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suck abstract from ncbi


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pmid25673211      Cell+Tissue+Res 2015 ; 360 (3): 773-83
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  • New Functions for Alpha-Catenins in Health and Disease: From Cancer to Heart Regeneration #MMPMID25673211
  • Vite A; Li J; Radice GL
  • Cell Tissue Res 2015[Jun]; 360 (3): 773-83 PMID25673211show ga
  • Strong cell-cell adhesion mediated by adherens junctions is dependent on anchoring the transmembrane cadherin molecule to the underlying actin cytoskeleton. To do this, cadherin cytoplasmic domain interacts with catenin proteins, which include ?-catenin that binds directly to filamentous actin. Originally thought to be a static structure, the connection between the cadherin/catenin adhesion complex and the actin cytoskeleton is now considered to be dynamic and responsive to both intercellular and intracellular signals. Alpha-catenins are mechanosensing proteins that undergo conformational change in response to cytoskeletal tension thus modifying the linkage between the cadherin and the actin cytoskeleton. There are three ?-catenin isoforms expressed in mouse and human: ?E-catenin (CTNNA1), ?N-catenin (CTNNA2), and ?T-catenin (CTNNA3). This review summarizes recent progress in understanding the in vivo function(s) of ?-catenins in tissue morphogenesis, homeostasis, and disease. The role of ?-catenin in the regulation of cellular proliferation will be discussed in the context of cancer and regeneration.
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