ArticlePloS one2013
Transmembrane and Juxtamembrane Structure of αL Integrin in Bicelles.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- Integrins in cancer: insights into mechanisms and therapeutic potential.Cell communication and signaling : CCS · 2026Review
- The structural basis of β2 integrin intra-cellular multi-protein complexes.Biophysical reviews · 2022Review
- Refinement of SARS-CoV-2 envelope protein structure in a native-like environment by molecular dynamics simulations.Frontiers in molecular biosciences · 2022Article
- LCP1 preferentially binds clasped αMβ2 integrin and attenuates leukocyte adhesion under flow.Journal of cell science · 2018Article
- Intramembrane ionic protein-lipid interaction regulates integrin structure and function.PLoS biology · 2018Article
- Structural model of the SARS coronavirus E channel in LMPG micelles.Biochimica et biophysica acta. Biomembranes · 2018Article
- The membrane-distal regions of integrin α cytoplasmic domains contribute differently to integrin inside-out activation.Scientific reports · 2018Article
- Membrane Anchoring of α-Helical Proteins: Role of Tryptophan.The journal of physical chemistry. B · 2018Article
- A Conserved Ectodomain-Transmembrane Domain Linker Motif Tunes the Allosteric Regulation of Cell Surface Receptors.The Journal of biological chemistry · 2016Article
- Integrin bondage: filamin takes control.Nature structural & molecular biology · 2015Article
- Integrin αIIbβ3 transmembrane domain separation mediates bi-directional signaling across the plasma membrane.PloS one · 2015Article
- Inhibition of the human respiratory syncytial virus small hydrophobic protein and structural variations in a bicelle environment.Journal of virology · 2014Article
- Lipid concentration and molar ratio boundaries for the use of isotropic bicelles.Langmuir : the ACS journal of surfaces and colloids · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The accepted model for the interaction of α and β integrins in the transmembrane (TM) domain is based on the pair αIIbβ3. This involves the so-called outer and inner membrane association clasps (OMC and IMC, respectively). In the α chain, the OMC involves a GxxxG-like motif, whereas in the IMC a conserved juxtamembrane GFFKR motif experiences a backbone reversal that partially fills the void generated by TM separation towards the cytoplasmic half. However, the GFFKR motif of several α integrin cytoplasmic tails in non-bicelle environments has been shown to adopt an α-helical structure that is not membrane-embedded and which was shown to bind a variety of cytoplasmic proteins. Thus it is not known if a membrane-embedded backbone reversal is a conserved structural feature in α integrins. We have studied the system αLβ2 because of its importance in leukocytes, where integrin deactivation is particularly important. Herein we show that the backbone reversal feature is not only present in αIIb but also in αL-TM when reconstituted in bicelles. Additionally, titration with β2 TM showed eight residues clustering along one side of αL-TM, forming a plausible interacting face with β2. The latter orientation is consistent with a previously predicted reported polar interaction between αL Ser-1071 and β2 Thr-686.
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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.