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Integrin bondage: filamin takes control

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Regulation of integrin activity is critical for human health, and the steps mediating integrin activation are well established. In contrast, the counteracting mechanisms of inactivation are less understood. An integrin inhibitor, filamin, is shown to stabilize the integrin resting state by bondage of the cytoplasmic domains of the integrin heterodimer, thus providing evidence of a new mechanism for integrin retention in the inactive state.

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Figure 1: Alignment of the membrane-proximal and cytoplasmic regions of all integrin α chains.
Figure 2: Superposition of IgFLMa20 in complex with IgFLMa21 (PDB 2J3S)12 or with αIIbβ3 (PDB 2MTP)2.
Figure 3: Views of the cytoplasmic tails of integrin α subunits.

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Correspondence to Johanna Ivaska.

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De Franceschi, N., Ivaska, J. Integrin bondage: filamin takes control. Nat Struct Mol Biol 22, 355–357 (2015). https://doi.org/10.1038/nsmb.3024

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