Al Green was most likely singing “Let’s Stay Together” to some babe he was in love with, but I’d like to imagine he was talking about cells. I’m not sure they play Al Green in the lab that today’s image comes from, but I’d suggest adding his work to their playlist (good advice for everyone, really). Today’s image is from a paper showing how cadherin’s structural changes affect cell adhesion.
Cadherins are transmembrane proteins that play an important role in cell-cell adhesion. Cell adhesion is a dynamic process that is highly regulated throughout development, during cancer progression, and for basic tissue function. A recent paper shows how physical and structural changes in certain cadherin domains affect the adhesive state of that cadherin. In this paper, Petrova and colleagues used a human colorectal tumor line of cells that don’t normally adhere to one another, but can be triggered to adhere and compact. By using a set of specialized monoclonal antibodies that can bind to certain states of active or inactive cadherin domains, Petrova and colleagues found that the structural changes in regions near calcium-binding sites, mediated by changes in another adhesion player called p120-catenin, affect adhesion activation. In the images above, cells treated with a control antibody (left) remain round and unattached, while cells treated with an adhesion-activating antibody (right) became attached and compact.
Petrova, Y., Spano, M., & Gumbiner, B. (2012). Conformational epitopes at cadherin calcium-binding sites and p120-catenin phosphorylation regulate cell adhesion Molecular Biology of the Cell, 23 (11), 2092-2108 DOI: 10.1091/mbc.E11-12-1060