Event Title
Identifying an Atypical Actin Binding Domain in the Fission Yeast Mid1 Scaffold
Presentation Type
Poster/Portfolio
Presenter Major(s)
Cell and Molecular Biology, Chemistry
Mentor Information
Dawn Clifford Hart, hartdaw@gvsu.edu
Department
Cell and Molecular Biology
Location
Henry Hall Atrium 75
Start Date
13-4-2011 1:00 PM
End Date
13-4-2011 2:00 PM
Keywords
Health, Illness, and Healing, Life Science
Abstract
The scaffolding protein Mid1, found in the fission yeast S. pombe, functions in the assembly and placement of the actin contractile ring, which is required for cell division. The placement and functionality of the division septum corresponds to the placement of the ring. Therefore, identifying contractile ring proteins that directly associate with Mid1 will contribute to our understanding of proper cell division and equal transfer of the cellular contents. Our preliminary results suggest that Mid1 contributes to the formation and placement of the actin contractile ring through direct association with F-Actin filaments. The main goals of this research project are to identify the actin binding domain in Mid1 and analyze the consequence of disrupting the interaction. To test this, we are using actin cosedimentation assays. After identifying the actin binding region within Mid1, mutants with alterations to the actin binding region will be generated and analyzed for cell division defects.
Identifying an Atypical Actin Binding Domain in the Fission Yeast Mid1 Scaffold
Henry Hall Atrium 75
The scaffolding protein Mid1, found in the fission yeast S. pombe, functions in the assembly and placement of the actin contractile ring, which is required for cell division. The placement and functionality of the division septum corresponds to the placement of the ring. Therefore, identifying contractile ring proteins that directly associate with Mid1 will contribute to our understanding of proper cell division and equal transfer of the cellular contents. Our preliminary results suggest that Mid1 contributes to the formation and placement of the actin contractile ring through direct association with F-Actin filaments. The main goals of this research project are to identify the actin binding domain in Mid1 and analyze the consequence of disrupting the interaction. To test this, we are using actin cosedimentation assays. After identifying the actin binding region within Mid1, mutants with alterations to the actin binding region will be generated and analyzed for cell division defects.