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https://hdl.handle.net/2440/68226
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dc.contributor.author | Kiema, T. | - |
dc.contributor.author | Lad, Y. | - |
dc.contributor.author | Jiang, P. | - |
dc.contributor.author | Oxley, C. | - |
dc.contributor.author | Baldassarre, M. | - |
dc.contributor.author | Wegener, K. | - |
dc.contributor.author | Campbell, I. | - |
dc.contributor.author | Ylanne, J. | - |
dc.contributor.author | Calderwood, D. | - |
dc.date.issued | 2006 | - |
dc.identifier.citation | Molecular Cell, 2006; 21(3):337-347 | - |
dc.identifier.issn | 1097-2765 | - |
dc.identifier.issn | 1097-4164 | - |
dc.identifier.uri | http://hdl.handle.net/2440/68226 | - |
dc.description.abstract | The ability of adhesion receptors to transmit biochemical signals and mechanical force across cell membranes depends on interactions with the actin cytoskeleton. Filamins are large, actin-crosslinking proteins that connect multiple transmembrane and signaling proteins to the cytoskeleton. Here, we describe the high-resolution structure of an interface between filamin A and an integrin adhesion receptor. When bound, the integrin β cytoplasmic tail forms an extended β strand that interacts with β strands C and D of the filamin immunoglobulin-like domain (IgFLN) 21. This interface is common to many integrins, and we suggest it is a prototype for other IgFLN domain interactions. Notably, the structurally defined filamin binding site overlaps with that of the integrin-regulator talin, and these proteins compete for binding to integrin tails, allowing integrin-filamin interactions to impact talin-dependent integrin activation. Phosphothreonine-mimicking mutations inhibit filamin, but not talin, binding, indicating that kinases may modulate this competition and provide additional means to control integrin functions. | - |
dc.description.statementofresponsibility | Tiila Kiema, Yatish Lad, Pengju Jiang, Camilla L. Oxley, Massimiliano Baldassarre, Kate L. Wegener, Iain D. Campbell, Jari Ylänne and David A. Calderwood | - |
dc.description.uri | http://www.sciencedirect.com/science/journal/10972765 | - |
dc.language.iso | en | - |
dc.publisher | Cell Press | - |
dc.rights | Copyright 2006 Elsevier Inc. | - |
dc.source.uri | http://dx.doi.org/10.1016/j.molcel.2006.01.011 | - |
dc.subject | NIH 3T3 Cells | - |
dc.subject | Animals | - |
dc.subject | Mice | - |
dc.subject | Microfilament Proteins | - |
dc.subject | Calpain | - |
dc.subject | Contractile Proteins | - |
dc.subject | Talin | - |
dc.subject | Integrin beta Chains | - |
dc.subject | Recombinant Fusion Proteins | - |
dc.subject | Crystallography, X-Ray | - |
dc.subject | Nuclear Magnetic Resonance, Biomolecular | - |
dc.subject | Reproducibility of Results | - |
dc.subject | Binding Sites | - |
dc.subject | Amino Acid Sequence | - |
dc.subject | Protein Conformation | - |
dc.subject | Protein Structure, Tertiary | - |
dc.subject | Protein Binding | - |
dc.subject | Sequence Homology, Amino Acid | - |
dc.subject | Models, Molecular | - |
dc.subject | Molecular Sequence Data | - |
dc.subject | Filamins | - |
dc.title | The molecular basis of filamin binding to integrins and competition with talin | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1016/j.molcel.2006.01.011 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Wegener, K. [0000-0002-1562-6060] | - |
Appears in Collections: | Aurora harvest Molecular and Biomedical Science publications |
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