ArticleThe Journal of biological chemistry2016
A Conserved Ectodomain-Transmembrane Domain Linker Motif Tunes the Allosteric Regulation of Cell Surface Receptors.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- Structure of the CD33 Receptor and Implications for the Siglec Family.Biochemistry · 2025Article
- Comparison of Integrin αIIbβ3 Transmembrane Association in Vesicles and Bicelles.Biochemistry · 2023Article
- Insight Into Pathological Integrin αIIbβ3 Activation From Safeguarding The Inactive State.Journal of molecular biology · 2021Article
- Orchestration of signaling by structural disorder in class 1 cytokine receptors.Cell communication and signaling : CCS · 2020Article
- Structural Understanding of Interleukin 6 Family Cytokine Signaling and Targeted Therapies: Focus on Interleukin 11.Frontiers in immunology · 2020Review
- Article
- On the contributing role of the transmembrane domain for subunit-specific sensitivity of integrin activation.Scientific reports · 2018Article
- Membrane Anchoring of α-Helical Proteins: Role of Tryptophan.The journal of physical chemistry. B · 2018Article
- Energy landscape differences among integrins establish the framework for understanding activation.The Journal of cell biology · 2018Article
- Application of Solution NMR to Structural Studies on α-Helical Integral Membrane Proteins.Molecules (Basel, Switzerland) · 2017Review
- Direct Evaluation of Protein-Lipid Contacts Reveals Protein Membrane Immersion and Isotropic Bicelle Structure.The journal of physical chemistry letters · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
In many families of cell surface receptors, a single transmembrane (TM) α-helix separates ecto- and cytosolic domains. A defined coupling of ecto- and TM domains must be essential to allosteric receptor regulation but remains little understood. Here, we characterize the linker structure, dynamics, and resulting ecto-TM domain coupling of integrin αIIb in model constructs and relate it to other integrin α subunits by mutagenesis. Cellular integrin activation assays subsequently validate the findings in intact receptors. Our results indicate a flexible yet carefully tuned ecto-TM coupling that modulates the signaling threshold of integrin receptors. Interestingly, a proline at the N-terminal TM helix border, termed NBP, is critical to linker flexibility in integrins. NBP is further predicted in 21% of human single-pass TM proteins and validated in cytokine receptors by the TM domain structure of the cytokine receptor common subunit β and its P441A-substituted variant. Thus, NBP is a conserved uncoupling motif of the ecto-TM domain transition and the degree of ecto-TM domain coupling represents an important parameter in the allosteric regulation of diverse cell surface receptors.
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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.