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|Title:||Regulation of α-catenin conformation at cadherin adhesions||Authors:||Biswas, Kabir Hassan||Keywords:||α-catenin
|Issue Date:||2018||Source:||Biswas, K. H. (2018). Regulation of α-catenin conformation at cadherin adhesions. Journal of Biomechanical Science and Engineering, in press.||Series/Report no.:||Journal of Biomechanical Science and Engineering||Abstract:||Cells in our body utilize a variety of adaptor proteins for transmitting context specific signals that arise from the cellular microenvironment. Adaptor proteins lack enzymatic activity and typically perform their function by acting as scaffolds that bind other signaling proteins. While most adaptor proteins are functionally modulated by biochemical alterations such as phosphorylation, a subset of adaptor proteins are functionally modulated by a mechanical alteration in their structure that makes cryptic sites available for binding to downstream signaling proteins. α-catenin is one such adaptor protein that localizes to cadherin-based cell adhesions by binding the membrane-localized cadherin-β-catenin complex at one side and the cytosolic F-actin on the other side. An increase in actomyosin tension is directly relayed to α-catenin resulting in a change in its conformation making cryptic binding sites accessible to its interacting partners. Here, I describe an updated view of the mechanical regulation of α-catenin in the context of cellular adhesion, including the role of cadherin clustering in its activation.||URI:||https://hdl.handle.net/10356/88901
|ISSN:||1880-9863||DOI:||http://dx.doi.org/10.1299/jbse.17-00699||Rights:||© 2018 The Japan Society of Mechanical Engineers. This is the author created version of a work that has been peer reviewed and accepted for publication by Journal of Biomechanical Science and Engineering, The Japan Society of Mechanical Engineers. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1299/jbse.17-00699].||Fulltext Permission:||open||Fulltext Availability:||With Fulltext|
|Appears in Collections:||MSE Journal Articles|
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