Integrins are transmembrane proteins that serve as primary sensors of the extracellular matrix (ECM) environment. In response to interactions with the ECM, integrins initiate signaling pathways that regulate cell migration, growth, and survival. Advances in imaging have contributed to the understanding of the dynamic nature of these cell-ECM interactions and the complexes that form at these sites and have provided insights into their regulation and signal organizing functions.
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Nanoscopy reveals integrin clustering reliant on kindlin-3 but not talin-1.
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Interdisciplinary Institute for Neuroscience, Université Bordeaux, CNRS, Bordeaux, France.
Single molecule tracking and super-resolution microscopy of integrin adhesion proteins and actin in developing Drosophila muscle attachment sites reveals that nanotopography triggered by Arp2/3-dependent actin protrusions promotes stable adhesion formation. The nanodomains formed during this process confine the diffusion of integrins and promote their immobilization. Spatial confinement is also applied to the motion of actin filaments, resulting in enhanced mechanical connection with the integrin adhesion complex.
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Department of Materials Science and Engineering, Korea University, Seoul, Republic of Korea.
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