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.

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Apr 23rd, 1:00 PM Apr 23rd, 3:00 PM

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