ArticleProteins2006
Two types of transmembrane homomeric interactions in the integrin receptor family are evolutionarily conserved.
Article in Proteins, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Peptide-Drug Conjugates: A New Hope for Cancer.Journal of peptide science : an official publication of the European Peptide Society · 2025Review
- Tests of integrin transmembrane domain homo-oligomerization during integrin ligand binding and signaling.The Journal of biological chemistry · 2011Article
- UVB-irradiation regulates VLA-4-mediated melanoma cell adhesion to endothelial VCAM-1 under flow conditions.Molecular carcinogenesis · 2011Article
- Interaction and conformational dynamics of membrane-spanning protein helices.Protein science : a publication of the Protein Society · 2009Review
- Transmembrane helices that form two opposite homodimeric interactions: an asparagine scan study of alphaM and beta2 integrins.Protein science : a publication of the Protein Society · 2008Article
- Structure and ion channel activity of the human respiratory syncytial virus (hRSV) small hydrophobic protein transmembrane domain.Protein science : a publication of the Protein Society · 2008Article
- Single-spanning transmembrane domains in cell growth and cell-cell interactions: More than meets the eye?Cell adhesion & migrationReview
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Integrins are heterodimers, but recent in vitro and in vivo experiments suggest that they are also able to associate through their transmembrane domains to form homomeric interactions. Two fundamental questions are the biological relevance of these aggregates and their form of interaction in the membrane domain. Although in vitro experiments have shown the involvement of a GxxxG-like motif, several crosslinking in vivo data are consistent with an almost opposite form of interaction between the transmembrane alpha-helices. In the present work, we have explored these two questions using molecular dynamics simulations for all available integrin types. We have tested the hypothesis that homomeric interactions are evolutionary conserved, and essential for the cell, using conservative substitutions to filter out nonnative interactions. Our results show that two models, one involving a GxxxG-like motif (model I) and an almost opposite form of interaction (model II) are conserved across all alpha and beta integrin types, both in homodimers and homotrimers, with different specificities. No conserved interaction was found for homotetramers. Our results are completely independent from experimental data, both during molecular dynamics simulations and in the selection of the correct models. We rationalize previous seemingly conflicting findings regarding the nature of integrin interhelical homomeric interactions.
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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.