Publications by authors named "Alexander William M Haining"
Article Synopsis
- Scientists are studying how proteins change shape (unfold) inside cells and why this matters for how cells act.
- They discovered that a specific protein called DLC1 helps control another protein (RhoA) that affects how cells stick together and move.
- By changing a part of another protein called talin, they learned that when talin unfolds, it affects DLC1 and how cells behave, which could be important for many different cell functions.
Mechanical stability is a key feature in the regulation of structural scaffolding proteins and their functions. Despite the abundance of α-helical structures among the human proteome and their undisputed importance in health and disease, the fundamental principles of their behavior under mechanical load are poorly understood. Talin and α-catenin are two key molecules in focal adhesions and adherens junctions, respectively.
View Article and Find Full Text PDFArticle Synopsis
- Cells can sense physical properties of their environment, like the rigidity of the surface they are on.
- Researchers explored how the length of adhesive tethers—molecules linking cells to their surroundings—affects cell behavior by modifying surfaces with different lengths of tethers.
- Results showed that as the tether length increased, cells became less adhesive, with significant reductions in the number of cells and their size, highlighting the importance of tether length in influencing how cells spread and interact without changing other factors like surface rigidity.
Although the relevance of mechanotransduction in cell signaling is currently appreciated, the mechanisms that drive this process remain largely unknown. Mechanical unfolding of proteins may trigger distinct downstream signals in cells, providing a mechanism for cellular mechanotransduction. Force-induced unfolding of talin, a prominent focal adhesion protein, has been demonstrated previously for a small portion of its rod domain.
View Article and Find Full Text PDF