ArticleThe Journal of biological chemistry2012
Integrin αIIbβ3 inside-out activation: an in situ conformational analysis reveals a new mechanism.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- An Updated Review on Glycoprotein IIb/IIIa Inhibitors as Antiplatelet Agents: Basic and Clinical Perspectives.High blood pressure & cardiovascular prevention : the official journal of the Italian Society of Hypertension · 2023Review
- Kindlin Assists Talin to Promote Integrin Activation.Biophysical journal · 2020Article
- The membrane-distal regions of integrin α cytoplasmic domains contribute differently to integrin inside-out activation.Scientific reports · 2018Article
- Article
- The dual structural roles of the membrane distal region of the α-integrin cytoplasmic tail during integrin inside-out activation.Journal of cell science · 2015Article
- Article
- Mechanisms of talin-dependent integrin signaling and crosstalk.Biochimica et biophysica acta · 2014Review
- Genetically modified T cells targeting neovasculature efficiently destroy tumor blood vessels, shrink established solid tumors and increase nanoparticle delivery.International journal of cancer · 2013Article
- Integrin inactivators: balancing cellular functions in vitro and in vivo.Nature reviews. Molecular cell biology · 2013Review
- Is There Still a Role for Glycoprotein IIb/IIIa Antagonists in Acute Coronary Syndromes?Cardiology research · 2013Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Integrins are a family of heterodimeric adhesion receptors that transmit signals bi-directionally across the plasma membranes. The transmembrane domain (TM) of integrin plays a critical role in mediating transition of the receptor from the default inactive to the active state on the cell surfaces. In this study, we successfully applied the substituted cysteine scanning accessibility method to determine the intracellular border of the integrin α(IIb)β(3) TM in the inactive and active states in living cells. We examined the aqueous accessibility of 75 substituted cysteines comprising the C terminus of both α(IIb) and β(3) TMs, the intracellular membrane-proximal regions, and the whole cytoplasmic tails, to the labeling of a membrane-permeable, cysteine-specific chemical biotin maleimide (BM). The active state of integrin α(IIb)β(3) heterodimer was generated by co-expression of activating partners with the cysteine-substituted constructs. Our data revealed that, in the inactive state, the intracellular lipid/aqueous border of α(IIb) TM was at Lys(994) and β(3) TM was at Phe(727) respectively; in the active state, the border of α(IIb) TM shifted to Pro(998), whereas the border of β(3) TM remained unchanged, suggesting that complex conformational changes occurred in the TMs upon α(IIb)β(3) inside-out activation. On the basis of the results, we propose a new inside-out activation mechanism for integrin α(IIb)β(3) and by inference, all of the integrins in their native cellular environment.
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