What are post-translational modifications?
Humans are believed to have more than one million proteins in their body despite having only about 20,000-25,000 genes [1]. This indicates that any one gene can code for more than one protein. These proteins are further customized by a process known as post-translational modifications, or PTMs, which are chemical in nature. PTMs are important because they can impact localization, activity, and interactions of proteins. PTMs may take place immediately following translation, or it may happen at a later step in the "life cycle of a protein," such as following localization [1]. Ultimately, PTMs can have important implications on disease biology and treatments, so they prove to be an essential area of study [1].
Figure 1. Depicts different types of PTMs that can affect a protein.
Post-translational modifications of GBA1
Phosphorylation is a common type of post-translational modification that may occur on serines, threonines, or tyrosines. Phosphorylation is involved in signaling and maintaining protein function [2]. NetPhos 3.1, a resource put forward by DTU Health Tech, provides information about phosphorylation patterns in GBA1, as seen here:
Figure 2. Represents the post-translational modifications found in GBA1 in humans.
Figure 3. Shows the post-translational modifications found in the GBA1 homolog in zebrafish.
Discussion
It is important to identify Serine sites of GBA1 that are susceptible to phosphorylation, as well as Serine sites in GBA1 that are conserved. Mutations at these amino acid sites indicate the possibility of disruption to phosphorylation, which would likely have a negative impact on an organism. Additionally, DTU health tech serves as a great resource to compare post translational modification sites between different organisms. Using MEGA, conserved Serine sites in GBA1 in humans can be identified. The corresponding sites in zebrafish can be found using DTU health tech.
References
1. Overview of post-translational modifications (PTMs). ThermoFisher Scientific. (n.d.). https://www.thermofisher.com/us/en/home/life-science/protein-biology/protein-biology-learning-center/protein-biology-resource-library/pierce-protein-methods/overview-post-translational-modification.html
2. Phosphorylation. Thermo Fisher Scientific - US. (n.d.). Retrieved April 19, 2023, from https://www.thermofisher.com/us/en/home/life-science/protein-biology/protein-biology-learning-center/protein-biology-resource-library/pierce-protein-methods/phosphorylation.html#:~:text=Phosphorylation%20regulates%20protein%20function%20and,catalytic%20activity%20of%20the%20protein
2. Phosphorylation. Thermo Fisher Scientific - US. (n.d.). Retrieved April 19, 2023, from https://www.thermofisher.com/us/en/home/life-science/protein-biology/protein-biology-learning-center/protein-biology-resource-library/pierce-protein-methods/phosphorylation.html#:~:text=Phosphorylation%20regulates%20protein%20function%20and,catalytic%20activity%20of%20the%20protein
Links to Images
Cover Image: https://www.nature.com/articles/s41579-019-0243-0
Figure 1: https://www.creative-proteomics.com/blog/index.php/strategies-for-post-translational-modifications-ptms/
Figure 2: https://services.healthtech.dtu.dk/services/NetPhos-3.1/
Figure 3: https://services.healthtech.dtu.dk/services/NetPhos-3.1/
Figure 1: https://www.creative-proteomics.com/blog/index.php/strategies-for-post-translational-modifications-ptms/
Figure 2: https://services.healthtech.dtu.dk/services/NetPhos-3.1/
Figure 3: https://services.healthtech.dtu.dk/services/NetPhos-3.1/