Structural, Kinetic and Functional Properties of CAP1/AC Complexes
dc.contributor.author | Mehrotra, Simran | |
dc.date.accessioned | 2017-03-14T12:22:58Z | |
dc.date.available | 2017-03-14T12:22:58Z | |
dc.date.issued | 2017-03 | |
dc.identifier.uri | http://hdl.handle.net/10675.2/621348 | |
dc.description | Poster presented at the 18th Annual Phi Kappa Phi Student Research and Fine Arts Conference | en |
dc.description.abstract | The major cause of death in pancreatic cancer is due to metastases; therefore, it is important to study the mechanism by which the pancreatic cancer cells migrate and invade. This would help advance therapeutics and ultimately help prolong survival. Adenylyl cyclase-associated protein 1 (CAP1) is a scaffold protein that is involved in the regulation of actin microfilament formation, which ultimately leads to cell migration and invasion. CAP1 binds to G-actin inhibiting polymerization. We first tested whether CAP1 binds to adenylyl cyclase (AC) by performing co-immunoprecipitation. We found that CAP1 not only interacts with G-actin, but also with a number of AC isoforms: AC1, AC3, AC4 and AC7. Further studies need to be done to determine how CAP1/AC/G-actin interact and the impact of these interactions on the invasive behavior of pancreatic cancer cells. | |
dc.description.sponsorship | Augusta University Scholarly Activity Award | en |
dc.language.iso | en | en |
dc.subject | Pancreatic Neoplasms | en |
dc.subject | Adenylyl Cyclases | en |
dc.subject | Immunoprecipitation | en |
dc.title | Structural, Kinetic and Functional Properties of CAP1/AC Complexes | en |
dc.type | Other | en |
dc.contributor.department | Department of Biological Sciences | en |
refterms.dateFOA | 2019-04-10T08:24:53Z | |
html.description.abstract | The major cause of death in pancreatic cancer is due to metastases; therefore, it is important to study the mechanism by which the pancreatic cancer cells migrate and invade. This would help advance therapeutics and ultimately help prolong survival. Adenylyl cyclase-associated protein 1 (CAP1) is a scaffold protein that is involved in the regulation of actin microfilament formation, which ultimately leads to cell migration and invasion. CAP1 binds to G-actin inhibiting polymerization. We first tested whether CAP1 binds to adenylyl cyclase (AC) by performing co-immunoprecipitation. We found that CAP1 not only interacts with G-actin, but also with a number of AC isoforms: AC1, AC3, AC4 and AC7. Further studies need to be done to determine how CAP1/AC/G-actin interact and the impact of these interactions on the invasive behavior of pancreatic cancer cells. |