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Type: Journal article
Title: The structure of an integrin/talin complex reveals the basis of inside-out signal transduction
Author: Anthis, N.
Wegener, K.
Ye, F.
Kim, C.
Goult, B.
Lowe, E.
Vakonakis, I.
Bate, N.
Critchley, D.
Ginsberg, M.
Campbell, I.
Citation: The EMBO Journal, 2009; 28(22):3623-3632
Publisher: Nature Publishing Group
Issue Date: 2009
ISSN: 0261-4189
Statement of
Nicholas J. Anthis, Kate L. Wegener, Feng Ye, Chungho Kim, Benjamin T. Goult, Edward D. Lowe, Ioannis Vakonakis, Neil Bate, David R. Critchley, Mark H. Ginsberg and Iain D. Campbell
Abstract: Fundamental to cell adhesion and migration, integrins are large heterodimeric membrane proteins that uniquely mediate inside-out signal transduction, whereby adhesion to the extracellular matrix is activated from within the cell by direct binding of talin to the cytoplasmic tail of the beta integrin subunit. Here, we report the first structure of talin bound to an authentic full-length beta integrin tail. Using biophysical and whole cell measurements, we show that a specific ionic interaction between the talin F3 domain and the membrane-proximal helix of the beta tail disrupts an integrin alpha/beta salt bridge that helps maintain the integrin inactive state. Second, we identify a positively charged surface on the talin F2 domain that precisely orients talin to disrupt the heterodimeric integrin transmembrane (TM) complex. These results show key structural features that explain the ability of talin to mediate inside-out TM signalling.
Keywords: CHO Cells
Cell Membrane
Macromolecular Substances
Signal Transduction
Cell Polarity
Amino Acid Sequence
Protein Structure, Tertiary
Protein Binding
Sequence Homology, Amino Acid
Models, Biological
Models, Molecular
Molecular Sequence Data
Rights: © 2009 European Molecular Biology Organization
DOI: 10.1038/emboj.2009.287
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Appears in Collections:Aurora harvest
Molecular and Biomedical Science publications

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