Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/88901
Title: Regulation of α-catenin conformation at cadherin adhesions
Authors: Biswas, Kabir Hassan
Keywords: α-catenin
Actin
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
http://hdl.handle.net/10220/44926
ISSN: 1880-9863
DOI: 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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