskeletal control of B cell receptor and integrin signaling in normal B cells and chronic lymphocytic leukemia.FEBS letters · 2025Review
- Focal adhesion kinase: A promising regulator of colitis-associated healing.World journal of gastroenterology · 2025Review
- Focal adhesion in the tumour metastasis: from molecular mechanisms to therapeutic targets.Biomarker research · 2025Review
- A phosphorylation-controlled switch confers cell cycle-dependent protein relocalization.Nature cell biology · 2024Article
- A phosphorylation-controlled switch confers cell cycle-dependent protein relocalization.bioRxiv : the preprint server for biology · 2024Article
- Inhibition of talin-induced integrin activation by a double-hit stapled peptide.Structure (London, England : 1993) · 2023Article
- ConFERMing the role of talin in integrin activation and mechanosignaling.Journal of cell science · 2023Article
- The complex role of tumor-infiltrating macrophages.Nature immunology · 2022Review
- Integrin Regulators in Neutrophils.Cells · 2022Review
- Review
- Structural, biochemical, and functional properties of the Rap1-Interacting Adaptor Molecule (RIAM).Biomedical journal · 2022Review
- The Connection Between Rap1 and Talin1 in the Activation of Integrins in Blood Cells.Frontiers in cell and developmental biology · 2022Review
- Phosphorylation of RIAM Activates Its Adaptor Function in Mediating Integrin Signaling.Journal of cellular signaling · 2021Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Integrin activation controls cell adhesion, migration, invasion, and extracellular matrix remodeling. RIAM (RAP1-GTP-interacting adaptor molecule) is recruited by activated RAP1 to the plasma membrane (PM) to mediate integrin activation via an inside-out signaling pathway. This process requires the association of the pleckstrin homology (PH) domain of RIAM with the membrane PIP2. We identify a conserved intermolecular interface that masks the PIP2-binding site in the PH domains of RIAM. Our data indicate that phosphorylation of RIAM by Src family kinases disrupts this PH-mediated interface, unmasks the membrane PIP2-binding site, and promotes integrin activation. We further demonstrate that this process requires phosphorylation of Tyr267 and Tyr427 in the RIAM PH domain by Src. Our data reveal an unorthodox regulatory mechanism of small GTPase effector proteins by phosphorylation-dependent PM association of the PH domain and provide new insights into the link between Src kinases and integrin 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.