The role of 4.1G phosphorylation in PKA mediated signaling and migration of SKOV3 ovarian cancer cells
Hurley, Julia M
Hurley, Julia M
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Abstract
Protein kinase A (PKA) is a serine-threonine kinase that regulates several cellular processes including proliferation and migration by phosphorylating downstream substrates. Our research has identified a novel PKA-mediated phosphorylation site at serine 529 on protein 4.1G. Protein 4.1 family members are membrane-cytoskeletal adaptor proteins. The overall goal of this study is to determine whether phosphorylation of 4.1G by PKA influences cytoskeletal events and cell migration. Towards this end, by employing CRISPR/Cas9 technology and site directed mutagenesis, we developed a tissue culture reconstitution system that will allow us to compare the wildtype 4.1G protein and a non-phosphorylatable 4.1G mutant (S529A).
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Date
2022-01-01
Student Status
Undergraduate
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virtual-oral-presentation
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Microbiology and Molecular Genetics
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College of Agriculture and Life Sciences
Patrick Leahy Honors College
Patrick Leahy Honors College
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Biological Sciences