Cyclin-dependent kinases (CDKs) are protein kinases regulated by cyclin subunits and are a popular target for cancer therapeutics due to the important role they play in the cell cycle. CDK16 is activated by cyclin Y and is a vital regulator of neuronal cell proliferation, brain development, neuronal migration, dendrite development, neurite outgrowth, and spermatogenesis. Garwain et al. (2018) identified Phospholipase Cβ1 (PLCβ1), a G-protein regulated enzyme important for cell differentiation, as an inhibitor of CDK16 activity. This interaction prevents uncontrolled cell growth. Our study sought to understand the mechanism through which PLCβ1 inhibits CDK16. Our approach is to express the proteins in cells and isolate the complex through immunoprecipitation. We were able to make complexes at high enough concentrations for structure resolution by cryo-EM where purity was confirmed by mass spectroscopy. We are currently assessing CDK16 kinase activity using a FRET-based commercial assay.​

• This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

Creator

• Case, Kallie

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-042524-131209
• 121715

Keyword

• CDK16
• Protein-protein Interactions
• PLCb1

Advisor

• Scarlata, Suzanne Frances

Year

• 2024

Date created

• 2024-04-25

Resource type

• Major Qualifying Project

Major

• Biochemistry

Source

• E-project-042524-131209

Rights statement

• In Copyright