TY  - GEN
AB  - Sensory adaptation in inner ear hair cells depends on myosin‑1c (Myo1c), the molecular motor that regulates mechanotransduction channel sensitivity. This dissertation examines how protein kinase A (PKA) phosphorylation modulates Myo1c function. We demonstrate that Myo1c can be phosphorylated by PKA at serine 701 (S701) under specific calcium and calmodulin-dependent conditions, though phosphorylation is inefficient in cells. Mutations at S701 significantly alter ATPase activity, actin translocation velocity, and force production, indicating a critical role for this site in motor mechanics. Additional in vitro studies suggest that Myo1c tail domains contribute to efficient motility and force generation. Together, these findings reveal complex regulatory mechanisms controlling Myo1c activity and support a role for PKA signaling in hair cell adaptation.
AD  - Oregon Health and Science University
AU  - Miller, Emilie
DA  - 2007
DO  - 10.6083/M46T0JK6
DO  - DOI
ED  - Gillespie, Peter
ED  - Mentor
ID  - 184
KW  - Phosphorylation
KW  - Medicine
KW  - Myosins
KW  - Hair Cells, Auditory
KW  - Protein Serine-Threonine Kinases
KW  - Cyclic AMP-Dependent Protein Kinases
KW  - Ear, Inner
KW  - pka
L1  - https://digitalcollections.ohsu.edu/record/184/files/184_etd.pdf
L2  - https://digitalcollections.ohsu.edu/record/184/files/184_etd.pdf
L4  - https://digitalcollections.ohsu.edu/record/184/files/184_etd.pdf
LK  - https://digitalcollections.ohsu.edu/record/184/files/184_etd.pdf
N2  - Sensory adaptation in inner ear hair cells depends on myosin‑1c (Myo1c), the molecular motor that regulates mechanotransduction channel sensitivity. This dissertation examines how protein kinase A (PKA) phosphorylation modulates Myo1c function. We demonstrate that Myo1c can be phosphorylated by PKA at serine 701 (S701) under specific calcium and calmodulin-dependent conditions, though phosphorylation is inefficient in cells. Mutations at S701 significantly alter ATPase activity, actin translocation velocity, and force production, indicating a critical role for this site in motor mechanics. Additional in vitro studies suggest that Myo1c tail domains contribute to efficient motility and force generation. Together, these findings reveal complex regulatory mechanisms controlling Myo1c activity and support a role for PKA signaling in hair cell adaptation.
PB  - Oregon Health and Science University
PY  - 2007
T1  - Phosphorylation of myosin-1c by cAMP-dependent protein kinase
TI  - Phosphorylation of myosin-1c by cAMP-dependent protein kinase
UR  - https://digitalcollections.ohsu.edu/record/184/files/184_etd.pdf
Y1  - 2007
ER  -