The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Activation of Integrin αIIbß3 by Modulation of Transmembrane Helix Associations
Abstract
Transmembrane helices of integrin α and β 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 β3 subunit enabled integrin αIIbβ3 to constitutively bind soluble fibrinogen. Further characterization of the G708N mutant revealed that it induced αIIbβ3 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.
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Cites
Hynes (2002) · doi:10.1016/s0092-8674(02)00971-6 · Cited by 8,606
Giancotti, F. G., & Ruoslahti, E. (1999) · Science · doi:10.1126/science.285.5430.1028 · Cited by 3,869
Crystal Structure of the Extracellular Segment of Integrin αVβ3
Xiong, J.-P., Stehle, T., Diefenbach, B., Zhang, R., Dunker, R., Scott, D. L., Joachimiak, A., Goodman, S. L., & Arnaout, M. A. (2001) · Science · doi:10.1126/science.1064535 · Cited by 1,276
Takagi, J., Petre, B. M., Walz, T., & Springer, T. A. (2002) · Cell · doi:10.1016/s0092-8674(02)00935-2 · Cited by 1,168
Changes in the platelet membrane glycoprotein IIb.IIIa complex during platelet activation.
Shattil, S. J., Hoxie, J. A., Cunningham, M., & Brass, L. F. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39154-8 · Cited by 942
Exposure of platelet fibrinogen receptors by ADP and epinephrine.
Bennett, J. S., & Vilaire, G. (1979) · Journal of Clinical Investigation · doi:10.1172/jci109597 · Cited by 849
Self-citationVinogradova, O., Velyvis, A., Velyviene, A., Hu, B., Haas, T. A., Plow, E. F., & Qin, J. (2002) · Cell · doi:10.1016/s0092-8674(02)00906-6 · Cited by 530
Gartner, T. K., & Bennett, J. S. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38962-7 · Cited by 427
Self-citationAsparagine-mediated self-association of a model transmembrane helix.
Lear, J. D., DeGrado, W. F., Choma, C. T., & Gratkowski, H. (2000) · Nature Structural Biology · doi:10.1038/72440 · Cited by 353
Self-citationPolar residues drive association of polyleucine transmembrane helices
Zhou, F. X., Merianos, H. J., Brunger, A. T., & Engelman, D. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.041593698 · Cited by 344
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The final steps of integrin activation: the end game
Shattil, S. J., Kim, C., & Ginsberg, M. H. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2871 · Cited by 1,086
Bidirectional Transmembrane Signaling by Cytoplasmic Domain Separation in Integrins
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Src kinase activation by direct interaction with the integrin β cytoplasmic domain
Arias-Salgado, E. G., Lizano, S., Sarkar, S., Brugge, J. S., Ginsberg, M. H., & Shattil, S. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2336149100 · Cited by 554
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Metadata
- Authors
- Li, R., Mitra, N., Gratkowski, H., Vilaire, G., Litvinov, R., Nagasami, C., Weisel, J. W., Lear, J. D., DeGrado, W. F., & Bennett, J. S.
- Venue
- Science
- Published
- 2003-05-02
- Volume
- 300
- Issue
- 5620
- Pages
- 795-798
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1506821897
- Cited by
- 290
- References
- 24
- FWCI
- 17.05
- Type
- journal article
- Language
- en
- Open access
- closed
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- Li, R., Mitra, N., Gratkowski, H., Vilaire, G., Litvinov, R., Nagasami, C., Weisel, J. W., Lear, J. D., DeGrado, W. F., & Bennett, J. S. (2003). Activation of Integrin αIIbß3 by Modulation of Transmembrane Helix Associations. Science. https://doi.org/10.1126/science.1079441
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
