ArticleThe Journal of biological chemistry2010
Structural requirements for activation in alphaIIb beta3 integrin.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- MnBiophysical journal · 2025Article
- Allosteric Disulfide Bridges in Integrins: The Molecular Switches of Redox Regulation of Integrin-Mediated Cell Functions.Antioxidants (Basel, Switzerland) · 2025Review
- An αIIbβ3 monoclonal antibody traps a semiextended conformation and allosterically inhibits large ligand binding.Blood advances · 2024Article
- Contributions of the individual domains of αCytoskeleton (Hoboken, N.J.) · 2024Article
- Review
- Electron microscopy shows that binding of monoclonal antibody PT25-2 primes integrin αIIbβ3 for ligand binding.Blood advances · 2021Article
- Autonomous conformational regulation of βProceedings of the National Academy of Sciences of the United States of America · 2018Article
- In silico analysis of structural modifications in and around the integrin αIIb genu caused by ITGA2B variants in human platelets with emphasis on Glanzmann thrombasthenia.Molecular genetics & genomic medicine · 2018Article
- The importance of N-glycosylation on βScientific reports · 2017Article
- αIIbβ3 variants defined by next-generation sequencing: predicting variants likely to cause Glanzmann thrombasthenia.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Inhibition of αIIbβ3 Ligand Binding by an αIIb Peptide that Clasps the Hybrid Domain to the βI Domain of β3.PloS one · 2015Article
- Redox-relevant aspects of the extracellular matrix and its cellular contacts via integrins.Antioxidants & redox signaling · 2014Review
- Complete integrin headpiece opening in eight steps.The Journal of cell biology · 2013Article
- Article
- Epitope mapping for monoclonal antibody reveals the activation mechanism for αVβ3 integrin.PloS one · 2013Article
- α(V)β(3) integrin crystal structures and their functional implications.Biochemistry · 2012Article
- Heparin modulates the conformation and signaling of platelet integrin αIIbβ3.Thrombosis research · 2012Article
- The platelet fibrinogen receptor: from megakaryocyte to the mortuary.JRSM cardiovascular disease · 2012Review
- Structural specializations of α(4)β(7), an integrin that mediates rolling adhesion.The Journal of cell biology · 2012Article
- Intact alphaIIbbeta3 integrin is extended after activation as measured by solution X-ray scattering and electron microscopy.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Integrins are postulated to undergo structural rearrangement from a low affinity bent conformer to a high affinity extended conformer upon activation. However, some reports have shown that a bent conformer is capable of binding a ligand, whereas another report has shown that integrin extension does not absolutely lead to activation. To clarify whether integrin affinity is indeed regulated by the so-called switchblade-like movement, we have engineered a series of mutant αIIbβ3 integrins that are constrained specifically in either a bent or an extended conformation. These mutant αIIbβ3 integrins were expressed in mammalian cells, and fibrinogen binding to these cells was examined. The bent integrins were created through the introduction of artificial disulfide bridges in the β-head/β-tail interface. Cells expressing bent integrins all failed to bind fibrinogen unless pretreated with DTT to disrupt the disulfide bridges. The extended integrins were created by introducing N-glycosylation sites in amino acid residues located close to the α-genu, where the integrin legs fold backward. Among these mutants, activation was maximized in one integrin with an N-glycosylation site located behind the α-genu. This extension-induced activation was completely blocked when the swing-out of the hybrid domain was prevented. These results suggest that the bent and extended conformers represent low affinity and high affinity conformers, respectively, and that extension-induced activation depends on the swing-out of the hybrid domain. Taken together, these results are consistent with the current hypothesis that integrin affinity is regulated by the switchblade-like movement of the integrin legs.
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