![2021 Undergraduate Research Showcase](../../assets/md5images/6fbf71b6f53e89cfbc8b1deb6f56b3f6.png)
Document Type
Student Presentation
Presentation Date
4-23-2021
Faculty Sponsor
Allan Albig
Abstract
The Notch signaling pathway plays important roles in developmental biology, Immune system, vascular system and variety of other systems. There is a great need to research more on how this pathway functions. The notch receptors located on the cell surface are activated when it interacts with a ligand that leads to the release of the Notch intracellular domain(NICD) that then translocate to the nucleolus and begins transcription. There are four notch proteins(NICDs) that contain an important Ankyrin domain for NICD homodimerization. The notch 4(NICD) is quite different in structure and how it performs compared to the rest of the group of notches and in published research performed by crow and Albig it was observed that notch4 (N4ICD) displayed a stronger dimerization activity. It is hypothesized that because it is disparate that it is able to dimerize far better than the other notches. Data collected from Crow and Albig found a site where 1-3 NICDs notches coded for a similar amino acid and N4ICD presented a different one. It was speculated that by converting the amino acid to the same one the other NICDs coded that it will convey if there is relation to its dimerization activity strength.
Recommended Citation
Marquez, Monik and Albig, Allan, "Notch Mutation Effects on NICD Molecules Dimerization" (2021). 2021 Undergraduate Research Showcase. 68.
https://scholarworks.boisestate.edu/under_showcase_2021/68