Event Title
Identification of Unique C-Terminus Binding Proteins of CP β1 and β2 Isoforms
Location
CSU 255
Start Date
25-4-2005 1:15 PM
End Date
25-4-2005 3:15 PM
Student's Major
Biological Sciences
Student's College
Science, Engineering and Technology
Mentor's Name
Marilyn Hart
Mentor's Department
Biological Sciences
Mentor's College
Science, Engineering and Technology
Description
Actin capping protein (CP), a heterodimer composed of α and β subunits, binds the barbed ends of actin filaments and regulates actin's specific binding affinities. Three isoforms of the β subunits (βi, β2, and β3), each encoded by the same gene, have been identified. Post transcriptional modification of the β subunit gene is responsible for variation in the C terminus of the protein. Although the N terminus of the CP β subunit is necessary for binding actin, the role of the variable C terminus remains undefined. Prior research, performed by the primary investigator of my studies, suggests that the β1 isoform of CP is necessary for attaching actin filaments to the Z-line of myocardium, and the β2 isoform organizes actin at the intercalated discs of myocardium. These findings suggest that CP is necessary for proper heart function and, accordingly, CP becomes a suspect in the causation of heart disease. We hypothesize that CP β1 and β2 interact with unique proteins at their C terminus and these interactions define their different roles in the organization of actin filaments in myocardium. Novel protein interactions with the β1 and β2 isoforms are currently being explored using Glutathione S-Transferase (GST) pulldown analysis. The gene encoding the β1 and β2 proteins has been inserted into the expression vector pGEX-lX, allowing the generation of GST-β1 and GST-P2 fusion proteins. The fusion protein is currently being used to bind proteins interacting with the C terminus of β subunits using GST as a means of isolation.
Identification of Unique C-Terminus Binding Proteins of CP β1 and β2 Isoforms
CSU 255
Actin capping protein (CP), a heterodimer composed of α and β subunits, binds the barbed ends of actin filaments and regulates actin's specific binding affinities. Three isoforms of the β subunits (βi, β2, and β3), each encoded by the same gene, have been identified. Post transcriptional modification of the β subunit gene is responsible for variation in the C terminus of the protein. Although the N terminus of the CP β subunit is necessary for binding actin, the role of the variable C terminus remains undefined. Prior research, performed by the primary investigator of my studies, suggests that the β1 isoform of CP is necessary for attaching actin filaments to the Z-line of myocardium, and the β2 isoform organizes actin at the intercalated discs of myocardium. These findings suggest that CP is necessary for proper heart function and, accordingly, CP becomes a suspect in the causation of heart disease. We hypothesize that CP β1 and β2 interact with unique proteins at their C terminus and these interactions define their different roles in the organization of actin filaments in myocardium. Novel protein interactions with the β1 and β2 isoforms are currently being explored using Glutathione S-Transferase (GST) pulldown analysis. The gene encoding the β1 and β2 proteins has been inserted into the expression vector pGEX-lX, allowing the generation of GST-β1 and GST-P2 fusion proteins. The fusion protein is currently being used to bind proteins interacting with the C terminus of β subunits using GST as a means of isolation.
Recommended Citation
Sullivan, Steve. "Identification of Unique C-Terminus Binding Proteins of CP β1 and β2 Isoforms." Undergraduate Research Symposium, Mankato, MN, April 25, 2005.
https://cornerstone.lib.mnsu.edu/urs/2005/poster-session-B/3
