Exploring mechanoregulation in cells through cytoskeletal regulatory proteins
In our bodies, chemical energy is converted to mechanical force by motor proteins like myosin ATPase. These forces can serve as mechanical signals that in turn create biochemical responses. Despite decades of research, regulatory mechanisms cells use to sense static mechanical forces, like gravity and tissue stiffness, are poorly understood.
Rasmussen and Jin discussed the functions of two structural proteins, calponin and transgelin, known to be involved in mechanoregulation.
Calponin and transgelin are thought to play important roles in processes like cell adhesion, migration, phagocytosis, and more. They are also thought to be involved with processes such as wound healing, inflammatory responses, ovarian development, and tumor metastasis.
“Understanding the mechanoregulation of cellular activities is of major biological and medical importance,” said author J.-P. Jin.
Calponin was first discovered in the 1980s in smooth muscle cells, but the past two decades have seen an increased interest in the proteins due to their functions in non-muscular cells. The authors summarized what is known about the proteins in cellular mechanoregulation with the aim of providing a foundation for future studies into the cellular sensing and conversion of static tension signal into biochemical activities.
“We hope to guide more researchers to study the mechanoregulation and function of calponin and transgelin as model systems to understand cellular sensing and responses to static mechanical force signals,” Jin said.
The authors hope further research will bring a better understanding of this enigmatic aspect of cellular function.
“We may look forward to more breakthroughs in the understanding of cellular sensing and responses to static mechanical force signals in the coming decade,” Jin said.
Source: “Mechanoregulation and function of calponin and transgelin,” by Monica Rasmussen and J.-P. Jin, Biophysics Reviews (2024). The article can be accessed at https://doi.org/10.1063/5.0176784 .