Event Title
Phosphorylation of the Actin Binding Protein Cortactin by Aurora Kinase
Faculty Sponsor
Anne Kruchten
Location
Jereld R. Nicholson Library
Date
5-13-2011 3:00 PM
End Date
5-13-2011 4:30 PM
Subject Area
Molecular Biology/Biochemistry
Description
Cortactin is an actin binding protein that is integral to the formation of lamellipodia and invadopodia, both of which are structures that allow cells to be motile. Previous studies have shown that cortactin is upregulated in breast, head and neck tumors, and phosphorylated on multiple sites by Src and ERK kinases. It was hypothesized that Aurora kinase phosphorylates cortactin on serine 348. To test this, serine 348 was mutated into alanine 348, to eliminate the phosphorylation site, and aspartate 348, to mimic the negative charge when phosphorylated. The two mutants were synthesized on different vectors each intended for study in bacterial and mammalian cells. This work was funded by a Medical Research Foundation Grant, a Linfield Faculty Student Collaborative Research Grant, and start-up funds from the M.J. Murdock Charitable Trust.
Recommended Citation
Frank, John; Baker, Kathryn; Hastings, Bonnie; and Wilder, Jannell, "Phosphorylation of the Actin Binding Protein Cortactin by Aurora Kinase" (2011). Science and Social Sciences. Event. Submission 16.
https://digitalcommons.linfield.edu/studsymp_sci/2011/all/16
Phosphorylation of the Actin Binding Protein Cortactin by Aurora Kinase
Jereld R. Nicholson Library
Cortactin is an actin binding protein that is integral to the formation of lamellipodia and invadopodia, both of which are structures that allow cells to be motile. Previous studies have shown that cortactin is upregulated in breast, head and neck tumors, and phosphorylated on multiple sites by Src and ERK kinases. It was hypothesized that Aurora kinase phosphorylates cortactin on serine 348. To test this, serine 348 was mutated into alanine 348, to eliminate the phosphorylation site, and aspartate 348, to mimic the negative charge when phosphorylated. The two mutants were synthesized on different vectors each intended for study in bacterial and mammalian cells. This work was funded by a Medical Research Foundation Grant, a Linfield Faculty Student Collaborative Research Grant, and start-up funds from the M.J. Murdock Charitable Trust.