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Author ORCID Identifier
https://orcid.org/0000-0003-1223-7120
AccessType
Open Access Dissertation
Document Type
dissertation
Degree Name
Doctor of Philosophy (PhD)
Degree Program
Molecular and Cellular Biology
Year Degree Awarded
2021
Month Degree Awarded
September
First Advisor
Margaret Stratton
Second Advisor
Scott Garman
Third Advisor
Peter Chien
Fourth Advisor
Luke Chao
Subject Categories
Biochemistry | Biophysics | Molecular Biology
Abstract
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.
DOI
https://doi.org/10.7275/24533941
Recommended Citation
Torres-Ocampo, Ana P., "Understanding how CaMKII holoenzyme dynamics facilities activation-triggered subunit exchange" (2021). Doctoral Dissertations. 2371.
https://doi.org/10.7275/24533941
https://scholarworks.umass.edu/dissertations_2/2371
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.