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- W2914805514 abstract "Trans-membrane proteins at the plasma membrane of the cell are equipped with modules to interact with the extra-cellular and the intra-cellular space. CD44 is a type I trans-membrane cell adhesion receptor that has been recently shown to compartmentalize the membrane into domains by acting as a membrane picket. This compartmentalization has been show to be necessary for membrane function of signaling receptors. While the extra-cellular domain of CD44 interacts with extracellular matrix (ECM) ligands hyaluronic acid and galectins, the intra-cellular domain interacts with a range of cytoskeletal adaptors, including ezrin and ankyrin at the cytoplasmic side. High spatial and temporal resolution imaging of living cells revealed a meso-scale architecture comprising of a meshwork pattern that is enriched with nano-scale clusters of CD44 along its perimeter. The nano-scale clustering in turn is orchestrated by engaging with the underlying actin cytoskeletal machinery. The cytoskeletal interaction mediated by specific sites on the intra-cellular domain influences the organization and dynamics of the protein both at the nano-scale and meso-scale providing a selective engagement with actin filaments nucleated by formin-based actin nucleation machinery over Arp2/3. Additionally, the extra-cellular domain and its interaction with elements of the extra-cellular matrix also influence the dynamics of the protein and its nano as well as meso-scale organization at the plasma membrane. Taken together, our data captures a hierarchical nature of organization of CD44 at the cell surface with cytoskeleton-templated nano-scale clusters populating the meso-scale domains." @default.
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- W2914805514 date "2019-02-01" @default.
- W2914805514 modified "2023-10-17" @default.
- W2914805514 title "Dynamic Actin Mediated Nanoclustering of Cd44 Regulates its Meso-Scale Organization at the Plasma Membrane" @default.
- W2914805514 doi "https://doi.org/10.1016/j.bpj.2018.11.1139" @default.
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