Off-campus UMass Amherst users: To download campus access dissertations, please use the following link to log into our proxy server with your UMass Amherst user name and password.
Non-UMass Amherst users: Please talk to your librarian about requesting this dissertation through interlibrary loan.
Dissertations that have an embargo placed on them will not be available to anyone until the embargo expires.
Author ORCID Identifier
Open Access Dissertation
Doctor of Philosophy (PhD)
Molecular and Cellular Biology
Year Degree Awarded
Month Degree Awarded
Biochemistry | Biophysics | Molecular Biology
Long-term memory and learning are still poorly understood from a molecular and cellular standpoint. Ca2+/calmodulin-dependent protein kinase II (CaMKII) is an oligomeric kinase that is involved in this remarkable process. However, the molecular details of its specific roles in these processes remains elusive. CaMKII activation-triggered subunit exchange presents a novel possible mechanism involved in long-term memory and learning by exchanging active subunits with other CaMKIIs. CaMKII subunit exchange also shows that exchanged CaMKIIs spread their phosphorylation state to newly synthesized CaMKIIs. This provides a long-lasting signal that might possibly be involved in long-term memory by escaping a cell’s protein turnover. In this thesis work, I expanded understanding of CaMKII activation-triggered subunit exchange to the other CaMKII human genes, CaMKIIγ and CaMKIIδ. I also characterized CaMKIIα holoenzyme stability. I also uncovered a potential new role for CaMKII oligomerization and how it is related to activation properties. Lastly, I used CaMKII FRET biosensor Camui for a proof of concept using microscopy technology FLIM-FRET.
Torres-Ocampo, Ana P., "Understanding how CaMKII holoenzyme dynamics facilities activation-triggered subunit exchange" (2021). Doctoral Dissertations. 2371.
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.
Available for download on Thursday, September 01, 2022