Identification of Proteins that Interact with Actin Capping Protein
Location
CSU 253/4/5
Start Date
23-4-2007 1:00 PM
End Date
23-4-2007 3:00 PM
Student's Major
Biological Sciences
Student's College
Science, Engineering and Technology
Mentor's Name
Marilyn C. Hart
Mentor's Department
Biological Sciences
Mentor's College
Science, Engineering and Technology
Description
Actin, a component of all eukaryotic cells, plays an important role in maintaining cell structure and contributes to cell motility. Actin is regulated by a variety of accessory proteins including actin capping protein (CP). CP attaches to the barbed end of actin filaments regulating length and stability. CP is composed of two subunits, an alpha (a) and a beta (p) subunit. In vertebrates, three alpha isoforms (al, a2, a3) and three beta isoforms (pi, p2, p3) have been identified. The pi isoform is the predominant isoform of muscle, whereas the P2 isoform is the predominant isoform of nonmuscle. Previous transgenic studies indicate that pi and p2 are functionally distinct in murine myocardium and might interact with novel proteins. We are using a yeast two hybrid genetic screen to identify proteins that interact with pi and p2. We have generated the appropriate constructs, confirmed their orientation, and expression. We have also amplified a mouse embryonic cDNA library. The screen is ongoing.
Identification of Proteins that Interact with Actin Capping Protein
CSU 253/4/5
Actin, a component of all eukaryotic cells, plays an important role in maintaining cell structure and contributes to cell motility. Actin is regulated by a variety of accessory proteins including actin capping protein (CP). CP attaches to the barbed end of actin filaments regulating length and stability. CP is composed of two subunits, an alpha (a) and a beta (p) subunit. In vertebrates, three alpha isoforms (al, a2, a3) and three beta isoforms (pi, p2, p3) have been identified. The pi isoform is the predominant isoform of muscle, whereas the P2 isoform is the predominant isoform of nonmuscle. Previous transgenic studies indicate that pi and p2 are functionally distinct in murine myocardium and might interact with novel proteins. We are using a yeast two hybrid genetic screen to identify proteins that interact with pi and p2. We have generated the appropriate constructs, confirmed their orientation, and expression. We have also amplified a mouse embryonic cDNA library. The screen is ongoing.
Recommended Citation
Strehler, Kevin Y. E. and Nathan M. Martinez. "Identification of Proteins that Interact with Actin Capping Protein." Undergraduate Research Symposium, Mankato, MN, April 23, 2007.
https://cornerstone.lib.mnsu.edu/urs/2007/poster-session-A/3
