The mammalian body is made up of proteins, lipids and water, with proteins making up 42 % of the total dry mass of a human body. Therefore, protein synthesis is a key process for the body. The biosynthetic pathway begins with amino acid chains in the Endoplasmic Reticulum (ER). They are modified, folded and then packaged into transport carriers at the ER Exit Site (ERES), transporting them to the Golgi for further modification. From there they are packaged into post-Golgi carriers to deliver the fully folded proteins to their destination, either inside the cell, or to the plasma membrane where they remain, or they are secreted into the extracellular space. Thus, efficient protein synthesis and transport is a key process to maintain homeostasis.
When it is lost, it can cause many common and varied diseases. The process is highly regulated to quickly meet the needs of the cell and the body, for example, increase in secretion of insulin in response to glucose, or increase in collagen secretion during postnatal growth, and also to ensure that no improperly made proteins are distributed throughout the cell.
When this goes wrong, it can be the cause of diseases such as fibrosis which is caused by excessive protein production, or osteogenesis imperfecta which is caused by a mutation in one of the ERES proteins.
Alison’s research group studies how different compounds can be used to modify the efficiency of the protein trafficking process, and how this will affect the normal balance within the cell.