JUPITER, FL, January 6, 2012 Scientists know that cells in all higher organisms cells need to bind to each other for the development, architecture, maintenance and function of tissues. Mysteries have remained, however, about exactly how cells manage this feat.
Scientists from the Florida campus of The Scripps Research Institute (TSRI) have now solved part of this puzzle by defining the structure of a protein known as α-catenin, which is essential to this process.
The work was published online ahead of print on January 6, 2012, by the journal Nature Structural & Molecular Biology.
Chain, Chain, Chain
Our cells bind to each other using specialized cell surface adhesion complexes called adherens junctions, which direct the formation of tight, Velcro-like contacts among cells.
Adherens junctions are made up of three types of proteinscadherin, α-catenin and β-catenin. First, cadherin receptors, which span the cell membrane, direct the binding of cells to each other using domains that project outside the cell. Second, their tail domains, found on the inside of the cell, bind to the protein β-catenin, which, in turn, is bound to α-catenin.
The term catenin is derived from the Latin word for chain, catena, and these three proteins literally make a chain. This complex is then stabilized when the end of the chain, α-catenin, attaches to the molecular framework of the cell, the cytoskeleton. Without this, link cells would simply be amorphous piles of goo. Furthermore, alterations of cadherins, β-catenin and/or α-catenin can lead to marked changes in cell signaling, growth and migrationwhich can result in abnormalities and cancer.
Confronting a Paradox
Exactly how α-catenin provides links to the cytoskeleton and to the cadherin-β-catenin complex, however, has long puzzled scientists.
Scientists have known that &
|Contact: Eric Sauter|
Scripps Research Institute