Journal
SCIENCE
Volume 300, Issue 5620, Pages 795-798Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1079441
Keywords
-
Categories
Funding
- NCI NIH HHS [K01 CA096706] Funding Source: Medline
- NHLBI NIH HHS [HL54500, HL40387] Funding Source: Medline
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available