Bidirectional Transmembrane Signaling by Cytoplasmic Domain Separation in Integrins
By Minsoo Kim, C. Carman, T. Springer. Science, 2003
855 citations recorded by the source corpus.
Subfields: Immunology and Allergy, Molecular Biology, Radiology, Nuclear Medicine and Imaging
View Paper: https://www.semanticscholar.org/paper/686484975c6a401ffde2a0c5186a6b3fa9a6a840
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In Immunology and Allergy
In Molecular Biology
In Radiology, Nuclear Medicine and Imaging
Citations in the corpus
- An Essential Role for Talin during αMβ2-mediated Phagocytosis (2007, background): “Interaction of talin head with the cytoplasmic domain of 2 is sufficient to increase binding of C3bi-RBCs in macrophages and transfected COS-7 cells (Figures 7 and 9). Moreover, talin and talin head interact with M2, as shown by coimmunoprecipitation and GST pull-down assays (Figures 3 and 4). This ”
- Structural basis of integrin regulation and signaling. (2007, background): “Furthermore, extracellular addition of Mn2+ and soluble ICAM-1, which induces integrin extension as shown by exposure of the KIM127 epitope, also induces α and β subunit cytoplasmic domain separation (35).”
- Integrin structure, activation, and interactions. (2011, methodology): “Evidence for this includes experiments using EM (Adair and Yeager 2002), disulfide cross-linking (Luo et al. 2004), activating mutations (Partridge et al. 2005), and FRET 4 Cite this article as Cold Spring Harb Perspect Biol 2011;3:a004994 of labeled cytoplasmic tails (Kim et al. 2003).”
- Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics (2004, background): “, and transmission of activation signals across the membrane involves separation between the α and β transmembrane and cytoplasmic domain”
- Structural Dynamics of α-Actinin-Vinculin Interactions (2005, background): “, the conserved proline residue in the B helix of R4), the spectrin repeats of -actinin are predicted to form similar unfolded intermediates in response to sheer stress, and -actinin binds to cadherin and integrin receptors in adherens junctions and focal adhesions, respectively, where mechanical st”
- Adhesion of membranes via receptor-ligand complexes: Domain formation, binding cooperativity, and active processes (2009, background): “In one of their conformations, the integrin molecules are extended and can bind to apposing ligands [102, 103, 104].”
- Getting to the site of inflammation: the leukocyte adhesion cascade updated (2007, background): “The most detailed information about integrin structural rearrangement during affinity upregulation in leukocytes comes from studies of LFA1 (Ref”
- Activation, coactivation, and costimulation of resting human natural killer cells (2006, background): “In the resting state, the aL and b2 cytoplasmic domains are close to each other and the extracellular domain is closed, but either inside-out signaling or ligand binding induces an extended conformation of the extracellular domain coupled to a spatial separation of the cytoplasmic domains (114).”
- Intracellular signalling controlling integrin activation in lymphocytes (2005, background): “FLUORESCENCE RESONANCE ENERGY TRANSFER (FRET) studies have shown that separation of the cytoplasmic regions of the α L - and β 2 -chain of LFA1 occurs following either inside-out signalling or ligand bindin”
- FAK phosphorylation sites mapped by mass spectrometry (2005, background): “Binding of the integrin cytoplasmic tails to the FERM domain of talin induces conformational changes in the integrin extracellular domains, thus increasing their affinity for ligands (Calderwood et al., 2004; Tadokoro et al., 2003; Calderwood et al., 2002; Kim et al., 2003 ).”