TY  - GEN
AB  - Potassium channels regulate a diverse array of physiological processes, including key aspects of learning and memory. Small-conductance calcium-activated potassium (SK or KCa2) channels are voltage-insensitive K channels that are gated solely by intracellular Ca2+. Functional SK channels are formed through heteromeric complexes of [alpha]-pore-forming subunits and CaM, with which they are constitutively associated. Previous work using a proteomics approach demonstrated that SK2 channels bind protein kinase CK2 (CK2) and protein phosphate 2A (PP2A) to form a macromolecular complex, and that CK2 phosphatase 2A (PP2A) to form a macromolecular complex, and that CK2 phosphorylation of SK2-bound calmodulin (CaM) on threonine 80 (T80) decreases SK channel Ca2+ sensitivity by destabilizing the open state of the channel. The work detailed in this thesis extends these initial findings.
AD  - Oregon Health and Science University
AU  - Allen, Duane
DA  - 2008-04-01
DO  - 10.6083/M45M64FB
DO  - DOI
ED  - Adelman, John
ED  - Advisor
ID  - 2760
KW  - Calcium, Dietary
KW  - Potassium Channels
L1  - https://digitalcollections.ohsu.edu/record/2760/files/3528_etd.pdf
L2  - https://digitalcollections.ohsu.edu/record/2760/files/3528_etd.pdf
L4  - https://digitalcollections.ohsu.edu/record/2760/files/3528_etd.pdf
LK  - https://digitalcollections.ohsu.edu/record/2760/files/3528_etd.pdf
N2  - Potassium channels regulate a diverse array of physiological processes, including key aspects of learning and memory. Small-conductance calcium-activated potassium (SK or KCa2) channels are voltage-insensitive K channels that are gated solely by intracellular Ca2+. Functional SK channels are formed through heteromeric complexes of [alpha]-pore-forming subunits and CaM, with which they are constitutively associated. Previous work using a proteomics approach demonstrated that SK2 channels bind protein kinase CK2 (CK2) and protein phosphate 2A (PP2A) to form a macromolecular complex, and that CK2 phosphatase 2A (PP2A) to form a macromolecular complex, and that CK2 phosphorylation of SK2-bound calmodulin (CaM) on threonine 80 (T80) decreases SK channel Ca2+ sensitivity by destabilizing the open state of the channel. The work detailed in this thesis extends these initial findings.
PY  - 2008-04-01
T1  - The organization and regulation of small conductance [calcium] activated K channel (KCNN2) multiprotein complexes
TI  - The organization and regulation of small conductance [calcium] activated K channel (KCNN2) multiprotein complexes
UR  - https://digitalcollections.ohsu.edu/record/2760/files/3528_etd.pdf
Y1  - 2008-04-01
ER  -