University of Notre Dame researchers, including Liangliang Sun, Michelle Bertke, Matthew Champion, Guijie Zhu, Paul Huber and Norman Dovichi, have revealed that the disruption of the Small Ubiquitin-like Modifier (SUMO) proteins during embryo development may contribute to congenital heart defects. They have reported their findings in a paper published in Scientific Reports.
The SUMO proteins can be covalently conjugated to and detached from a lysine residue in a target protein. In this way, SUMO helps modify the function of other proteins in cells. SUMO is involved in many important cellular processes. Its ability to regulate gene expression during organism development is of great interest. But this ability has not been well defined.
Transcription dynamics during organism development have been studied extensively. But protein data about organism development is limited. To better understand the role of proteins in embryo development, Dovichi's team analyzed expression dynamics of nearly 4,000 proteins of Xenopus laevis during embryo development. Xenopus laevis is a species of African aquatic frog, and its embryos and eggs are a popular model system for scientific research because the animal has close evolutionary relationship with humans compared to many other model organisms.
The researchers obtained a large dataset of protein expression during development. They discovered that when the activity of the SUMO protein was inhibited, some embryos had heart defects. Besides, some studies showed that alterations in SUMO are associated with heart failure and congenital heart defects. Previously, the connection between SUMO and gene expression was not fully understood. Now Dovichi's study provided clues to this connection.
TDovichi's team inhibited SUMO activity in the developing cardiovascular tissue, and identified three predominate heart defects in the SUMO-deficient hearts, indicating that restoring the function of SUMO may be a way to prevent congenital heart defects. In the next step, the team will study the function of SUMO in other aspects of development. Understanding why development defects occur would help find an approach to prevent them.
The SUMO proteins have something in common with ubiquitin. But SUMO is not used to tag proteins for degradation. The covalent attachment of a SUMO to substrate protein is a process known as sumoylation. Sumoylation is critical to many different biological processes such as nuclear-cytosolic transport, transcriptional regulation, protein stability and apoptosis. (By the way, Cusabio help you do your research by offering high quality proteins and antibodies including SUMO and polyclonal antibody.)