Activation of integrin alphaIIbbeta3 by modulation of transmembrane helix associations - PubMed (original) (raw)
. 2003 May 2;300(5620):795-8.
doi: 10.1126/science.1079441.
Affiliations
- PMID: 12730600
- DOI: 10.1126/science.1079441
Activation of integrin alphaIIbbeta3 by modulation of transmembrane helix associations
Renhao Li et al. Science. 2003.
Abstract
Transmembrane helices of integrin alpha and beta subunits have been implicated in the regulation of integrin activity. Two mutations, glycine-708 to asparagine-708 (G708N)and methionine-701 to asparagine-701, in the transmembrane helix of the beta3 subunit enabled integrin alphaIIbbeta3 to constitutively bind soluble fibrinogen. Further characterization of the G708N mutant revealed that it induced alphaIIbbeta3 clustering and constitutive phosphorylation of focal adhesion kinase. This mutation also enhanced the tendency of the transmembrane helix to form homotrimers. These results suggest that homomeric associations involving transmembrane domains provide a driving force for integrin activation. They also suggest a structural basis for the coincidence of integrin activation and clustering.
Comment in
- Structural biology. Changing partners.
Hynes RO. Hynes RO. Science. 2003 May 2;300(5620):755-6. doi: 10.1126/science.1084854. Science. 2003. PMID: 12730590 No abstract available.
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