有哪些信誉好的足球投注网站morphology and viscoelasticity of actin networks formed with the mutually interacting crosslinkers palladin and alpha-actinin形态和粘弹性的肌动蛋白网络形成相互交互的交联剂palladin alpha-actinin.pdfVIP
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morphology and viscoelasticity of actin networks formed with the mutually interacting crosslinkers palladin and alpha-actinin形态和粘弹性的肌动蛋白网络形成相互交互的交联剂palladin alpha-actinin
Morphology and Viscoelasticity of Actin Networks Formed with the Mutually Interacting Crosslinkers: Palladin and Alpha-actinin 1 2 3 4 Brian Grooman , Ikuko Fujiwara , Carol Otey , Arpita Upadhyaya * 1 Department of Physics, University of Maryland, College Park, Maryland, United States of America, 2 National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland, United States of America, 3 Department of Cell and Molecular Physiology, University of North Carolina, Chapel Hill, North Carolina, United States of America, 4 Department of Physics and Institute for Physical Science and Technology (IPST), University of Maryland, College Park, Maryland, United States of America Abstract Actin filaments and associated actin binding proteins play an essential role in governing the mechanical properties of eukaryotic cells. Even though cells have multiple actin binding proteins (ABPs) that exist simultaneously to maintain the structural and mechanical integrity of the cellular cytoskeleton, how these proteins work together to determine the properties of actin networks is not clearly understood. The ABP, palladin, is essential for the maintenance of cell morphology and the regulation of cell movement. Palladin coexists with a-actinin in stress fibers and focal adhesions and binds to both actin and a-actinin. To obtain insight into how mutually interacting actin crosslinking proteins modulate the properties of actin networks, we characterized the micro-structure and mechanics of actin networks crosslinked with palladin and a- actinin. We first showed that palladin crosslinks actin filaments into bundled networks which are viscoelastic in nature. Our studies also showed that composite networks of a-actinin/palladin/actin behave very
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